ID A0A0G4IY90_PLABS Unreviewed; 267 AA.
AC A0A0G4IY90;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=PBRA_008042 {ECO:0000313|EMBL:CEP00308.1}, PLBR_LOCUS2302
GN {ECO:0000313|EMBL:SPQ95087.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OG Mitochondrion {ECO:0000313|EMBL:SPQ95087.1}.
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP00308.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEP00308.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEP00308.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPQ95087.1, ECO:0000313|Proteomes:UP000290189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fogelqvist J.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505}.
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DR EMBL; CDSF01000100; CEP00308.1; -; Genomic_DNA.
DR EMBL; OVEO01000003; SPQ95087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IY90; -.
DR STRING; 37360.A0A0G4IY90; -.
DR EnsemblProtists; CEP00308; CEP00308; PBRA_008042.
DR OMA; TREAWIQ; -.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR Proteomes; UP000290189; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000313|EMBL:SPQ95087.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324}.
FT DOMAIN 4..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 248..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 267 AA; 29190 MW; 7050773C9F9F440F CRC64;
MATSLEGRRV PDAAFRFFKD GRFTDVRTDQ LFNNQSIVAF ALPGAFTPTC SSNHFPRYLE
LAQHFFDNGV DAILCISVND SFVLDAWSKD QGNDDTVVMV PDGNGEFTKQ LGMLLDLSSA
GLGHRSRRYS MLVRDGLIEK AFVEPNVVGD PYVVSDADTI LAYLCPSLIL QPDITVFTKA
TCPVSHAAKG WLKNRSLSFS EVVVGKDVSN QVLRAVSGST KVPQIFVSGH HIGGFDELQT
REAWIQSGEA REPKLSAEAG SVTPRSE
//
