GenomeNet

Database: UniProt
Entry: A0A0D9Y424_9ORYZ
LinkDB: A0A0D9Y424_9ORYZ
Original site: A0A0D9Y424_9ORYZ 
ID   A0A0D9Y424_9ORYZ        Unreviewed;       771 AA.
AC   A0A0D9Y424;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
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:OGLUM01G05450.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM01G05450.1}
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:OGLUM01G05450.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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|ARBA:ARBA00000707};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0D9Y424; -.
DR   STRING; 40148.A0A0D9Y424; -.
DR   EnsemblPlants; OGLUM01G05450.1; OGLUM01G05450.1; OGLUM01G05450.
DR   EnsemblPlants; OGLUM01G05450.2; OGLUM01G05450.2; OGLUM01G05450.
DR   Gramene; OGLUM01G05450.1; OGLUM01G05450.1; OGLUM01G05450.
DR   Gramene; OGLUM01G05450.2; OGLUM01G05450.2; OGLUM01G05450.
DR   eggNOG; KOG0944; Eukaryota.
DR   HOGENOM; CLU_009884_1_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:1990450; F:linear polyubiquitin binding; IEA:EnsemblPlants.
DR   GO; GO:0061815; F:Met1-linked polyubiquitin deubiquitinase activity; IEA:EnsemblPlants.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:EnsemblPlants.
DR   GO; GO:0071370; P:cellular response to gibberellin stimulus; IEA:EnsemblPlants.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR   GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:EnsemblPlants.
DR   GO; GO:0048767; P:root hair elongation; IEA:EnsemblPlants.
DR   CDD; cd02658; Peptidase_C19B; 1.
DR   CDD; cd14295; UBA1_atUBP14; 1.
DR   CDD; cd14388; UBA2_atUBP14; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 2.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR016308-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          159..269
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          311..771
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          585..626
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          646..686
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ   SEQUENCE   771 AA;  85877 MW;  E7D92B8EA934D499 CRC64;
     MDLLRSHLHK VRIPEPGSRI HKDECCVSFD TPRSEGGLYV DMTSFLGFGR EHVAWNYEKS
     GNPVYLHIVQ RRKPEPDDEA DRPLKKPTLL AIGVEGGFTD QEPEYDEAFE IVILPEFTSL
     PFPSIDLPEK VRIAVDKVIL AESADRKQQL ASWVADKKKV SAHAMDLKQL DNGVIVPPTG
     WKCSKCDKTE NLWLNLTDGM ILCGRRLWDG SGGNNHAIEH YEQTKYPLAV KLGTITADLE
     AADVFSYPED DSVEDPLLAQ HLSHFGIDFS SLQKTEMTTA ERELDHNTNY DWNRIQESGK
     DAELLYGPGY TGLVNLGNSY FEKQSLKAAF AIAPADPTLD LNMQMTKLAH GMLSGKYSVP
     NQEGQEGIHP RMFKTVIAAK HPEFSSMRQQ DALDFFLHLI DQVDQANTGN HELNPFTGFK
     FIIEERLQCP SGKVSYNKRS DYILSLNIPL HEATNKEQLE AFHEKKAAMD LDGKEVSNEE
     IVRPRVPLEA CLASFSGAEE VPEFYSTALN SKTTAIKTAG FKTFPDYLVL QMRKFVMEAG
     WVPKKLDVPD IIDISHMRSK GIQPGEELLP EGASGDNKAE PVHPVASEDI VSQLASMGFN
     YLHCQKAAIS TSNTGVEEAM NWLLSHMDDP DINDPISKDS QAAEQTVDET SVQTLVSFGF
     QEDVARKALA ASGGNIERAT DWIFSHPEAS SSVPTDSSTS NMEDDDAHIP DGSGRYKLMA
     FVSHMGTSTH CGHYVAHVLK DGRWVIFNDS KVAASVDLPK DMGYLYFFQR I
//
DBGET integrated database retrieval system