ID A1CQU2_ASPCL Unreviewed; 240 AA.
AC A1CQU2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 22-FEB-2023, entry version 60.
DE SubName: Full=Thioredoxin, putative {ECO:0000313|EMBL:EAW08013.1};
GN ORFNames=ACLA_027350 {ECO:0000313|EMBL:EAW08013.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW08013.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW08013.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027059; EAW08013.1; -; Genomic_DNA.
DR RefSeq; XP_001269439.1; XM_001269438.1.
DR AlphaFoldDB; A1CQU2; -.
DR STRING; 344612.A1CQU2; -.
DR EnsemblFungi; EAW08013; EAW08013; ACLA_027350.
DR GeneID; 4701263; -.
DR KEGG; act:ACLA_027350; -.
DR VEuPathDB; FungiDB:ACLA_027350; -.
DR eggNOG; ENOG502QTH7; Eukaryota.
DR HOGENOM; CLU_069253_0_1_1; -.
DR OMA; KPTNTFD; -.
DR OrthoDB; 19921at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd03024; DsbA_FrnE; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR PANTHER; PTHR13887:SF41; THIOREDOXIN SUPERFAMILY PROTEIN; 1.
DR Pfam; PF01323; DSBA; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 5..116
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT DOMAIN 141..231
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
SQ SEQUENCE 240 AA; 26832 MW; 07649465478AFE80 CRC64;
MTNITIQIVS DTVCPWCYIG LRRLSRAITT HRASHPTDTF TLTWQPFYLN PQAPAYPGTN
KREHYASKFG GERARAIFAR LAGVGAGEDI AFAFGGQTGR TRDSHRVLWY AGRKEREREL
RGGEEGVKEE KKEEGVGIGG LQTRVAEQLF RAYFEEEKNI TDRGVLVEAA AAAGLDRAEV
ERFLESGDEG GKEVDLEAER ARQRLVTGVP YFTVQGRYAV EGADEPDTFL EIFEKVKQVV
//