ID A0A3P9BBH7_9CICH Unreviewed; 207 AA. AC A0A3P9BBH7; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 08-MAY-2019, entry version 3. DE RecName: Full=UMP-CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_03172}; DE AltName: Full=Deoxycytidylate kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=CK {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=dCMP kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE AltName: Full=Nucleoside-diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_03172}; DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=UMP/CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=UMP/CMPK {ECO:0000256|HAMAP-Rule:MF_03172}; GN Name=CMPK1 {ECO:0000256|HAMAP-Rule:MF_03172}; GN Synonyms=CMPK {ECO:0000256|HAMAP-Rule:MF_03172}; OS Maylandia zebra (zebra mbuna). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Haplochromini; Maylandia; OC Maylandia zebra complex. OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005007136, ECO:0000313|Proteomes:UP000265160}; RN [1] {ECO:0000313|Ensembl:ENSMZEP00005007136, ECO:0000313|Proteomes:UP000265160} RP NUCLEOTIDE SEQUENCE. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). RN [2] {ECO:0000313|Ensembl:ENSMZEP00005007136} RP IDENTIFICATION. RG Ensembl; RL Submitted (DEC-2018) to UniProtKB. CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in CC de novo pyrimidine nucleotide biosynthesis. Has preference for UMP CC and CMP as phosphate acceptors. Also displays broad nucleoside CC diphosphate kinase activity. {ECO:0000256|HAMAP-Rule:MF_03172}. 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=2.7.4.14; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; 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=2.7.4.14; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside CC 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; CC EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-Rule:MF_03172}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03172}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03172}. CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172}. Note=Predominantly CC nuclear. {ECO:0000256|HAMAP-Rule:MF_03172}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and CC two small peripheral domains, NMPbind and LID, which undergo CC movements during catalysis. The LID domain closes over the site of CC phosphoryl transfer upon ATP binding. Assembling and dissambling CC the active center during each catalytic cycle provides an CC effective means to prevent ATP hydrolysis. {ECO:0000256|HAMAP- CC Rule:MF_03172}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03172}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03172}. 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 Ensembl; ENSMZET00005007445; ENSMZEP00005007136; ENSMZEG00005005486. DR GeneTree; ENSGT00940000160589; -. DR Proteomes; UP000265160; LG18. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009041; F:uridylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01428; ADK; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006266; UMP_CMP_kinase. DR PANTHER; PTHR23359; PTHR23359; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03172}; KW Complete proteome {ECO:0000313|Proteomes:UP000265160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03172, KW ECO:0000256|RuleBase:RU003330}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03172}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03172}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03172}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03172, KW ECO:0000256|RuleBase:RU003330}. FT NP_BIND 36 41 ATP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT NP_BIND 72 74 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT NP_BIND 104 107 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT REGION 144 154 LID. {ECO:0000256|HAMAP-Rule:MF_03172}. FT BINDING 111 111 CMP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT BINDING 145 145 ATP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT BINDING 151 151 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT BINDING 162 162 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}. FT BINDING 190 190 ATP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03172}. SQ SEQUENCE 207 AA; 23363 MW; 36BC55E2CF418034 CRC64; MIGRLFGNLS QKVPSLLYRV SLVMKPQVVF VLGGPGAGKG TQCSKIVESY GYTHLEESEF GQLIANYIKE GKIVPVEITI NLLRKAMEAT MKENENKFRF LIDGFPRNED NLQGWNSVMD GKADVKFVLF FDCSNEVCIN RCLERGKSSG RTDDNRESLE KRIQTYLQST RPIIDLYEKQ GKVHTIDASR SVDEVFADVK AILDKEG //