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Database: UniProt
Entry: A0A286XBE3_CAVPO
LinkDB: A0A286XBE3_CAVPO
Original site: A0A286XBE3_CAVPO 
ID   A0A286XBE3_CAVPO        Unreviewed;       261 AA.
AC   A0A286XBE3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Uridine-cytidine kinase {ECO:0000256|RuleBase:RU003825};
DE            EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN   Name=UCK2 {ECO:0000313|Ensembl:ENSCPOP00000022726.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000022726.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000022726.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000022726.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00000503,
CC         ECO:0000256|RuleBase:RU003825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00000734,
CC         ECO:0000256|RuleBase:RU003825};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000256|ARBA:ARBA00004784,
CC       ECO:0000256|RuleBase:RU003825}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000256|ARBA:ARBA00004690,
CC       ECO:0000256|RuleBase:RU003825}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family.
CC       {ECO:0000256|ARBA:ARBA00005408, ECO:0000256|RuleBase:RU003825}.
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DR   EMBL; AAKN02037360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02037361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003468715.1; XM_003468667.3.
DR   AlphaFoldDB; A0A286XBE3; -.
DR   STRING; 10141.ENSCPOP00000022726; -.
DR   Ensembl; ENSCPOT00000045740.1; ENSCPOP00000022726.1; ENSCPOG00000032384.1.
DR   GeneID; 100733408; -.
DR   KEGG; cpoc:100733408; -.
DR   CTD; 7371; -.
DR   VEuPathDB; HostDB:ENSCPOG00000032384; -.
DR   eggNOG; KOG4203; Eukaryota.
DR   GeneTree; ENSGT01020000230412; -.
DR   InParanoid; A0A286XBE3; -.
DR   OMA; TVKPMHE; -.
DR   OrthoDB; 180154at2759; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000032384; Expressed in zone of skin and 11 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043771; F:cytidine kinase activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   PANTHER; PTHR10285:SF131; URIDINE-CYTIDINE KINASE 2; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00988; URIDINKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003825};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003825};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT   DOMAIN          22..217
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   261 AA;  29280 MW;  20D2C24DED213AFD CRC64;
     MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YHQKQVVILS
     QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK
     EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ
     ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG
     CLNGYTPSRK RQTSESGSRP H
//
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