(data stored in SCRATCH zone)

SWISSPROT: Q6BLZ6_DEBHA

ID   Q6BLZ6_DEBHA            Unreviewed;       160 AA.
AC   Q6BLZ6;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   OrderedLocusNames=DEHA2F09526g {ECO:0000313|EMBL:CAG89116.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89116.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89116.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|RuleBase:RU000499, ECO:0000256|SAAS:SAAS00719801}.
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DR   EMBL; CR382138; CAG89116.2; -; Genomic_DNA.
DR   RefSeq; XP_460775.2; XM_460775.1.
DR   STRING; 4959.XP_460775.2; -.
DR   PeroxiBase; 5592; DhGPx01.
DR   EnsemblFungi; CAG89116; CAG89116; DEHA2F09526g.
DR   GeneID; 2903617; -.
DR   KEGG; dha:DEHA2F09526g; -.
DR   HOGENOM; HOG000277054; -.
DR   InParanoid; Q6BLZ6; -.
DR   KO; K00432; -.
DR   OMA; NQFGSQD; -.
DR   OrthoDB; 1483113at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLZ6.
DR   SWISS-2DPAGE; Q6BLZ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000499,
KW   ECO:0000256|SAAS:SAAS00719797};
KW   Peroxidase {ECO:0000256|RuleBase:RU000499,
KW   ECO:0000256|SAAS:SAAS00719795};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   ACT_SITE     35     35       {ECO:0000256|PIRSR:PIRSR000303-1}.
SQ   SEQUENCE   160 AA;  18003 MW;  2D7F66C24AF68E98 CRC64;
     MSFYDLSPLD TNDKPFPFEE LKGKVVLVVN VASKCGFTPQ YKELEELNKK YQDKGLQIIG
     FPCNQFGGQE PGSSEEIASF CSLNYGVSFP VLKKVDVNGD KTDPVYKYLK GEKSGLLGLN
     RIKWNFEKFL IDKNGKVIER YSSLTKPASL SSTIEELLKK
//

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