ID A0A1Y2DDF1_9PEZI Unreviewed; 241 AA.
AC A0A1Y2DDF1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
GN ORFNames=BCR38DRAFT_401848 {ECO:0000313|EMBL:ORY57312.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY57312.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY57312.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY57312.1,
RC ECO:0000313|Proteomes:UP000193689};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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:ORY57312.1}.
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DR EMBL; MCFJ01000020; ORY57312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DDF1; -.
DR STRING; 1141098.A0A1Y2DDF1; -.
DR InParanoid; A0A1Y2DDF1; -.
DR OrthoDB; 257613at2759; -.
DR Proteomes; UP000193689; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF23; PEROXIREDOXIN DOT5; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193689}.
FT DOMAIN 45..204
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 25294 MW; E07E245E37CFAAF2 CRC64;
MPVELRKRKA PAPAPEPPAK KTSKVSKAVA KVKETVKSTP TKSSEPNGAA KPVVGATITL
DGFGGEIETN EGTKTTLKAL VDESKSGVAL FTYPKASTPG CTNQACLFRD SYEPFTKDGL
AIYGLSTDSP KANTTFKEKQ KLPYPLLCDP SATLIDAIGL KKKPKGTQRG VFAIDKAGKV
LLAEPGGPAA TVEAVRKLVE STVGTEVKTE PVPVSEESNP VNGEDGTDEK KPEEAVTEPA
D
//
