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UCK2B_DANRE
ID   UCK2B_DANRE             Reviewed;         261 AA.
AC   Q7ZV79;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Uridine-cytidine kinase 2-B;
DE            Short=UCK 2-B;
DE            EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9BZX2};
DE   AltName: Full=Cytidine monophosphokinase 2-B;
DE   AltName: Full=Uridine monophosphokinase 2-B;
GN   Name=uck2b; ORFNames=si:ch211-284b7.4, zgc:56174;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC       and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides
CC       or purine ribonucleosides. Can use ATP or GTP as a phosphate donor.
CC       {ECO:0000250|UniProtKB:Q9BZX2}.
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:0000250|UniProtKB:Q9BZX2};
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:0000250|UniProtKB:Q9BZX2};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000250|UniProtKB:Q9BZX2}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000250|UniProtKB:Q9BZX2}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BZX2}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR   EMBL; AL954171; CAM14217.1; -; Genomic_DNA.
DR   EMBL; BC045968; AAH45968.1; -; mRNA.
DR   RefSeq; NP_956058.1; NM_199764.2.
DR   AlphaFoldDB; Q7ZV79; -.
DR   SMR; Q7ZV79; -.
DR   STRING; 7955.ENSDARP00000033495; -.
DR   PaxDb; Q7ZV79; -.
DR   Ensembl; ENSDART00000037698; ENSDARP00000033495; ENSDARG00000022213.
DR   GeneID; 327057; -.
DR   KEGG; dre:327057; -.
DR   CTD; 327057; -.
DR   ZFIN; ZDB-GENE-030131-5265; uck2b.
DR   eggNOG; KOG4203; Eukaryota.
DR   GeneTree; ENSGT01020000230412; -.
DR   HOGENOM; CLU_021278_1_1_1; -.
DR   InParanoid; Q7ZV79; -.
DR   OMA; QDTFRYH; -.
DR   OrthoDB; 929897at2759; -.
DR   PhylomeDB; Q7ZV79; -.
DR   TreeFam; TF316686; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   PRO; PR:Q7ZV79; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000022213; Expressed in mature ovarian follicle and 28 other tissues.
DR   ExpressionAtlas; Q7ZV79; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043771; F:cytidine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004849; F:uridine kinase activity; ISS:UniProtKB.
DR   GO; GO:0044211; P:CTP salvage; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; ISS:UniProtKB.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR029925; UCK-2.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   PANTHER; PTHR10285:SF147; PTHR10285:SF147; 1.
DR   Pfam; PF00485; PRK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00235; udk; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..261
FT                   /note="Uridine-cytidine kinase 2-B"
FT                   /id="PRO_0000346105"
FT   REGION          238..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         29..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
SQ   SEQUENCE   261 AA;  29876 MW;  142358968B3E308D CRC64;
     MAGDSETHLK DRAENGHAVR QPFLIGVSGG TASGKSSVCE KIMELLGQNK IDRHQRQVVI
     LSQDSFYREL TPEQKAKAVK GQFNFDHPDA FDSELIMKTL RDIIQGKTVH IPVYDFVTHS
     RKDEFLTLYP ADVVLFEGIL MFYSQEIRDL FKMKLFVDTD PDTRLSRRVL RDISERGREL
     EQVLNQYITF VKPAFEEFCL PTKKYADVII PRGADNLVAI NLIVQHIQDI LNGGFTKRQN
     GFQNGHGTPR QRRTSESSRP H
 
 
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