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YDJC_DANRE
ID   YDJC_DANRE              Reviewed;         313 AA.
AC   A2BIR6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000250|UniProtKB:Q53WD3};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q53WD3};
GN   Name=ydjc; ORFNames=si:ch211-89f7.6;
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).
CC   -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC       carbohydrates an important step in the degradation of oligosaccharides.
CC       {ECO:0000250|UniProtKB:Q53WD3}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q53WD3};
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000305}.
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DR   EMBL; BX957246; CAM14368.1; -; Genomic_DNA.
DR   RefSeq; NP_001076331.1; NM_001082862.1.
DR   RefSeq; XP_005165107.1; XM_005165050.3.
DR   RefSeq; XP_017211642.1; XM_017356153.1.
DR   AlphaFoldDB; A2BIR6; -.
DR   SMR; A2BIR6; -.
DR   STRING; 7955.ENSDARP00000085284; -.
DR   PaxDb; A2BIR6; -.
DR   PRIDE; A2BIR6; -.
DR   Ensembl; ENSDART00000090851; ENSDARP00000085284; ENSDARG00000062655.
DR   Ensembl; ENSDART00000182189; ENSDARP00000153022; ENSDARG00000062655.
DR   GeneID; 569036; -.
DR   KEGG; dre:569036; -.
DR   CTD; 150223; -.
DR   ZFIN; ZDB-GENE-060526-182; ydjc.
DR   eggNOG; ENOG502RYFJ; Eukaryota.
DR   GeneTree; ENSGT00390000002575; -.
DR   HOGENOM; CLU_064244_1_0_1; -.
DR   InParanoid; A2BIR6; -.
DR   OMA; HPQEGGC; -.
DR   OrthoDB; 845079at2759; -.
DR   PhylomeDB; A2BIR6; -.
DR   TreeFam; TF329340; -.
DR   PRO; PR:A2BIR6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000062655; Expressed in blastula and 21 other tissues.
DR   GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR006879; YdjC-like.
DR   PANTHER; PTHR31609; PTHR31609; 1.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..313
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000328776"
FT   REGION          262..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        13
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
SQ   SEQUENCE   313 AA;  34977 MW;  E4CDAC8CC7FAF516 CRC64;
     MPQPKVKLVV TGDDFGYCER RNQGIVDCFR AGGISNVSLL VNAVSAKHAA DLAKRYHMPI
     GLHANLSEGL PVSQELKGST LLNKDGFFHG KMGFREVLHS GQLKMSEVEA ELRAQVNRFF
     ELIGHMPYHM DGHQHVHVLP DVREVFAQVL SDFGITYTRV PIEPGLRFCN FLPSHLREFN
     AQVEKDALES VEVFHRNGIR WPDVYLGLST MGKNMCLSNL KRALEASLDD GVSSPLILTQ
     SNNAASNCYR PVTAELMVHP GYPSQPQQGG CGEGPDDFSQ STDRLHELNT LRDPMVLNFY
     RQQGIHLCAF KDF
 
 
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