ID A0A0E0M5M7_ORYPU Unreviewed; 961 AA.
AC A0A0E0M5M7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G02440.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC10G02440.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC10G02440.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
CC {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; A0A0E0M5M7; -.
DR STRING; 4537.A0A0E0M5M7; -.
DR EnsemblPlants; OPUNC10G02440.1; OPUNC10G02440.1; OPUNC10G02440.
DR Gramene; OPUNC10G02440.1; OPUNC10G02440.1; OPUNC10G02440.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_0_1; -.
DR OMA; PCHAQQS; -.
DR Proteomes; UP000026962; Chromosome 10.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF46; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10-RELATED; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 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 Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 18..138
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 312..938
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 69..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 108446 MW; 3CC848D4BE4CA0CD CRC64;
MTIPSAEGFL QAASCLPCTA AEERELVVAL TREAEENVKD GDLRYLVSHS WWINWQHYVG
LIKPDENDTD MLPQATSRPG EIDNSKLVSE ESSSIGDEPE LQRTLREGDD YALVPQEVWR
KLHEWYKGGP ELSRRVICSS PTSRSYIVDV YPLRLKLFDE RDSLERIIRI SRKAKVSELY
SLVCSLMSVE QSKIDIWDFY QKTKGKKLIN LNETVEEAQL MMDQEIIVEV KADDAWCSDL
GTRSNNELAL IPLEPSTSSF SIAGGPAFSN GFSSGFGSSF SQDNSFSPLL RDTEDGYSIF
SNGTKDDIHG LSGLHNLGNT CFMNSAIQSL VHTPPLVEYF LQDYSREINT ENPLGLQVMG
VLVLICSKDC QLMIIMVISE NISIEQGELA IAFGELLRKL WSAGRTSVAP RAFKTKLSRF
APQFSGYNQH DSQELLAFLL DGLHEDLNRV KKKPYIEAKD ADGRPDEELA EECWNYHKAR
NDSIIVDKFQ GQYKSTLVCP DCKKISVTFD PFMYLSLPLP STVTRMMNVT VFSGTGDALP
MPYTVKVQKN GVCGDLVKSL SVMCCLQSSE TLLLAEVYDH RIYRYWNSSE PLCHIKDEDK
LVAYRLPVGS ENLLRVEILH RVVDRYTSES MFNLSRKLIG SPLVTCIPND STRKADIYAI
VSSLLAPFVR AKVHTLDESA TKLNSNGPSL DGIVLTDNGA TCEEGVSTSN VDEEAADEEV
LPFQLWLTDD KANKREHIDA DSNGVPGSTM RLLMDWSDRE HEVYDIKYMD ELSVVFKPGF
VSKKNRQEAV NLFSCLDAFL KDEPLGPDDM WYCPRCKEHK QASKKLDLWR LPEILVVHLK
RFSYSRFMKN KLDTFVNFPI HDLDMSRYAN HSRGDQPPIY ELYAVINHYG GMGGGHYSAY
AKLVEEDSWY HFDDSHVSSV GEEDIRTSSA YLLFYRRVGS SSCSVSKNVA VDTDMVDSLD
T
//
