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-JUL-2019, entry version 4.
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}.
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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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000265160};
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
//