ID   A0A0D3F1K1_9ORYZ        Unreviewed;       406 AA.
AC   A0A0D3F1K1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
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:OBART02G06090.1};
RN   [1] {ECO:0000313|EnsemblPlants:OBART02G06090.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G06090.1};
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:OBART02G06090.1}
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|RuleBase:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|RuleBase:RU361215}.
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DR   AlphaFoldDB; A0A0D3F1K1; -.
DR   STRING; 65489.A0A0D3F1K1; -.
DR   PaxDb; 65489-OBART02G06090-1; -.
DR   EnsemblPlants; OBART02G06090.1; OBART02G06090.1; OBART02G06090.
DR   Gramene; OBART02G06090.1; OBART02G06090.1; OBART02G06090.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_0_1_1; -.
DR   Proteomes; UP000026960; Chromosome 2.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR   Gene3D; 1.20.58.860; -; 1.
DR   Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF30; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW   Protease {ECO:0000256|RuleBase:RU361215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Thiol protease {ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          80..279
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   DOMAIN          343..388
FT                   /note="Peptidase C12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18031"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          292..319
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   406 AA;  45508 MW;  2E0CFAA68899DFC3 CRC64;
     MGPCPTPSLQ SHPSPTTHAR SPPTRRRRRI RFAPSAAPRA ASVDAGPTRA VREGGGGGGA
     SAGSDHLQEG AQGFFFDMSW AAIENDPGVF TELLQQMQLK GLQVDELYSL DLDALNDLQP
     VYGLIVLYKW QPPEKDERPI KDPIPNLFFA KQIINNACAT QAIVSVLLNS PGITLSEELK
     KLKEFAKDLP PDLKGLAIVN SESIRLASNS FARPEVPEEQ KSSVKDDDVY HFISYVPVDG
     VLYELDGLKE GPISLGKCPG GVGDIGWLRM VQPVIQERID RFSQNEIRFS VMAILKNRRE
     KFTLELKELQ RKRENLLAQM GDPSANRHAP SVEHSLAEVA AHIEAVTEKI IMEEEKWKKW
     KTENIRRKHN YVPFLFNFLK ILEERQQLKP LIEKAKQKSH SSANPR
//