ID A0A2T3ZBT3_9HYPO Unreviewed; 579 AA.
AC A0A2T3ZBT3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M441DRAFT_165314 {ECO:0000313|EMBL:PTB42267.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB42267.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB42267.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB42267.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-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; KZ679260; PTB42267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZBT3; -.
DR STRING; 1042311.A0A2T3ZBT3; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000240493; 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; 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; 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:UP000240493}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 160..339
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 294..571
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
SQ SEQUENCE 579 AA; 63564 MW; A6359725BE69F9A8 CRC64;
MDVHLLVYDL SRGLARQMSL GLLGFQLDAV YHTSIELQGR EYVYDGGIIS IVPGTSHLGQ
PLERLHLGKT NLPMDVIGDY LESIRSIFTI EAYDLFRHNC NNFTDAFSNF LLGKGIPSHI
SQMPQAVLDS PFGRMLMPQL TQGVNASRQN GSILGLQQSA QPIAPVKVAS VKDVTGHAEL
SALLDQAKQS CAVVYFTSAT CAPCKMIYPL YDSLAEEFAG KATLIKIDIS QPQANLLASQ
YSISATPTFI TFLKGEQENR WSGADPATLR GNLQLLVQMA HPHHPHEKLR LPTFANPDTK
PVLFGKVPPM QKLMIKMGTE VSGKPEIQHL KRFIEDRANG EALDAVLPNM GHMASFLQES
VAKLPLEIMF TVVDLLRCAL LDPRVSGYFA EETAHKTVVG ILNAVNEQSE CPYALRLVTL
QMACNFFSTP LFPDEILRHE HLRGPITRLI STSFLDDNHS NTRVAASSLL FNIALADRRS
RLGEAKPSLP EDDLVELAAS VVEAVSQEET SQEALQGMLS ALGHLVYCTK LDGELADLLR
ALDAEGTVLE KKKTFPNEAL IAEVGSELLG KGLKMERLN
//
