ID   A0A3P9BBH7_9CICH        Unreviewed;       207 AA.
AC   A0A3P9BBH7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 14.
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   ECO:0000313|Ensembl:ENSMZEP00005007136};
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; 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., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., 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 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 de
CC       novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP
CC       as phosphate acceptors. Also displays broad nucleoside diphosphate
CC       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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001331, 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 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03172};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03172};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-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 two
CC       small peripheral domains, NMPbind and LID, which undergo movements
CC       during catalysis. The LID domain closes over the site of phosphoryl
CC       transfer upon ATP binding. Assembling and dissambling the active center
CC       during each catalytic cycle provides an effective means to prevent ATP
CC       hydrolysis. {ECO:0000256|HAMAP-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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03172}.
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DR   Ensembl; ENSMZET00005007445.1; ENSMZEP00005007136.1; ENSMZEG00005005486.1.
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:0036430; F:CMP kinase activity; IEA:RHEA.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:RHEA.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; -; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03172};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03172}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03172}.
FT   REGION          144..154
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         36..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         72..74
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         104..107
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         111
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         151
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         162
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="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
//