ID   A0A1Y2D1S6_9FUNG        Unreviewed;       159 AA.
AC   A0A1Y2D1S6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=BCR33DRAFT_711821 {ECO:0000313|EMBL:ORY52535.1};
OS   Rhizoclosmatium globosum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Rhizoclosmatium.
OX   NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY52535.1, ECO:0000313|Proteomes:UP000193642};
RN   [1] {ECO:0000313|EMBL:ORY52535.1, ECO:0000313|Proteomes:UP000193642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL800 {ECO:0000313|EMBL:ORY52535.1,
RC   ECO:0000313|Proteomes:UP000193642};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORY52535.1}.
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DR   EMBL; MCGO01000003; ORY52535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2D1S6; -.
DR   STRING; 329046.A0A1Y2D1S6; -.
DR   OrthoDB; 5471093at2759; -.
DR   Proteomes; UP000193642; Unassembled WGS 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; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
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; 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:UP000193642}.
FT   ACT_SITE        39
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   159 AA;  17527 MW;  38199F015021A103 CRC64;
     MTGSFYELSI NKINNGKGTI NFADLKGKVV LAVNVASRCG RTKHYTGLEA LYKKYASQGL
     VVIGFPSNEF GAQEPGTEDE IVEFCSRNYD VTFDITEKIQ VNGSGAHPVF TYLKTHTNGA
     EVSWNFEKFL ISKDGSAVYR FENVVPEGLE AKINELLTA
//