ID A0A2T4BDI4_9HYPO Unreviewed; 1633 AA.
AC A0A2T4BDI4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BBK36DRAFT_1158222 {ECO:0000313|EMBL:PTB67384.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB67384.1, 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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KZ680211; PTB67384.1; -; Genomic_DNA.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000241546}.
FT DOMAIN 253..368
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 610..1440
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1204
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 178675 MW; 6E96BDC90B919A61 CRC64;
MSEQVQVPGH PHRLSRQPAP AVFPPELPGQ LTVKTSSSKK RKLARPLTID FDAPTSPSPD
TAIPSCEPDD DAALSFSATP IASGLEAPLY VRAGSVTASS VPPRLQTQAQ AQIASSLVSA
DYASSVASSP GTSFYPEPSI DSERGGDDAS SVRTYARSQS PFLISRRALV NGDADLPQRS
SSPLKRRASS MDPETAPNKN GDAATSAGDV EMTSSSNPSA ELPRAMSVDI EASDSKPSAN
NGADAAAQSA PPPPLIEQVK IIEMLLKASA EKLPQEGDQA YIVSRTWVDK ALSLRSGKAD
VTEVSLGPVD NSDIIEEVIQ EPGREDFVRL KPGLDQQSFE LFPEDAWKLV MDWYGMVEGQ
KPIVRTAINT AADAQSPTEV VYELHPPIFR VHRLWSVVSP LPIEQTLKAE NPPPLALVRS
RKTHAQAFIK DIKRLAGIPM DRKVRLWLVD TESLKANQAP AKASTTAKAP ALLTTPPDSP
GREDSDGAAE SGWSHLLVDV ATFGSVPRDS RRVATLEDHT VNPNYNGSAS IQLFDLVTDQ
TLIVDEMVNK GLWVSTCTSR SLVEKAIPTR TNDTALAKPL NNRTSPSSSE GPTTRGRMQK
KRNGRSVGAV GLHNLGNTCY MNSALQCVRS VEELTKYFLT DAYAAELNKS NPLGYNGKVA
MAYGALLREI YDEGRGSVSP REFKNTVGRC RSTFAGWGQQ DSQEFLGFLL DALQEDLSRI
KKKPYIEKPD STDDMINNPE AIKEMADKVW DITRKRDDSV IADLFTGMYK STLKCPECGK
ISITFDPFNN LTLPLPVENM WSKTVKFFPL NDVPVMFEVE LPKHSSIESL KSFLSIRTGV
PPNRLMGAEE FKDRFFKIYD NSGDVSEEIG ANDVATFHEL EAVPTNWPAK GYQKKPRSML
DLDDTPADAT EEWNDPKYDT MVVPVLHRRP FSTGKVPEGT SPPHFITLTR EEASSYDMIK
RKVLERVATF STWSKFKEQQ NAEGSEADMV IATASDADSS GDGKVVANSV EGEDDIVDVT
MKDASSTASA NATVMPPPEL PLPNQPQLLR QFNSQRPKFV QPGEFLGPEL QGLFELSYFA
NRTDGTVPTG WTNVDNNKTL PKLADRIPEA QREEEDQPSP ESWNSTASGN EESSNEEENP
QPESSQTRMA DESSEEDVPH GARTLARTGA NRPQKLGTGG RKKFKNHKAY GKKGNKRRDK
QMRAGKHVQR SPVVESEPTP PAVADGGPLI RLYEGLVVDW SEEAWETVFG YTGKKQDASQ
GAKTFVDLET INDPALKISQ RKRQSRRSRG ITLDECLDEF ERAEVLSEQD MWYCPRCKEH
RRASKKFDLW KSPDYLVAHL KRFSSSGWRR DKLDVLVDFP IEGLDLTSRV IQKEEGKEEI
YDLIAVDDHY GGLGGGHYTA YAKNFVDGRW YNYNDSSVSA VSDPSSVVTS AAYLLFYRRR
TSGHLGGPRF AKIFEKYNTD TSGDDEGESD DGLGRTVGSS SAAPHTTIKS LSDSHEAELP
PYEEAIRSIE DEGLGASGSY QIAAPKFDMT QSWSFNNLDG SGADGSTAAD YASDDAQFDS
SADERGGSRE DLFEADTHMA SVGSVNGFTN GEAASPAGAH EEVLTVPTGP SGGEDEDEVA
EIHIEGDNVA RSE
//
