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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
 
 
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