ID X6NQJ7_RETFI Unreviewed; 249 AA.
AC X6NQJ7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN ORFNames=RFI_08562 {ECO:0000313|EMBL:ETO28565.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO28565.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO28565.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:ETO28565.1}.
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DR EMBL; ASPP01006596; ETO28565.1; -; Genomic_DNA.
DR AlphaFoldDB; X6NQJ7; -.
DR EnsemblProtists; ETO28565; ETO28565; RFI_08562.
DR OMA; VRHTTCN; -.
DR OrthoDB; 47465at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:RHEA.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000313|EMBL:ETO28565.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT DOMAIN 27..184
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 249 AA; 28504 MW; 10E51E91ED844374 CRC64;
MSSIFSSRLW SRCTAAATRT FVQKRHLQIQ QLAPSFSATA VIDKKFSTIK LQDYKGKYLV
LFFYPLDFTF VCPTEIIEFS DRVKEFKELD CEVIGASIDS HFSHLAWIET PREKGGLGEM
NIPLLADITG KISKDYDCMS DEGFTVRATY IIDSKGKVRH ISLTDTSVGR SVDEVLRLVE
AFQYTDHYGE VCPAGWKEGG KTVILFNFKL FYFKRQSLLK LMFSVENLNF VTFSLNQTFV
IMKTIHAIF
//
