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Database: UniProt
Entry: A0A0M4EGW7_DROBS
LinkDB: A0A0M4EGW7_DROBS
Original site: A0A0M4EGW7_DROBS 
ID   A0A0M4EGW7_DROBS        Unreviewed;       212 AA.
AC   A0A0M4EGW7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=Dbus_chr3Lg906 {ECO:0000313|EMBL:ALC43740.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC43740.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC43740.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC43740.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-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; CP012525; ALC43740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4EGW7; -.
DR   SMR; A0A0M4EGW7; -.
DR   STRING; 30019.A0A0M4EGW7; -.
DR   OMA; IGFPANN; -.
DR   Proteomes; UP000494163; Chromosome 3l sequence.
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   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 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:UP000494163}.
FT   DOMAIN          67..212
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   212 AA;  23449 MW;  93779591E98B47E0 CRC64;
     MNLKHMQSIG RQASRCFRLS AVAANKPSQQ RRYCVVLLPL AVVHCTADTK KAQYSTAAGI
     DMSGGDFKNA ASVYEFTVKD THGNDVSLEK YKGRVLLVVN IASKCGLTKN NYQKLTELKE
     KFGERGLTIL NFPCNQFNSQ MPESDGEAMV NVNGDDAAPL YKYLKAKQTG TLGSGLKWNF
     TKFLVNKEGI PVNRYAPTTD PMDIAKDIEK LL
//
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