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Database: UniProt
Entry: H2P2N5_PONAB
LinkDB: H2P2N5_PONAB
Original site: H2P2N5_PONAB 
ID   H2P2N5_PONAB            Unreviewed;       548 AA.
AC   H2P2N5; A0A2J8R2S0; A0A663DA68;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Uridine-cytidine kinase {ECO:0000256|RuleBase:RU003825};
DE            EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN   Name=UCKL1 {ECO:0000313|Ensembl:ENSPPYP00000012572.2};
GN   ORFNames=CR201_G0054498 {ECO:0000313|EMBL:PNJ02837.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000012572.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000012572.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ02837.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ02837.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000012572.2}
RP   IDENTIFICATION.
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|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   EMBL; NDHI03003786; PNJ02837.1; -; Genomic_DNA.
DR   RefSeq; XP_002830587.1; XM_002830541.2.
DR   STRING; 9601.ENSPPYP00000012572; -.
DR   Ensembl; ENSPPYT00000013069.3; ENSPPYP00000012572.2; ENSPPYG00000011253.3.
DR   GeneID; 100445813; -.
DR   KEGG; pon:100445813; -.
DR   CTD; 54963; -.
DR   eggNOG; KOG4203; Eukaryota.
DR   GeneTree; ENSGT01020000230412; -.
DR   HOGENOM; CLU_021278_0_1_1; -.
DR   OMA; EPQLHCE; -.
DR   OrthoDB; 180154at2759; -.
DR   TreeFam; TF105902; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000001595; Chromosome 20.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   CDD; cd02023; UMPK; 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; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   PANTHER; PTHR10285:SF68; URIDINE-CYTIDINE KINASE-LIKE 1; 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|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:UP000001595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT   DOMAIN          101..287
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  61113 MW;  E9D1BE8A802FE199 CRC64;
     MAAPPARADA DPSPTSPPTA QDTPGRQAEK SETACEDRSN AESLDRLLPP VGTGRSPRKR
     TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE
     ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN NFNFDHPDAF DFDLIISTLK KLKQGKSVKV
     PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR
     DISERGRDIE GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL
     EERELSVRAA LASAHQCHPL PRTLSVLKST PQVRGMHTII RDKETSRDEF IFYSKRLMRL
     LIEHALSFLP FQDCVVQTPQ GQDYAGKCYA GKQITGVSIL RAGETMEPAL RAVCKDVRIG
     TILIQTNQLT GEPELHYLRL PKDISDDHVI LMDCTVSTGA AAMMAVRVLL DHDVPEDKIF
     LLSLLMAEMG VHSVAYAFPR VRIITTAVDK RVNDLFRIIP GIGNFGDRYF GTDAVPDGSD
     EEEVAYTG
//
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