GenomeNet

Database: UniProt
Entry: A0A0L7QTW0_9HYME
LinkDB: A0A0L7QTW0_9HYME
Original site: A0A0L7QTW0_9HYME 
ID   A0A0L7QTW0_9HYME        Unreviewed;       196 AA.
AC   A0A0L7QTW0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
DE   Flags: Fragment;
GN   ORFNames=WH47_05883 {ECO:0000313|EMBL:KOC61994.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC61994.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC61994.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC61994.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; KQ414741; KOC61994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7QTW0; -.
DR   STRING; 597456.A0A0L7QTW0; -.
DR   EnsemblMetazoa; XM_017938199.1; XP_017793688.1; LOC108575418.
DR   Proteomes; UP000053825; 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:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 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:UP000053825};
KW   Selenocysteine {ECO:0000256|ARBA:ARBA00022933}.
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KOC61994.1"
SQ   SEQUENCE   196 AA;  22313 MW;  8A144A825AACF22B CRC64;
     VALLTVLFFC GVIAEKCEDD KQEQCLASFD QDKDWKLATT IYDFHAKDIH GNDVSLDKYR
     GHVCIIVNVA SGCGLTDTHY KELVQLYEKY SEKEGLRILA FPSNQFGGQE PGTSQNILDF
     VKTYNVTFDM FEKIDVNGDE AHPLWKWLKT QASGFITGSI KWNFTKFLVN KEGKVVSRYG
     PTTSPLEIES ELKNYF
//
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