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Database: UniProt
Entry: A0A0E0IEX0_ORYNI
LinkDB: A0A0E0IEX0_ORYNI
Original site: A0A0E0IEX0_ORYNI 
ID   A0A0E0IEX0_ORYNI        Unreviewed;       787 AA.
AC   A0A0E0IEX0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   31-JUL-2019, entry version 28.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA08G24270.1, ECO:0000313|Proteomes:UP000006591};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA08G24270.1, ECO:0000313|Proteomes:UP000006591}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA08G24270.1,
RC   ECO:0000313|Proteomes:UP000006591};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA08G24270.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA08G24270.1};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-
CC       ubiquitin 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,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|RuleBase:RU366025,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
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DR   STRING; 4536.ONIVA08G24270.1; -.
DR   EnsemblPlants; ONIVA08G24270.1; ONIVA08G24270.1; ONIVA08G24270.
DR   Gramene; ONIVA08G24270.1; ONIVA08G24270.1; ONIVA08G24270.
DR   OMA; VAYVRQS; -.
DR   Proteomes; UP000006591; Chromosome 8.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 2.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006591};
KW   Hydrolase {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044331}; Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       63    125       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      209    271       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      301    785       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      63    125       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   ZN_FING     209    271       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION        1     29       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      145    168       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     21       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   787 AA;  86161 MW;  0D706DFD46421E57 CRC64;
     MDEKARAGKS PRLKRRSSGS DPLEEAAGLT SDSSSIRRCR HVSCDQTTID LGIALIKASI
     DGPACDSFKC GTTEERGILV CLDCGSSLCA LHARWHARMN RHWVALMHKR PNVAYCFSCE
     DAYFISRVRF GGTADEDFFP ISTPKKDEKG NKVDNEAGGH ASAATGAGSG GGTMAVLTSN
     VSPQRCCHVY KKGDVARVIK RIMFSDIAAA CSDSMCDTTG RSLILVCLGC ENPFCSGHAD
     VHAKSTKHWN YLIYQSPYIV CCFVCKGIVF LGGQDKEEMP VDNATAGDAS GSVIEHAHAI
     RGIPNLGNTC YLNSLVQCLL ALGRLRARML RPEDTTGRLG TVLRYLFQDT DSVNNSGGLL
     NPSGLLRRVR MFVPESQVTS MHDSHEALCR LRTNLDEEER LMKYGALSVE APTVIDSIFG
     GQLSVTKTCK CCSLSSVSLG IVFHDLSMPI PPKKPLAKRV EPLWITKGRR SQRKRNTEKT
     HTIAEDGDSQ NVMVKTSEPL GVDSTKVEQI SQSKDAVQGP LQIQKDKVQG KAVDFLPQNV
     LSDAKVEGMD ATRADSHIPE YLAPAPTFSP LREDDARVAL GIDVEKNGSA VRPEVSTEAK
     VTTSSAKVTA KDKGRTRSSN IICNKAQDIN SLASIEECLE LHFEAETVEL TCENCSKFAQ
     KLNKSVIQTR LSLLPPVLVI HLKRSLLQSD KVKGHVSFKE ILDVGLFMDP SSVDKDNSIY
     RLAGVIEHHG HGKDSGHFVA YVRQSRPQQT NGSSSWFWAS DTDIREVPLE EVLKCEAYLL
     FYERMEG
//
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