(data stored in SCRATCH3701 zone)

SWISSPROT: KCY_RICTY

ID   KCY_RICTY               Reviewed;         219 AA.
AC   Q68WL3;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 78.
DE   RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=RT0509;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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:0000255|HAMAP-
CC         Rule:MF_00238};
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:0000255|HAMAP-
CC         Rule:MF_00238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00238}.
DR   EMBL; AE017197; AAU03979.1; -; Genomic_DNA.
DR   RefSeq; WP_011190960.1; NC_006142.1.
DR   SMR; Q68WL3; -.
DR   STRING; 257363.RT0509; -.
DR   EnsemblBacteria; AAU03979; AAU03979; RT0509.
DR   KEGG; rty:RT0509; -.
DR   eggNOG; ENOG4105CAT; Bacteria.
DR   eggNOG; COG0283; LUCA.
DR   HOGENOM; HOG000242849; -.
DR   KO; K00945; -.
DR   OMA; LKIFMTA; -.
DR   OrthoDB; 776861at2; -.
DR   BioCyc; RTYP257363:G1G0L-516-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68WL3.
DR   SWISS-2DPAGE; Q68WL3.
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..219
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_0000131967"
FT   NP_BIND         21..29
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   219 AA;  24348 MW;  4B6D963183883660 CRC64;
     MVDLKTKAFD IAQNFTISLD GPAASGKGTI GLILAKKFAL KYFQSSIVYR QLAFNCIHQQ
     IDITDIDAVI ALSQELKLDN NIDLENEDIG DIASKIAVIS EVRNNLNHNL INLVKTTPRI
     IMEGRDIGTV VAPDADLKIF ITASPYVRAV RRYNQLQAKG KTCILDEIIQ QIILRDKRDK
     ERKVGPLLPA LGAFIIDTSK LSAIEVVEEV TNYIKNKIT
//

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