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Database: UniProt
Entry: A0A0A0WXA0_9SPIO
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ID   A0A0A0WXA0_9SPIO        Unreviewed;       801 AA.
AC   A0A0A0WXA0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   10-APR-2019, entry version 25.
DE   RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN   ORFNames=JO41_02685 {ECO:0000313|EMBL:AIW88838.1};
OS   Treponema sp. OMZ 838.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=1539298 {ECO:0000313|EMBL:AIW88838.1, ECO:0000313|Proteomes:UP000030314};
RN   [1] {ECO:0000313|EMBL:AIW88838.1, ECO:0000313|Proteomes:UP000030314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OMZ 838 {ECO:0000313|EMBL:AIW88838.1,
RC   ECO:0000313|Proteomes:UP000030314};
RA   Chan Y., Ma A.P.Y., Lacap D.C., Huo Y.-B., Leung F.C., Watt R.M.;
RT   "Complete genome sequence for Treponema sp. OMZ 838 (ATCC 700772, DSM
RT   16789) isolated from a necrotizing ulcerative gingivitis lesion.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238,
CC       ECO:0000256|SAAS:SAAS01150963}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00238,
CC       ECO:0000256|SAAS:SAAS01150955}.
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DR   EMBL; CP009227; AIW88838.1; -; Genomic_DNA.
DR   RefSeq; WP_044013625.1; NZ_CP009227.1.
DR   STRING; 1539298.JO41_02685; -.
DR   EnsemblBacteria; AIW88838; AIW88838; JO41_02685.
DR   KEGG; trm:JO41_02685; -.
DR   KO; K02945; -.
DR   OrthoDB; 1235756at2; -.
DR   Proteomes; UP000030314; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd02020; CMPK; 1.
DR   HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000110; Ribosomal_S1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   Pfam; PF00575; S1; 5.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; SSF50249; 6.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
DR   TIGRFAMs; TIGR00717; rpsA; 1.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00238,
KW   ECO:0000256|SAAS:SAAS01150973}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030314};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238,
KW   ECO:0000256|SAAS:SAAS01150960};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00238,
KW   ECO:0000256|SAAS:SAAS01150975};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00238,
KW   ECO:0000256|SAAS:SAAS01150957};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030314};
KW   Ribonucleoprotein {ECO:0000313|EMBL:AIW88838.1};
KW   Ribosomal protein {ECO:0000313|EMBL:AIW88838.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00238,
KW   ECO:0000256|SAAS:SAAS01150965}.
FT   DOMAIN      260    321       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      339    411       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      432    500       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      517    587       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      604    674       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      691    763       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   NP_BIND       7     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00238}.
FT   COILED      318    338       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   801 AA;  89322 MW;  A654DF7EC811BD60 CRC64;
     MIIAIDGPAG SGKSTVAKMI AADLGFTFMN TGSFYRALTL AVLRSLGGDE SGAGAEKPDL
     ENEVKWTDFA KTVSLEYKQD GMYLDGSCVE AYLRSDAVES VVAALSAIVP IRHLINKKIR
     AAAAKLNIVC EGRDMTTVVF PDAECKVYLD ASAEARARRR FEQGTSNLSE AEIRKSIEER
     DAIDRNKKEG SLKIAEDAFY LDTSDLTIMQ VCEKIKDKIH DKGLFMEQKE VAMDAVTNSD
     QSIQTQLPEE YLNFESPEVG TLKEGRIIAI TDDSVFIDVG GKSEGRVARE EFTEEPKIGD
     TVQVYIEKTE ATDGKLIISK EKADRNILRK ELQNAYRNKT PVTGVIKKLV NKSGYDVDLG
     ANMIAFLPIS QAAAQKVDKP ESLLGEKGSF YIEKMVFDRK GNRDNIVVNR RKYLEDTLEK
     NREAFFENTN IGDVVKGTVK SFTSFGAFID LGGFDGLLHI NDMSWGHVTR PKDFVKKGQE
     IDLKVIRLDP AEKRINLSLK HFTPDPWLEF EDKFQVNDIV KGHVTKITDF GAFVELSEGI
     EGLVHISEFS WVKKVSKPSD MVKIGDEVEC MILGYDIQAG RVSLGLKQVT ANPWDNIGER
     YPVGTRLTRK VVKLTNAGAF IELEEGIDGF LHVDDLSWTK RVRHPNSELE AGQELEVIVI
     ECNPAEHRVR LGVKQLSDDP WKTFAEAYKP GSTVEGEVTS VTDFGIFVKV PGDIEGLIHK
     QNLVENREDN PDEVLKKYAV GDKVKAAVLD VNVKDKKTAF SIRDYKKRLQ QEELSRYMST
     KQEDGEGAFT LGDLMKNKAS E
//
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