ID   A0A2V5HS82_9EURO        Unreviewed;       459 AA.
AC   A0A2V5HS82;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Thioredoxin-domain-containing protein {ECO:0000313|EMBL:PYI27338.1};
GN   ORFNames=BP00DRAFT_429421 {ECO:0000313|EMBL:PYI27338.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI27338.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI27338.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI27338.1,
RC   ECO:0000313|Proteomes:UP000248817};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ825572; PYI27338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5HS82; -.
DR   Proteomes; UP000248817; Unassembled WGS sequence.
DR   CDD; cd03002; PDI_a_MPD1_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR45815; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR   PANTHER; PTHR45815:SF3; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..459
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016090943"
FT   DOMAIN          14..144
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          250..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  48833 MW;  05D9DCF74068EF7C CRC64;
     MLPPSSAVFL AASLLAALPV QADGLYTKKS PVLQVTSKNY DQLIAQSNHT SIVEFYAPWC
     GHCQNLKPAY EKAAKNLDGL AKVAAINCDE DANKPICGQM GVRGFPTLKI VTPGKKPGKP
     RVEDYQGART AKAIVEAVVD RIPNHVRRLT DPDLEDWLAS TTGDVATPKA ILFTEKGTTS
     ALIRALAIDF LGAVQVAQVR SKETAAVERF GVTAFPTVVL VPAGGTEQDA IVYDGELKKA
     PLVAFLSQVA APNPDPAPVP PKKKKADKEE KQAAQPDDAK AEEESPKPAP AAPVPAPPIE
     LLTTPEALAA ACLAPKSGTC VLALLPGEQQ QEQTEPEPES SAAQVALASL AEVAHKHALH
     KSKLFPLYGV PATNGAAKAL RAALALAEQD LEIVAVNGRR GWWRKYDPAE ADYSVERVDA
     WVDAIRLGEG SKQKLPEGVI VEETQEDEKP VVAAEHDEL
//