GLRX1_VACCC
ID GLRX1_VACCC Reviewed; 108 AA.
AC P68690; P20818;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 29-SEP-2021, entry version 78.
DE RecName: Full=Glutaredoxin-1;
GN ORFNames=O2L;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
RN [3]
RP IDENTIFICATION.
RX PubMed=1994586; DOI=10.1016/0042-6822(91)90508-9;
RA Johnson G.P., Goebel S.J., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Vaccinia virus encodes a protein with similarity to glutaredoxins.";
RL Virology 181:378-381(1991).
CC -!- FUNCTION: Displays thioltransferase and dehydroascorbate reductase
CC activities. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; M35027; AAA48055.1; -; Genomic_DNA.
DR PIR; E42510; E42510.
DR BMRB; P68690; -.
DR SMR; P68690; -.
DR Proteomes; UP000008269; 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;
KW Reference proteome; Transport; Virion.
FT CHAIN 1..108
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141615"
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