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Database: UniProt
Entry: P68691
LinkDB: P68691
Original site: P68691 
ID   GLRX1_VACCP             Reviewed;         108 AA.
AC   P68691; P20818;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   01-OCT-2014, entry version 47.
DE   RecName: Full=Glutaredoxin-1;
OS   Vaccinia virus (strain L-IVP) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=31531;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2250685;
RA   Riazankina O.I., Shchelkunov S.N., Muravlev A.I., Netesova N.A.,
RA   Mikriukov N.N., Gutorov V.V., Nikulin A.E., Kulichkov V.A.,
RA   Malygin E.G.;
RT   "Molecular-biological study of vaccinia virus genome. II. Localization
RT   and nucleotide sequence of vaccinia virus genes coding for proteins
RT   36K and 12K.";
RL   Mol. Biol. (Mosk.) 24:968-976(1990).
CC   -!- FUNCTION: Has thioltransferase and dehydroascorbate reductase
CC       activities.
CC   -!- SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 glutaredoxin domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00686}.
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DR   EMBL; X61166; CAA43476.1; -; Genomic_DNA.
DR   PIR; E42510; E42510.
DR   RefSeq; YP_232951.1; NC_006998.1.
DR   ProteinModelPortal; P68691; -.
DR   SMR; P68691; 1-107.
DR   GeneID; 3707602; -.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
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;
KW   Virion.
FT   CHAIN         1    108       Glutaredoxin-1.
FT                                /FTId=PRO_0000141616.
FT   DOMAIN        3    106       Glutaredoxin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00686}.
FT   DISULFID     23     26       Redox-active. {ECO:0000250}.
SQ   SEQUENCE   108 AA;  12355 MW;  8C754AE57D7F54D4 CRC64;
     MAEEFVQQRL ANNKVTIFVK YTCPFCRNAL DILNKFSFKR GAYEIVDIKE FKPENELRDY
     FEQITGGRTV PRIFFGKTSI GGYSDLLEID NMDALGDILS SIGVLRTC
//
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