ID A0A0D3B2X2_BRAOL Unreviewed; 861 AA.
AC A0A0D3B2X2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:Bo3g019020.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo3g019020.1, 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:Bo3g019020.1}
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|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|ARBA:ARBA00000707,
CC 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 AlphaFoldDB; A0A0D3B2X2; -.
DR STRING; 109376.A0A0D3B2X2; -.
DR EnsemblPlants; Bo3g019020.1; Bo3g019020.1; Bo3g019020.
DR Gramene; Bo3g019020.1; Bo3g019020.1; Bo3g019020.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_013307_0_0_1; -.
DR OMA; GHEKRCH; -.
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; cd02661; Peptidase_C19E; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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 PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 135..438
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 643..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 96051 MW; CACAA4743907ED59 CRC64;
SDHSLFEISR KSYRLYYLSL HSFFTPDKSQ NRVSCLNSNR RFLWICRMEA SSNGSCAVSS
VFRKIEFHPA RKPFNGFSNG KSDFKIETLN PSSSSASKQA FFSSPSFKKR DGSDLLENGL
DRELTFNRTI RKIGAGLENL GNTCFLNSVL QCLTYTEPLA AYLHDVGHEK RCHVAGFCAL
CAMQKHVRNA LQATGKILAP KYLVSNLRCV SRNFRNCRQE DAHEYMVNLL ECMHKCSLPS
GVSSESSDAY RSSLVHKIFG GSLRSRVKCA QCSHSSDKFD PFLDLSLDIS KADSLQRALT
RFTAVELLDD GAKVYQCERC KQKVKATKEL TVFKAPYVLT VHLKRFEAHR SEKIDKKVEF
ASAVDMKPFV SGPCEGNLKY TLYGVLVHYG RSIHSGHYAC FVRTSSGMWY SLDDNRVLQV
SEKNVFNQKA YMLFYVRDRQ NTAPKNVVPM VKKESLPTAR ASMIISSNGN DQVSGSTVMK
ASILNGLGAN GRAPLRSCDQ GAPAVFNRKD LNAKETQKDP PSSVEAKEIL KRENGLSATA
VLSQKDSNAR ENLQKELPIS QANGERSLVK EKIKAPCATL PGKAAPLLDG SRNAQILVNL
PTSVANKDEE TLTTPRKTRK GKTKTLQVGL KLFKLALGVR KKMKQKRGRS SAVKVIPEEL
RSKKGATDQE RSTSEITSEV ASGSSCLPGK DNIVSVHNER RRNSNGNMLL GSATGDLKER
TNENGAVLAS DQKPPLRSSD LSKASQIAKR KRESSKDEQI VLQKDEPTVL TRGLPETVVA
KWDEEVSASK KMGMNEGTRI GYVADEWDEE YDRGKKKKIR IKEEMYKGPN PFQMIASKKQ
QTDTKKKWTQ RMNTAKTGFR I
//
