ID   GLRX2_VACCC             Reviewed;         124 AA.
AC   P68461; P21025;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   23-FEB-2022, entry version 76.
DE   RecName: Full=Glutaredoxin-2;
GN   ORFNames=G4L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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; M35027; AAA48068.1; -; Genomic_DNA.
DR   PIR; I42511; I42511.
DR   SMR; P68461; -.
DR   Proteomes; UP000008269; 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_0000141627"
FT   DISULFID        13..16
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  13987 MW;  DFBE2D7B3A1A9CA6 CRC64;
     MKNVLIIFGK PYCSICENVS DAVEELKSEY DILHVDILSF FLKDGDSSML GDVKRGTLIG
     NFAAHLSNYI VSIFKYNPQT KQMAFVDINK SLDFTKTDKS LVNLEILKSE IEKATYGVWP
     PVTE