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GLRX1_CWPXG
ID   GLRX1_CWPXG             Reviewed;         108 AA.
AC   Q80E01;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   29-SEP-2021, entry version 75.
DE   RecName: Full=Glutaredoxin-1;
GN   ORFNames=R2L;
OS   Cowpox virus (strain GRI-90 / Grishak) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265871;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shchelkunov S.N., Safronov P.F., Totmenin A.V., Miheev M.V.,
RA   Ryazankina O.I., Petrov N.A., Gutorov V.V., Kotwal G.J., Sandakhchiev L.S.;
RT   "Structure-function and organization of cowpox virus strain GRI-90 complete
RT   genome.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has 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; X94355; CAD90618.1; -; Genomic_DNA.
DR   SMR; Q80E01; -.
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; Virion.
FT   CHAIN           1..108
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000141623"
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;  12339 MW;  C36BBB0A639054C2 CRC64;
     MAEEFVQQRL ANNKVTIFVK FTCPFCRNAL DILNKFSFKR GAYEIVDIKE FKPENELRDY
     FEQITGGRTV PRIFFGKTSI GGYSDLLEID NMDALGDILS SIGVLRTC
 
 
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