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GLRX1_VACCW
ID   GLRX1_VACCW             Reviewed;         108 AA.
AC   P68692; P20818;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   29-SEP-2021, entry version 86.
DE   RecName: Full=Glutaredoxin-1;
GN   OrderedLocusNames=VACWR069; ORFNames=O2L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
RP   CHARACTERIZATION.
RX   PubMed=1496000; DOI=10.1073/pnas.89.15.7060;
RA   Ahn B.-Y., Moss B.;
RT   "Glutaredoxin homolog encoded by vaccinia virus is a virion-associated
RT   enzyme with thioltransferase and dehydroascorbate reductase activities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7060-7064(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Displays thioltransferase and dehydroascorbate reductase
CC       activities.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:1496000}.
CC       Note=Localizes to the virion core. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; M76472; AAA48249.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89348.1; -; Genomic_DNA.
DR   PIR; E42510; E42510.
DR   RefSeq; YP_232951.1; NC_006998.1.
DR   BMRB; P68692; -.
DR   SMR; P68692; -.
DR   DNASU; 3707602; -.
DR   GeneID; 3707602; -.
DR   KEGG; vg:3707602; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02180; GRX_euk; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport; Virion.
FT   CHAIN           1..108
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000141618"
FT   DOMAIN          3..106
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        23..26
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   108 AA;  12355 MW;  8C754AE57D7F54D4 CRC64;
     MAEEFVQQRL ANNKVTIFVK YTCPFCRNAL DILNKFSFKR GAYEIVDIKE FKPENELRDY
     FEQITGGRTV PRIFFGKTSI GGYSDLLEID NMDALGDILS SIGVLRTC
 
 
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