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