ID A0A0V0R5M2_PSEPJ Unreviewed; 125 AA.
AC A0A0V0R5M2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=PPERSA_02643 {ECO:0000313|EMBL:KRX09771.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX09771.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX09771.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX09771.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX09771.1}.
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DR EMBL; LDAU01000044; KRX09771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R5M2; -.
DR EnsemblProtists; KRX09771; KRX09771; PPERSA_02643.
DR InParanoid; A0A0V0R5M2; -.
DR OMA; HMMKDID; -.
DR OrthoDB; 177208at2759; -.
DR Proteomes; UP000054937; 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 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:SF27; GLUTATHIONE PEROXIDASE 8-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; 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:UP000054937}.
SQ SEQUENCE 125 AA; 14558 MW; DFB599D7812E796B CRC64;
MDQLYDKYGQ KGLEIFAFPC NQFGAQEPNP NNEILDAARK KTNCKIQYPF FEKLEVNGKA
CHEVYQFLKN NSSLWNESKG KCEDIKWNFG KFLVDGQGYV KNYYEPGITP MEIEEDIKKL
LKSVQ
//
