ID A0A0Q3EJW1_BRADI Unreviewed; 1117 AA.
AC A0A0Q3EJW1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=100834129 {ECO:0000313|EnsemblPlants:KQJ86692};
GN ORFNames=BRADI_4g07167v3 {ECO:0000313|EMBL:KQJ86692.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ86692.1};
RN [1] {ECO:0000313|EMBL:KQJ86692.1, ECO:0000313|EnsemblPlants:KQJ86692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ86692.1,
RC ECO:0000313|EnsemblPlants:KQJ86692};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ86692.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ86692.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ86692}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ86692};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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}.
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DR EMBL; CM000883; KQJ86692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3EJW1; -.
DR EnsemblPlants; KQJ86692; KQJ86692; BRADI_4g07167v3.
DR Gramene; KQJ86692; KQJ86692; BRADI_4g07167v3.
DR Proteomes; UP000008810; Chromosome 4.
DR ExpressionAtlas; A0A0Q3EJW1; baseline.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00121; MATH; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF881; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 55..180
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 200..524
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 131270 MW; CF29CA1B6965D6B5 CRC64;
MTMMTPPPLE QQEDEEMLVP HQELPAADAA QPMEVVAQTE PVSMAENQPP EDPQTSRFTW
TIDNFTRLSG KKHYSDVFVV GGFKWRVLIF PKGNNVEHLS MYLDVADSGN LPYGWSRYAQ
FSLAIVNQVH QKYTTRKDTQ HQFNARESDW GFTSFMPLSE LYDPSRGYLL NDTVVIEAEV
AVRKMVDYWT YDSKKETGYV GLKNQGATCY MNSLLQTLYH IPYFRKAVYH MPTTENDMPS
GSIPLALQSL FYKLQYSDNS VATKELTKSF GWDTYDSFMQ HDVQELNRVL CEKLEDKMKG
TVVEGTIEQL FEGHHINYIE CINVDYKSNR KESFYDLQLD VKGCRDVYAS FDKYVEVESL
DGDNKYQAEQ HGLQDAKKGV LFLDFPPVLQ LQLKRFEYDY MRDTMVKIND RYEFPLQLDL
DRDDGKYLTP DADRSIRNLY TLHSVLVHSG GVHGGHYYAF IRPTLSDQWY KFDDERVTKE
DTKKALEEQY GGEEELPQVN PGFNNTPFKF TKYSNAYMLV YIRESDKEKI MCNVDEKDIA
EHLRIRLKKE QEEKEHKKKE KAEAHLYTII KVARDEDLKE QIGKNIYFDL VDHEKVRSFR
IQKQLPFTSF KEEVAKEYGI PVQSQRFWLW AKRQNHTYRP NRPLAPHEET QSVGQLREVS
NKAHNAELKL FLEVELGLDL RPIRPPEKSK EDILLFFKLY NPEKEELRFV GRLFVKALGK
PSDILTKLNE MAGFSPNEEI ELYEEIKFEP HVMCEHIDKK LTFRSSQLED GDIICFQKPS
VPDADTQLRY AEVPSFLEYV HNRQVVHFRC LEKPKEDDFC LELSKLHTYD DVVERVASQL
SLDDPSKIRL TSHNCYSQQP KPQPIRYRGV EHLLDMLVHY NQTSDILYYE VLDIPLPELQ
CLKTLKVAFH HATKEEVVIH SIRLPKNSTI SDVITDLKTK VELSNTDAEL RLLEVFYHKI
YKIFPLQEKI ENINDQYWTL RAEEIPEEEK NLAPHDRLIH VYHFMKDPNQ NQIQNFGDPF
LLVIREGETA SEVMERVRRK LRVLDEEFSK WKLAFISMNR PEYIQDTDVV SARFQRRDVY
GAWEQYLGLE HTDTTPKRSY TANQNRHTYE KPVKIYN
//
