GLRX1_VACCA
ID GLRX1_VACCA Reviewed; 108 AA.
AC Q76ZV3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 29-SEP-2021, entry version 84.
DE RecName: Full=Glutaredoxin-1;
GN OrderedLocusNames=MVA061L, ACAM3000_MVA_061;
OS Vaccinia virus (strain Ankara) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=126794;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT "The complete genomic sequence of the modified vaccinia Ankara strain:
RT comparison with other orthopoxviruses.";
RL Virology 244:365-396(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Acambis 3000;
RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA Khristova M., Wohlhueter R.M.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has thioltransferase and dehydroascorbate reductase
CC activities.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; U94848; AAB96432.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10459.1; -; Genomic_DNA.
DR RefSeq; YP_232951.1; NC_006998.1.
DR BMRB; Q76ZV3; -.
DR SMR; Q76ZV3; -.
DR DNASU; 3707602; -.
DR GeneID; 3707602; -.
DR KEGG; vg:3707602; -.
DR Proteomes; UP000159908; Genome.
DR Proteomes; UP000172909; 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 3: Inferred from homology;
KW Disulfide bond; Electron transport; Redox-active center; Transport.
FT CHAIN 1..108
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141614"
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