ID K1VKK3_TRIAC Unreviewed; 234 AA.
AC K1VKK3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:EKD04675.1};
GN ORFNames=A1Q2_01013 {ECO:0000313|EMBL:EKD04675.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04675.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04675.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04675.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKD04675.1}.
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DR EMBL; AMBO01000192; EKD04675.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VKK3; -.
DR STRING; 1220162.K1VKK3; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; K1VKK3; -.
DR OMA; CEPCTAV; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
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 CDD; cd02984; TRX_PICOT; 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.
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:UP000006757}.
FT DOMAIN 10..96
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT DOMAIN 149..213
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT REGION 109..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 25776 MW; 534E18104200486A CRC64;
MSTSNFVNIS SPEQFKEELS KDLNRVSLLN FWAPWAEPCA AFNKAVEEAA AKYPSVLFLN
AEEQADIAES FDIEAVPSFV LLRGHTLLGR HSGADTGVLN ALLSQNATSS SAPSSNVSAA
ASTPAEPSRP RTEEEITERC KELMNKHKVV LFMKGNPSAP KCGFSRQTVG LLREKGVEFA
WFDILSDEEV RQGLKRVNDW PTFPQIILNG ELVGGLDILK EMIESGEWDE VYNA
//