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
//