ID A0A0G4FSJ4_VITBC Unreviewed; 312 AA.
AC A0A0G4FSJ4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=Vbra_21670 {ECO:0000313|EMBL:CEM17404.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM17404.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM17404.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001346};
CC -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC {ECO:0000256|ARBA:ARBA00025782}.
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DR EMBL; CDMY01000488; CEM17404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4FSJ4; -.
DR VEuPathDB; CryptoDB:Vbra_21670; -.
DR InParanoid; A0A0G4FSJ4; -.
DR OMA; TADAYKC; -.
DR OrthoDB; 1201562at2759; -.
DR PhylomeDB; A0A0G4FSJ4; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR CDD; cd09212; PUB; 1.
DR Gene3D; 1.20.58.2190; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR PANTHER; PTHR13871:SF7; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SMART; SM00580; PUG; 1.
DR SUPFAM; SSF143503; PUG domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000041254}.
FT DOMAIN 25..194
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 34316 MW; D44270172FF8DF6D CRC64;
MSNVKSTSNV IIRAVRLKLL RVPSSQVEEK NMTMALVPLF GDHLIRGTTP VPTASLDADV
IGIYFSAHWC PPCQIFTPQL AQVYMVAKTM EKSFEIVFVS SDRDASSFQH YFATMPWLAI
PFDKPTRQVL KSRYGISGIP SLVLINGRDG SLINKEGRQQ ALQPNFVQGL PMGGGLDASV
RGVDLEAALE ALDSSGVGDE EKRIGLETIA TVIRNVVNHP GEAKYRTLKK SNKSVQQKLG
RPEFAQLLKV AGFREQQDSY TIPEANTRDT SHIKAVLDTL SCLIETLPQQ QQEQEQLRQA
DDAPQPNADA AA
//
