ID A0A0D3B809_BRAOL Unreviewed; 906 AA.
AC A0A0D3B809;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=106335548 {ECO:0000313|EnsemblPlants:Bo3g044810.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g044810.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo3g044810.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo3g044810.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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|ARBA:ARBA00037450, 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 RefSeq; XP_013629547.1; XM_013774093.1.
DR AlphaFoldDB; A0A0D3B809; -.
DR STRING; 109376.A0A0D3B809; -.
DR EnsemblPlants; Bo3g044810.1; Bo3g044810.1; Bo3g044810.
DR GeneID; 106335548; -.
DR Gramene; Bo3g044810.1; Bo3g044810.1; Bo3g044810.
DR KEGG; boe:106335548; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_0_1; -.
DR OMA; PCHAQQS; -.
DR OrthoDB; 653068at2759; -.
DR Proteomes; UP000032141; Chromosome C3.
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 Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
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:SF46; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10-RELATED; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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:UP000032141};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 20..129
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 298..889
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 906 AA; 101998 MW; 87DB2FC6CB6BEE05 CRC64;
MTIANSTDFM VENAVCDFPS TPEEERRIVS ELTTESEDNL KEGNLYFVIS KRWYTRWEKY
VEQPTTNGGC ESPRPGPIEN SDIIEDTSDD PQLRRLLVEG EHYVLVPQQV WNRLAEWYSG
GPPIPRKLIC QGFYTRSYSV EVYPLCLLLT DARDDSITAI RLGKQASIKE LYDKVCAMTE
VSQEKARIWD YFGKRKGQLL DPSSNKSLEE SSLHMDQDIL LEVDGSSSSQ YAMSSAGNEL
ALVPLEPSRS LVTIAGGPTL SNGHSTTSKF SLFPRITSED DGCDSLSILG KGERGGLAGL
SNLGNTCFMN SALQCLAHTP PIIEYFLQDY SEDINRDNPL GMCGELAIAF GELLKKLWSS
GRNAVAPRSF KTKLARFAPQ FSGYNQHDSQ ELLAFLLDGL HEDLNKVKRK PYIELKDSDS
RPDDEVAEEL WNYHKARNDS VIVNVCQGQY KSTLICPVCG KISITFDPFM YLSLPLPSTL
TRQITVTLFY CDGSHLPMQY TVTVPKYGSC RDLITALGTA CCLTNDESLL LAEIYDHKVF
RYFENPLESL NLIKDDEHIV AYRMKQMQKG SGKAKLEILH GGQERAVLES VRGRDVKLFG
TPFVTYVNTE RLSGPDIDAV ISGFLSPLHR VQASSKIHNG VENGHLPDAD TVEASGSISS
PDTEIEDACD RELSFRIFLT DERGLDFKPL KSDSSLKPGI VTRVLVEWNE NEHENYDSSY
LCDLPEVHKT SFSAKKTRQE AISLFSCLEA FLAEEPLGPD DMWFCPGCKE HRQANKKLDL
WKLPDILVFH LKRFTYSRYL KNKIETFVDF PINDLDLSKY VKNKNGQSYL YELYAVSNHY
GGLGGGHYTA YAKLIDDNKW HHFDDSHVSS VNESEIKNSA AYVLFYRRVG SKTETQSAEV
SMADMD
//
