ID   GLRX2_VARV              Reviewed;         124 AA.
AC   P0DSY4; P32994; Q76Q24;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   23-FEB-2022, entry version 12.
DE   RecName: Full=Glutaredoxin-2;
GN   ORFNames=G4L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RA   Shchelkunov S.N., Sosnovtsev S.V., Totmenin A.V., Resenchuk S.M.,
RA   Blinov V.M., Sandakhchiev L.S.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RX   PubMed=10639322; DOI=10.1006/viro.1999.0086;
RA   Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V.,
RA   Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.;
RT   "Alastrim smallpox variola minor virus genome DNA sequences.";
RL   Virology 266:361-386(2000).
CC   -!- FUNCTION: Glutaredoxin necessary for virion morphogenesis and virus
CC       replication. Functions as a thiol-disulfide transfer protein between
CC       membrane-associated A2.5 and substrates L1 or F9. The complete pathway
CC       for formation of disulfide bonds in intracellular virion membrane
CC       proteins sequentially involves oxidation of E10, A2.5 and G4. Exhibit
CC       thioltransferase and dehydroascorbate reductase activities in vitro (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with A2.5; this
CC       interaction involves formation of a transient disulfide-bonded
CC       intermediate, allowing disulfide bond transfer. Interacts with L1; this
CC       interaction involves formation of a transient disulfide-bonded
CC       intermediate, allowing disulfide bond transfer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60814.1; -; Genomic_DNA.
DR   EMBL; X76267; CAA53871.1; -; Genomic_DNA.
DR   EMBL; Y16780; CAB54666.1; -; Genomic_DNA.
DR   PIR; H72158; H72158.
DR   PIR; T28504; T28504.
DR   RefSeq; NP_042110.1; NC_001611.1.
DR   SMR; P0DSY4; -.
DR   GeneID; 1486432; -.
DR   KEGG; vg:1486432; -.
DR   Proteomes; UP000111493; Genome.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008554; Glutaredoxin-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF05768; Glrx-like; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Host cytoplasm; Redox-active center;
KW   Transport.
FT   CHAIN           1..124
FT                   /note="Glutaredoxin-2"
FT                   /id="PRO_0000448227"
FT   DISULFID        13..16
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  14014 MW;  3FB68E3E2E4A89A7 CRC64;
     MKNVLIIFGK PYCSICENVS EAVEELKSEY DILHVDILSF FLKDGDSSML GDVKRGTLIG
     NFAAHLSNYI VSIFKYNPQT KQMAFVDINK SLDFTKTDKS LVNLEILKSE IEKANYGVWP
     PVTE