ID B8B7E9_ORYSI Unreviewed; 885 AA.
AC B8B7E9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=OsI_24972 {ECO:0000313|EMBL:EEC81550.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC81550.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC81550.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 EMBL; CM000132; EEC81550.1; -; Genomic_DNA.
DR AlphaFoldDB; B8B7E9; -.
DR STRING; 39946.B8B7E9; -.
DR EnsemblPlants; BGIOSGA025185-TA; BGIOSGA025185-PA; BGIOSGA025185.
DR Gramene; BGIOSGA025185-TA; BGIOSGA025185-PA; BGIOSGA025185.
DR HOGENOM; CLU_001060_7_0_1; -.
DR OMA; TGQLVIM; -.
DR Proteomes; UP000007015; Chromosome 7.
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:UP000007015};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 262..885
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 885 AA; 98973 MW; 1D992A4F2BF2BDAA 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 IDNITPQMKE FEAPLLAVLP ERANGLTLKN IYLKLLEPLR FSKSTSSLND
SGRCNSGCAA VMMDATPDSD SKFQSAPSEN APESSQSETI ECQMTEGPSE SNIGDTTDSD
REAHMEEFEF YLINGRGEFQ QTRIQTDEVD LQTTPNRLLI NVHWQQNAVG QYDTSMLKSL
PEIHKLELIP KGNEDSVALH GCLEAFLKEE PLGPEDMWYC PCCKKHQQAM KKLDLWRLPE
VLVIHLKRFS YTQFTRNKLE TFVDFPISDL DLSSYIIDKS ELSDCHYRLY AISNHYGNMG
GGHYTASIYH EEGKGWYKFD DECVRPITED SIKTPAAYVL FYRRE
//
