ID G0W654_NAUDC Unreviewed; 299 AA.
AC G0W654;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN Name=NDAI0B02300 {ECO:0000313|EMBL:CCD23265.1};
GN OrderedLocusNames=NDAI_0B02300 {ECO:0000313|EMBL:CCD23265.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD23265.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD23265.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE580268; CCD23265.1; -; Genomic_DNA.
DR RefSeq; XP_003668508.1; XM_003668460.1.
DR AlphaFoldDB; G0W654; -.
DR STRING; 1071378.G0W654; -.
DR GeneID; 11497969; -.
DR KEGG; ndi:NDAI_0B02300; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR OMA; NGPRCGF; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000000689; Chromosome 2.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 1..112
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 299 AA; 34111 MW; BF5DD092325597BC CRC64;
MPALQITTNE QFTQLTEASS PPDNKLIVLY FYTKWAEPCH STNELFDALN DEFRNENALF
LAIDADINND IISNLNVSIV PYFIFIQNGK LLEQLSGEDP KKFVQILDQY LCISSTLSLS
NLSLSNNNNN IYEYDSDNSA DSNNSKYTID SDYTSEDDIK HTKHFHNHMH HVDTQHLMNE
DEFNLKLSKL VQAAPVMLFL KGTPSEPKCG YSRQMVKILR ANKIRFGFFN VLSDNNVRIN
MKKFSDWPTF PQLYINGEFQ GGLDIIKETL LDDPDYFFHT LQSSPTGGGT INPQIPSSL
//
