ID A0A319CJZ0_9EURO Unreviewed; 595 AA.
AC A0A319CJZ0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:PYH75728.1};
GN ORFNames=BO82DRAFT_359789 {ECO:0000313|EMBL:PYH75728.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH75728.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH75728.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH75728.1,
RC ECO:0000313|Proteomes:UP000248340};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DeSI family.
CC {ECO:0000256|ARBA:ARBA00008140}.
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DR EMBL; KZ821779; PYH75728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CJZ0; -.
DR STRING; 1448315.A0A319CJZ0; -.
DR VEuPathDB; FungiDB:BO82DRAFT_359789; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.90.1720.30; PPPDE domains; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008580; PPPDE_dom.
DR InterPro; IPR042266; PPPDE_sf.
DR InterPro; IPR013535; PUL_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12378; DESUMOYLATING ISOPEPTIDASE; 1.
DR PANTHER; PTHR12378:SF7; DESUMOYLATING ISOPEPTIDASE 1; 1.
DR Pfam; PF05903; Peptidase_C97; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM01179; DUF862; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51858; PPPDE; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340}.
FT DOMAIN 1..122
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 146..278
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 306..593
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
SQ SEQUENCE 595 AA; 64912 MW; 3E33A4B89A7E00C1 CRC64;
MPLTGTQIDA IYHTSLVLNG IEYYFGQGIQ TAVPGSTHHG QPMEKLHLGQ TELPLDVIEE
YIQSMAEIYT PESYDLFLHN CNNFTQDLAM FLLGKGIPEH IQNLPQTFLS TPFGQMMKPQ
IEMALRGVTQ GTGTDGAQAP PASRPAAAAA AAAAAAATPA QQPSSPPVSQ GVVRMASSLA
QLEQHLTAAS QSCAVIFFTS ATCPPCRMVY PMYDELAEEA GDRAILIKVD ISTARDVSTK
YRVRATPTFM TFLKGQKVDE WSGANPAQLR GNVRLLLEMA TPTHRHRQLH LPSFQRHLPN
YVTYKKIPPL DKLRQKLHPH TDDSTLTSIL DFIQRRFITT SPDSTGAAAA ADVALPASLP
TFGPYLQTTL GTLTPENQFA LVDLVRLLFI DPRVSGWFAA EDPHHELLRT LLSSTNTAAA
TTTITTPYPL RITLCQLACN LFTTSLYPDH FLPTSPNNDP QLLPLLLNLT TTSLLDPHPN
LRIVAASFAY NLAAHNHNAR FAGRPDPLPT EMQVELVASL VEALDRETQS REAVHGLLFA
LGLLVYEAPE DGEVVDLCKA MGVHEMIVAK KGIPALQGEE ALLREVGEVL LGRGM
//
