ID A0A0D3EK94_9ORYZ Unreviewed; 775 AA.
AC A0A0D3EK94;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART01G05020.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART01G05020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART01G05020.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART01G05020.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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 ECO:0000256|PIRNR:PIRNR016308};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308}.
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DR AlphaFoldDB; A0A0D3EK94; -.
DR STRING; 65489.A0A0D3EK94; -.
DR PaxDb; 65489-OBART01G05020-1; -.
DR EnsemblPlants; OBART01G05020.1; OBART01G05020.1; OBART01G05020.
DR Gramene; OBART01G05020.1; OBART01G05020.1; OBART01G05020.
DR eggNOG; KOG0944; Eukaryota.
DR HOGENOM; CLU_009884_1_0_1; -.
DR Proteomes; UP000026960; Chromosome 1.
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:UniProtKB-UniRule.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 1.
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 Hydrolase {ECO:0000256|PIRNR:PIRNR016308};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308}; Protease {ECO:0000256|PIRNR:PIRNR016308};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
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..775
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 589..630
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 650..690
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 775 AA; 86359 MW; C08595A6B026E8C3 CRC64;
MDLLRSHLHK VRIPEPGSCI HKDECCVSFD TPRSEGGLYV DMTSFLGFGR EHVAWNYEKS
GNPVYLHIVQ RRKPEPDDEA DRPLKKPTLL AIGVEGGFTD QEPEYNEAFE 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
WVPKKLDVYV DVPDIIDISH MRSKGIQPGE ELLPEGASGD NKAEPVHPVA SEDIVSQLAS
MGFNYLHCQK AAISTSNTGV EEAMNWLLSH MDDPDINDPI SKDSQAAEQT VDETSVQTLV
SFGFQEDVAR KALAASGGNI ERATDWIFSH PEAFSSVPTD SSTSNMEDDD AHIPDGSGRY
KLMAFVSHMG TSTHCGHYVA HVLKDGRWVI FNDSKVAASV DLPKDMGYLY FFQRI
//
