ID KCY_METVS Reviewed; 174 AA. AC A6USC1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 03-AUG-2022, entry version 73. DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00239}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_00239}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00239}; DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00239}; DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00239}; GN Name=cmk {ECO:0000255|HAMAP-Rule:MF_00239}; OrderedLocusNames=Mevan_1499; OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 OS / SB). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=406327; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus vannielii SB."; RL Submitted (JUN-2007) 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:0000255|HAMAP- CC Rule:MF_00239}; 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_00239}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00239}. CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00239}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000742; ABR55393.1; -; Genomic_DNA. DR RefSeq; WP_012066307.1; NC_009634.1. DR AlphaFoldDB; A6USC1; -. DR SMR; A6USC1; -. DR STRING; 406327.Mevan_1499; -. DR EnsemblBacteria; ABR55393; ABR55393; Mevan_1499. DR GeneID; 5325171; -. DR KEGG; mvn:Mevan_1499; -. DR eggNOG; arCOG01037; Archaea. DR HOGENOM; CLU_079959_1_0_2; -. DR OMA; FIFRDMA; -. DR OrthoDB; 110333at2157; -. DR Proteomes; UP000001107; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00239; Cytidyl_kinase_type2; 1. DR InterPro; IPR011892; Cyt_kin_arch. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02173; cyt_kin_arch; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1..174 FT /note="Cytidylate kinase" FT /id="PRO_1000005681" FT BINDING 7..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00239" SQ SEQUENCE 174 AA; 19713 MW; 01C8BF8DC33DA26E CRC64; MIITIGGLPG TGTTTISKLL SEKYGLSHVC AGFIFRDMAK ENNMTLQEFS NYAEKNSGVD NEIDRRQVEA AKSGNLILEG RLAGWILKKN DMVPDLSIWL KADPMVRCKR ISEREHENVD LALEKMLLRE ASEKKRYKEI YNIEIDDLSI YDLVIESSKW GATGVFNIIE KAIK //