ID   A0A0E0AFZ1_9ORYZ        Unreviewed;       974 AA.
AC   A0A0E0AFZ1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM07G03100.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM07G03100.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM07G03100.1}
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; A0A0E0AFZ1; -.
DR   STRING; 40148.A0A0E0AFZ1; -.
DR   EnsemblPlants; OGLUM07G03100.1; OGLUM07G03100.1; OGLUM07G03100.
DR   EnsemblPlants; OGLUM07G03100.2; OGLUM07G03100.2; OGLUM07G03100.
DR   EnsemblPlants; OGLUM07G03100.3; OGLUM07G03100.3; OGLUM07G03100.
DR   Gramene; OGLUM07G03100.1; OGLUM07G03100.1; OGLUM07G03100.
DR   Gramene; OGLUM07G03100.2; OGLUM07G03100.2; OGLUM07G03100.
DR   Gramene; OGLUM07G03100.3; OGLUM07G03100.3; OGLUM07G03100.
DR   eggNOG; KOG1870; Eukaryota.
DR   HOGENOM; CLU_001060_7_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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   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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF68; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          262..883
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  108888 MW;  87587C293054EEFC CRC64;
     MATAATAQAS ASSSTASTRG SPAASSSSHS AVCLVPFRWW ARVREEAPPE GGVRYAATAA
     ASPSSYYGLR LLHSFLHPDL VLRLERGGCR GTGAGAGGRS YALVPADELS RVLARQNSSL
     ALHNKHSFAE DSAGAYPLVL RISVRETSIL TVKISKKDNP VENYKRAYKI FNIDSQPVHV
     WDFSGQTNLI LMNEWNRSNH DCCHSELENI LEVQVYAMSD SLTSKIGGTS KEYTEQSSAD
     VNDMDVDLSY GSFGRSSSHG LIGLENLGNT CFMNSSIQCL AHTSKLVDYF LGDYDRDINR
     TNPLGLNGEL ALAFGELLRR LWNTERKPVS PHHFKAKIAC FAPQFSGFNQ HDSQELLAFL
     LDGLHEDLNQ VKCKPYEEAK DASGRPDKEV ADEYWSNHLA RNDSVIVDTY HGQYKSTLTC
     PTCSKTSVTF DPFMYLSLPV PSTAKRTMTV TVFSTDGSIE PISYDVTVPQ FGSLNDLVQA
     LSSACSLGDD EILLITEVYN NRILRYLEEP SDSVSLLRDG DKLAAFRLPR KYEKSPVVVF
     THQYFDERSS VDNITPQMKE FEAPLLAVLP ERANGLTLKN IYLKLLEPLR FSKSTSSLND
     SGRCNSGCAA VMMDATPDSD SKFQSAPSEN APESSQSETI ECQMTEGPSE SNIGDTTDSD
     REAHMEEFEF YLINGRGEFQ QTRIQTDEVD LQTTPNRLLI NVHWQQNAGQ YDTSMLKSLP
     EIHKLELIPK GNEDSVALHG CLEAFLKEEP LGPEDMYCPC CKKHQQAMKK LDLWRLPEVL
     VIHLKRFSYT QFTRNKLETF VDFPISDLDL SSYIIDKSEL SDCHYRLYAI SNHYGNMGGG
     HYTASIYHEE GKGWYKFDDE CVRPITEDSI KTPAAYENIY MIISDSDLSP ELCCLTNNIR
     LLLSSVLFGL IALDKYSDIS QQHLFCLDIS QDQTRLDGHQ SFMCNKVSWT NCVLNDNSIP
     QGRTDFDDHE GKKR
//