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Database: UniProt
Entry: A0A8C4Z8X9_GADMO
LinkDB: A0A8C4Z8X9_GADMO
Original site: A0A8C4Z8X9_GADMO 
ID   A0A8C4Z8X9_GADMO        Unreviewed;       262 AA.
AC   A0A8C4Z8X9;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 3.
DT   28-JAN-2026, entry version 19.
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:ENSGMOP00000008134.2};
GN   Synonyms=uck2a {ECO:0000313|Ensembl:ENSGMOP00000008134.2};
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049 {ECO:0000313|Ensembl:ENSGMOP00000008134.2, ECO:0000313|Proteomes:UP000694546};
RN   [1] {ECO:0000313|Ensembl:ENSGMOP00000008134.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSGMOP00000008134.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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   -!- SIMILARITY: Belongs to the uridine kinase family.
CC       {ECO:0000256|ARBA:ARBA00005408, ECO:0000256|RuleBase:RU003825}.
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DR   AlphaFoldDB; A0A8C4Z8X9; -.
DR   Ensembl; ENSGMOT00000008367.2; ENSGMOP00000008134.2; ENSGMOG00000007600.2.
DR   GeneTree; ENSGT01020000230412; -.
DR   OMA; WPPCPAM; -.
DR   OrthoDB; 10257085at2759; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000694546; Chromosome 12.
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; 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; NF004018; PRK05480.1; 1.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 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:UP000694546};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT   DOMAIN          24..219
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   262 AA;  29744 MW;  5A4BF97685AB4AC1 CRC64;
     MAGDDETKPD DQTANDQNNR QPFLIGVAGG TASGKSSVCS KIMELLGQNK IDHHHRQVVI
     LSLDSFYRVL SPEQKARALK GQFNFDHPDA FDNDLIISTL WDILEGKIVQ LPVYDFVIHS
     RKEETVTVYP ADVVLCEGIL MFYAQEIRDM FQMKLFVDTD ADTRLSRRVL RDICERGRDL
     ESVLSQYIMF VKPAFEEFCL PTKKYADVII PRGADNLVAI NLIVQHIQDI LNGGLNKKNN
     GCLEDYELTQ NLQNTEPSSR PH
//
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