ID A0A395I2X8_ASPHC Unreviewed; 591 AA.
AC A0A395I2X8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:RAL14541.1};
GN ORFNames=BO97DRAFT_364685 {ECO:0000313|EMBL:RAL14541.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL14541.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL14541.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL14541.1,
RC ECO:0000313|Proteomes:UP000248961};
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 -!- SIMILARITY: Belongs to the DeSI family.
CC {ECO:0000256|ARBA:ARBA00008140}.
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; KZ824274; RAL14541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I2X8; -.
DR STRING; 1450537.A0A395I2X8; -.
DR VEuPathDB; FungiDB:BO97DRAFT_364685; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000248961; 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:UP000248961}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 163..286
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 302..590
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
FT REGION 149..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 65066 MW; 531843391841639D CRC64;
MDVELYVYDL SKGLARLYSM PLTGTQIDAI YHTSLVLNGV EYYYGQGIQT AVPGSTHHGQ
PMEKLHLGQT ELPLDVIEEY IQSVVEIYTP ESYDLFLHNC NNFTQDLAMF LLGKGIPEHI
RNLPQTFLST PFGQMMKPQI EMALRGVTQG TGTDGAQAPA TRAPAAPAAP AQPSPVTQGV
VRMASSLAQL EQHLTAASHS CAVIFFTSAT CPPCRMVYPT YDELAEEAGD RAILIKVDIS
SALDVSTKYR VRATPTFMTF LKGQKVDEWA GANPAQLRGN VRLLLEMAHP THRHRQLHLP
SFQRHLTNYV TYKKIPSLDK LRQKLHPHTT DTTLTAIIDF IQRRFSSPEP AADVALPSSL
PTFGPYLQTT LRTLAPEHQF ALVDLARLLF LDPRVSGYFA AEDPHHDLLR TLLASATASP
STTPYPLRIT LLQLACNLFT TPLYPDHFSG SNNNQNLALL QDLLHLTTAS LLDPHTNLRI
VAASFAYNLA AHNHNARFAS RPDPLTDEMQ VELVASLVEA IGQETQSREA LHGALFALGL
LVYEAPEEGT VVDLCKAMGV AEMVVGKRNI PELKGEETLI REVGEVLLGR G
//
