ID   A0A0E0QKY5_ORYRU        Unreviewed;       335 AA.
AC   A0A0E0QKY5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G22180.3, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI08G22180.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       and may therefore play an important regulatory role at the level of
CC       protein turnover by preventing degradation.
CC       {ECO:0000256|RuleBase:RU367104}.
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:RU367104};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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DR   AlphaFoldDB; A0A0E0QKY5; -.
DR   EnsemblPlants; ORUFI08G22180.3; ORUFI08G22180.3; ORUFI08G22180.
DR   Gramene; ORUFI08G22180.3; ORUFI08G22180.3; ORUFI08G22180.
DR   HOGENOM; CLU_046927_0_0_1; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd22760; OTU_plant_OTU4-like; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR047947; OTU4_OTU.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR   PANTHER; PTHR13312:SF5; UBIQUITIN THIOESTERASE OTU; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW   Hydrolase {ECO:0000256|RuleBase:RU367104};
KW   Protease {ECO:0000256|RuleBase:RU367104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW   Thiol protease {ECO:0000256|RuleBase:RU367104};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT   DOMAIN          173..311
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
SQ   SEQUENCE   335 AA;  37095 MW;  8775080577CD2D8F CRC64;
     MSFDIEFGHS CTADIGWTGC GSTHLQSICG DLLNFHGGLT QSLGLRKCSR SQTSSYNVKL
     GLVDCSLHRN IKSSDRPSLR YFVSLVGRQF RCGLSGKEGS LNMKLDMPSR DNFSSMSWKW
     RGLHQKIGGT TSGLCLGFAV SGIANAEVPV EISISNSAAS TSSTHGKEVY TDYSVTGIPG
     DGRCLFRSVI HGACIRAGRP IPNEDLQRKL ADELRAMVAD EFVKRREESE WFIEGDFDTY
     VSHIRHPHVW GGEPELFMAS HVLEMPITVY MHDEDAGGLI TIAEYGQQYG KEDPIQVLYD
     GFAHYDAVQI PAKKCSREMT SEFLKFQGSN GRIWS
//