ID A0A2T4BJY6_9HYPO Unreviewed; 667 AA.
AC A0A2T4BJY6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:PTB69637.1};
GN ORFNames=BBK36DRAFT_63694 {ECO:0000313|EMBL:PTB69637.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB69637.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., 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.
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DR EMBL; KZ680208; PTB69637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BJY6; -.
DR OrthoDB; 1749511at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02662; Peptidase_C19F; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF936; C-TERMINAL HYDROLASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000241546};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..629
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 270..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 73090 MW; 8242C0B6AA0811FA CRC64;
MNSRQRGFDT FYDDQVAARR QFYARRETAV NRINDVAVLV TVAALAVTLL AKFYSPDGSL
EGIFSLLGNF LWDALVFLTP APLLFALDNW MDSSTTRPMR DTTNQSNHAA KSEAMRRVMG
LDRQDGVMNS VLRARTRALS MTGSVLGLKT DSDRPAGLGN RDNSCYQNSV LQGLASLQSM
PDYLSACLKG LEEAGHGADG NVAHTLRALI ADLNDVSNNG KTLWTPSVLK SMNTWTQQDA
QEYYSKVLDD VEKAAALAAK KLASEKLAGL EGGDVNNTDE GSTSEHSDDS GYHSQLSSSI
ADSKRMLRNP LEGLQAQRVA CVQCGHSEGL SMIPFNCLTL SLGLDKNHHD LYERLDAYSK
LEAIEGVECA KCTLLKAQRL LTKLVERMRS EGATDDKLAE PLRRLEAVQL ALEEDQFDEE
TIKDRCKIAA QSRVNVTKTK QIVVARPPQS LAIHVNRSVF DPSTFNMIKN SAPVSFPMTL
DLGPWCLGSA GPVKSSSKET ADVKKGKGVE ERWPLEPMSS MVAGDMGESR LTGPIYELRA
VVTHYGRHEN GHYICYRKYP PLTSPSVGHA GGKPAEPSAD ETTTTDEKPS YTDRDSTWWR
LSDHNVSPVN EETVMSLSPG VFMLFYECVD ASMILHCEEE NEATTPASIA SQAATKQDEG
SSVLLGR
//
