ID   GLRX2_VAR67             Reviewed;         124 AA.
AC   P0DSY3; P32994; Q76Q24;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   23-FEB-2022, entry version 8.
DE   RecName: Full=Glutaredoxin-2;
GN   ORFNames=G4L;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8109158; DOI=10.1016/0168-1702(93)90093-3;
RA   Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V.,
RA   Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of a 43 kbp segment of the genome of
RT   variola virus India-1967 strain.";
RL   Virus Res. 30:239-258(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8383392; DOI=10.1016/0168-1702(93)90110-9;
RA   Shchelkunov S.N., Blinov V.M., Totmenin A.V., Marennikova S.S.,
RA   Kolykhalov A.A., Frolov I.V., Chizhikov V.E., Gytorov V.V., Gashikov P.V.,
RA   Belanov E.F., Belavin P.A., Resenchuk S.M., Andzhaparidze O.G.,
RA   Sandakhchiev L.S.;
RT   "Nucleotide sequence analysis of variola virus HindIII M, L, I genome
RT   fragments.";
RL   Virus Res. 27:25-35(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X67119; CAA47566.1; -; Genomic_DNA.
DR   EMBL; X69198; CAA49007.1; -; Genomic_DNA.
DR   PIR; S33081; S33081.
DR   RefSeq; NP_042110.1; NC_001611.1.
DR   SMR; P0DSY3; -.
DR   GeneID; 1486432; -.
DR   KEGG; vg:1486432; -.
DR   Proteomes; UP000002060; 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   Reference proteome; Transport.
FT   CHAIN           1..124
FT                   /note="Glutaredoxin-2"
FT                   /id="PRO_0000141630"
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