GLRX1_ECTVM
ID GLRX1_ECTVM Reviewed; 108 AA.
AC Q8JLF5;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 29-SEP-2021, entry version 93.
DE RecName: Full=Glutaredoxin-1;
GN OrderedLocusNames=EVM053;
OS Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=265874;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14675635; DOI=10.1016/s0042-6822(03)00520-8;
RA Chen N., Danila M.I., Feng Z., Buller R.M., Wang C., Han X.,
RA Lefkowitz E.J., Upton C.;
RT "The genomic sequence of Ectromelia virus, the causative agent of
RT mousepox.";
RL Virology 317:165-186(2003).
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; AF012825; AAM92357.1; -; Genomic_DNA.
DR RefSeq; NP_671571.1; NC_004105.1.
DR PDB; 2HZE; X-ray; 1.80 A; A/B=1-108.
DR PDB; 2HZF; X-ray; 1.80 A; A/B=1-108.
DR PDBsum; 2HZE; -.
DR PDBsum; 2HZF; -.
DR SMR; Q8JLF5; -.
DR GeneID; 951620; -.
DR KEGG; vg:951620; -.
DR EvolutionaryTrace; Q8JLF5; -.
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 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Transport; Virion.
FT CHAIN 1..108
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141624"
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"
FT HELIX 2..7
FT /evidence="ECO:0007829|PDB:2HZE"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2HZE"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:2HZE"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2HZE"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2HZE"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2HZE"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2HZE"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2HZE"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2HZE"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:2HZE"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:2HZE"
SQ SEQUENCE 108 AA; 12327 MW; 92BA76087D7F54D4 CRC64;
MAEEFVQQRL ANNKVTIFVK YTCPFCRNAL DILNKFSFKR GAYEIVDIKE FKPENELRDY
FEQITGGKTV PRIFFGKTSI GGYSDLLEID NMDALGDILS SIGVLRTC