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Database: UniProt
Entry: A0A8C4H5F7_DICLA
LinkDB: A0A8C4H5F7_DICLA
Original site: A0A8C4H5F7_DICLA 
ID   A0A8C4H5F7_DICLA        Unreviewed;       530 AA.
AC   A0A8C4H5F7;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 2.
DT   28-JAN-2026, entry version 20.
DE   RecName: Full=Uridine-cytidine kinase {ECO:0000256|RuleBase:RU003825};
DE            EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN   Name=si:ch211-243j20.2 {ECO:0000313|Ensembl:ENSDLAP00005037437.2};
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489 {ECO:0000313|Ensembl:ENSDLAP00005037437.2, ECO:0000313|Proteomes:UP000694389};
RN   [1] {ECO:0000313|Ensembl:ENSDLAP00005037437.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDLAP00005037437.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- FUNCTION: May contribute to UTP accumulation needed for blast
CC       transformation and proliferation. {ECO:0000256|ARBA:ARBA00056790}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + ATP = CMP + ADP + 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:ARBA00047436,
CC         ECO:0000256|RuleBase:RU003825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine + ATP = UMP + ADP + H(+); 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:ARBA00048909,
CC         ECO:0000256|RuleBase:RU003825};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {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: Interacts with RNF19B. {ECO:0000256|ARBA:ARBA00065923}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family.
CC       {ECO:0000256|ARBA:ARBA00005408, ECO:0000256|RuleBase:RU003825}.
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DR   AlphaFoldDB; A0A8C4H5F7; -.
DR   Ensembl; ENSDLAT00005039954.2; ENSDLAP00005037437.2; ENSDLAG00005016520.2.
DR   GeneTree; ENSGT01020000230412; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000694389; Unassembled WGS sequence.
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:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   CDD; cd02023; UMPK; 1.
DR   FunFam; 3.40.50.2020:FF:000010; Uridine-cytidine kinase; 1.
DR   FunFam; 3.40.50.300:FF:000200; Uridine-cytidine kinase; 1.
DR   Gene3D; 3.40.50.2020; -; 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; IPR029057; PRTase-like.
DR   InterPro; IPR000836; PRTase_dom.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   NCBIfam; NF001097; PRK00129.1; 1.
DR   NCBIfam; NF004018; PRK05480.1; 1.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   Pfam; PF00485; PRK; 1.
DR   Pfam; PF14681; UPRTase; 1.
DR   PRINTS; PR00988; URIDINKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003825};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003825};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003825}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694389};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          76..263
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   DOMAIN          312..515
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14681"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  59451 MW;  22D4EAC230051573 CRC64;
     NHTDSRDLTS GDDSLDGLSN RVPRCPLTPS LSPQKRTTSQ SKTEPPLLRT DKRTIYTAGR
     PPWYNVTGTT FKEAFVIGLC GGSASGKTTV ANKIIEALDV PWVVLLSMDS FYKVLNKEEQ
     ELAAKNEYNF DHPDAFDFEL LVTVLRKLKK GKSIKVPVYD FTSHCRRKEW KTVYGANVVI
     FEGILAFANK ELLKLLDMKV FVDTDSDIRL IRRLKRDISQ RGRDISGIIK QYNKFVKPAF
     EQYIEPTVQS ADIVVPRGGE NFVALDLIVQ HVHSQLEKVR VPRPVSVSVR ESALASAHQG
     QPLPKTLSVM ESTPQVRGMH TIIRNKETNR DEFIFYSKRL MRLLIEHALS FLPLKPVSVE
     TPQGGVYDGK RLSGKRITGV SILRAGETME QALMAVCKDI RLGKILIQTN HDTGEPELHY
     LRLPKDISED YVILMDSTVS TGAAALMAVR VLLDHDVAED KIFLLSLLMA EMGVHSVAYA
     FPKVRIITTA VDKEVNDQFH IIPGIGNFGD RYFGTDAPSD WCESDEGMDF
//
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