ID T0R4B2_SAPDV Unreviewed; 225 AA.
AC T0R4B2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 28-JUN-2023, entry version 31.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=SDRG_01161 {ECO:0000313|EMBL:EQC41185.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC41185.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC41185.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC41185.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. {ECO:0000256|PIRNR:PIRNR000239}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family.
CC {ECO:0000256|PIRNR:PIRNR000239}.
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DR EMBL; JH767134; EQC41185.1; -; Genomic_DNA.
DR RefSeq; XP_008604899.1; XM_008606677.1.
DR AlphaFoldDB; T0R4B2; -.
DR STRING; 1156394.T0R4B2; -.
DR EnsemblProtists; EQC41185; EQC41185; SDRG_01161.
DR GeneID; 19941888; -.
DR VEuPathDB; FungiDB:SDRG_01161; -.
DR eggNOG; KOG0854; Eukaryota.
DR InParanoid; T0R4B2; -.
DR OMA; PTNWKIN; -.
DR OrthoDB; 64061at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|PIRNR:PIRNR000239};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239}; Peroxidase {ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762}.
FT DOMAIN 7..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 225 AA; 25048 MW; 081E6E6A27D8A72B CRC64;
MAPAPTLQVG MKIPKLVGST QMGAIKLHDF IDGAWALLLT FPQDFHPVWI TELGMLAKLK
PQFDVRNCRV LGLSIGSLKN QARFLDDVNE TQDTQVNFPI FADESGLLSR MLGLVNPTSA
PSSADHAVLP YSAAFLMDVD MVIRFAFYYP MSIGRNLYEF IRVLDGLQLA AYNQVVLPTN
WKINDDVFVE PDISSEAAKA LFPNGFHEIK PYFRVTPAPV LSEDQ
//
