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Database: UniProt
Entry: A0A158PP78_ANISI
LinkDB: A0A158PP78_ANISI
Original site: A0A158PP78_ANISI 
ID   A0A158PP78_ANISI        Unreviewed;       237 AA.
AC   A0A158PP78;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   03-MAY-2023, entry version 27.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|ARBA:ARBA00012310, ECO:0000256|RuleBase:RU000499};
GN   ORFNames=ASIM_LOCUS13287 {ECO:0000313|EMBL:VDK49354.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001385901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001385901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK49354.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000217};
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; UYRR01031355; VDK49354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158PP78; -.
DR   WBParaSite; ASIM_0001385901-mRNA-1; ASIM_0001385901-mRNA-1; ASIM_0001385901.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; Unassembled WGS sequence.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF88; GLUTATHIONE PEROXIDASE-RELATED; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000499};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..237
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035112093"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   237 AA;  27134 MW;  2F58442E28D0C64F CRC64;
     MTIGHSATAS AGILLLVAVS IVQQGHHVNA TPGPAVVDET SRWTQCRLSN QSIYDFQVQQ
     LDGKFTDLSK YRGQVLLIIN VATFCAFTQQ YLDFNPLIEQ NKRTTFKILA FPCNQFALQE
     PSENHELLNG IRYVRPGNGW KPHSNLHIFG KLQVNGENNH PLYEFVKDQC PQTVNRIGKR
     DELMYDPIRP SDITWNFEKF LVDRQGKVRF RFHPTAWSHG DVVQPFIQQL ANERARA
//
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