ID   A0A2T4AY15_9HYPO        Unreviewed;      1297 AA.
AC   A0A2T4AY15;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=BBK36DRAFT_152423 {ECO:0000313|EMBL:PTB61943.1};
OS   Trichoderma citrinoviride.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB61943.1, 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};
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DR   EMBL; KZ680226; PTB61943.1; -; Genomic_DNA.
DR   OrthoDB; 1423057at2759; -.
DR   Proteomes; UP000241546; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02666; Peptidase_C19J; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR025305; UCH_repeat_domain.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF13446; RPT; 2.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000241546}.
FT   DOMAIN          604..1213
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          292..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1222..1297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..733
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1222..1251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1297 AA;  145511 MW;  75498B62BE48DF52 CRC64;
     MGARYDLRSQ DPEPLAYAAL PGTQSGFVPT NPTPMKSALV GRDVIGCHPS RWIYELINNN
     FTVCDLFQRA RNANLDSHYN WEHPHQLVIN GNQSYSTASS KVLSAICLDC HFHFMFRVEW
     EREQEDFSCH HSQSQWPLGD TQFPWHHLAW ACSEDEKRIT QERSKYYPLL AREFFVCTAA
     PCTVQITLEV SEPRMPSSWV KLLLDHETIL QQLKAAREDE PARYESATDD WIYQAPSNLN
     TYLKNLLEAT PDSARSISKR NKRFYVLFGP RCFHIFRELE FKEVVDMQDG VDEGSFTPTA
     PPPAEGPSKS TEINTYRAYL EDVRSEVQNL IFKSGHTAES PTFCIAALHN HLGCAEVPRV
     SENALVNLER YKLMGVLPTQ SIEIVVNAYK RQWDLLPSRR RDLVEALMAI ANDTNDDLLS
     DYAITQSSVF ESQLQRHSGD DDDGLVAQAL EYFSLSPPNT HSADAILQAF REKIARDPFD
     ASTARSMLLL IARSSKDDSY QMKLVLEADS KMTLETCKVV LGLKTLDGPW EDMVRATKEL
     LNNASSSEAK ATYLDALDSI AEHTASPSLK QAVLELRNEF NLGISGSDGT VSSDPRATNL
     DLPVGLHNIG NTCYLNSLLQ YLFTVKPIRD IVFNYDSLRL GLDDESIRER RLGGNKMQMD
     RGEAVVAQAF AEEMATLFET LRTSDRTATR PSQRLANAVL LSTHTLLSSP KQPSETPTAP
     NPPPLPARPS PAPPTNSYDD VNMVNVSVQA VSDSLETQSS SSTQTLVNQD DARSDHSYEK
     VETIVEEASQ PVQVATGGSG DDISMVEAPL DDKKPTVLMD LDESKDTPIS AGQVNHDVDM
     TDAEKPETVD QKVLNALEHQ KRSSGTDQQD VEEVMGSILN RLQAAIRPTS VDPETGIQLE
     KIMETFFVTT VNYTKKFDEQ EYQHEISFDR SITAFPATEG PCSLYDALGR NFDQQILEDS
     KLSRYTAIKT LPPVLHILIQ RSQSMGNKNG NPVVIPETLY LDRFMDAPHD SPIFRQRVQD
     WITAERIGDL KSQRSKVVTN PRYMTFLQTY ESGDGTTEDP TNEAPMGAEE PPKQEEPLEN
     WDFDGPVEDD FLLVTAENTK KAAASGESVT KLENIQKTHA TVLEMMEKEL SERQETLEKS
     LNSQKQIAYR LHAVICHRGH LMSGHYWVWI HDFEANVWRW YNDADVKENK DTAEVLRTLS
     TSGEPYYLCY VRDEDKEQYV SIPKREVPKE KAADKQQDGE DGSKVEEEAP ANEAEATAPL
     AVADKDGDVE VSDARPEDGP EVVPAVDAVP EEPREES
//