ID B8N6S7_ASPFN Unreviewed; 269 AA.
AC B8N6S7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Thioredoxin, putative {ECO:0000313|EMBL:EED54428.1};
GN ORFNames=AFLA_016800 {ECO:0000313|EMBL:EED54428.1}, G4B84_006244
GN {ECO:0000313|EMBL:QMW30863.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED54428.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED54428.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED54428.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW30863.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW30863.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; EQ963474; EED54428.1; -; Genomic_DNA.
DR EMBL; CP059869; QMW30863.1; -; Genomic_DNA.
DR RefSeq; XP_002375700.1; XM_002375659.1.
DR AlphaFoldDB; B8N6S7; -.
DR STRING; 332952.B8N6S7; -.
DR EnsemblFungi; EED54428; EED54428; AFLA_016800.
DR VEuPathDB; FungiDB:AFLA_002131; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR OMA; CEPCTAV; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:EnsemblFungi.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:EnsemblFungi.
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.
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}.
FT DOMAIN 1..114
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 113..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 28882 MW; 91B89B08C5E55985 CRC64;
MSTLIEISSE AEFDSHIKSL PSTTLSILYF HAPWAAPCAQ MRTVLAALAS QYPATQPPTT
SFISINAEEL PDISETYEVT AVPFVVLTRD GKILESISGS DAVRVREAIE RHAGSKASAG
APATIPPPLA AVPRETGPTT ATQPPAGAAN GDALTPEQSK EALFARLREL VKAAPVMLFM
KGTPSAPQCG FSRQLVAILR ERSVKYGFFN ILADEDVRQG LKEFADWPTF PQLWVGGELV
GGLDIVKDEI ENDPDFLREH SVNKAPVAA
//
