ID A0A0V0QGB2_PSEPJ Unreviewed; 233 AA.
AC A0A0V0QGB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JUN-2023, entry version 22.
DE SubName: Full=Thioredoxin-like fold {ECO:0000313|EMBL:KRX01299.1};
GN ORFNames=PPERSA_11746 {ECO:0000313|EMBL:KRX01299.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX01299.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX01299.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX01299.1};
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}.
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:KRX01299.1}.
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DR EMBL; LDAU01000171; KRX01299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QGB2; -.
DR EnsemblProtists; KRX01299; KRX01299; PPERSA_11746.
DR InParanoid; A0A0V0QGB2; -.
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; 2.
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; 2.
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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937}.
FT REGION 90..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 27326 MW; 78D79215D2919371 CRC64;
MGNSGIKKLF FPGEYVETKY KNFYELEGID LDLNKQNFHQ FEKKIILCTN VSSRGSMAKE
QFQNLEKIQQ EGNQYYKAAL ESHMDILKNQ QNDKNKQKNS KNQKNSSNKD SDNQQIPGFN
NNGFEILCFP SNQFYNEPGT FSNLKQIYLL NDSYRNLRFF GKVELNGQYA SPIFKFLKRN
SILYDYRSLS AEPIVEDFSK FLIDQNGQVI KYYRNDVSAS QITKDYNKVQ QIH
//
