ID A0A3B6MPL4_WHEAT Unreviewed; 1118 AA.
AC A0A3B6MPL4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G123300.8};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS5D02G123300.8}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5D02G123300.8};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G123300.8}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B6MPL4; -.
DR EnsemblPlants; TraesCS5D02G123300.8; TraesCS5D02G123300.8; TraesCS5D02G123300.
DR Gramene; TraesCS5D02G123300.8; TraesCS5D02G123300.8; TraesCS5D02G123300.
DR Gramene; TraesCS5D03G0307400.8; TraesCS5D03G0307400.8.CDS; TraesCS5D03G0307400.
DR Proteomes; UP000019116; Chromosome 5D.
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:UP000019116};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 56..181
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 201..525
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 131214 MW; 17BD63ED69FAAB99 CRC64;
MTMMTPSPLE QQQEDEEMLV PHQELSTADA AQPMEVVAQT EPTNTAESQA PEDPQTSRFT
WTIENFTRVS GKKHYSDVFV VGGFKWRVLI FPKGNNVDHL SMYLDVADSG NLPYGWSRYA
QFSLAIVNQI HQKYTARKDT QHQFNARESD WGFTSFMPLS ELYDPSRGYL VNDTVVVEAE
VAVRKMIDYW TYDSKKETGY VGLKNQGATC YMNSLLQTLY HIPYFRKAVY HMPTTENDMP
SGSIPLALQS LFYKLQYSDN SVATKELTKS FGWDTYDSFM QHDVQELNRV LCEKLEDKMK
GTVVEGTIEQ LFEGHHINYI ECINVDYKSN RKESFYDLQL DVKGCRDVYA SFDKYVEVER
LEGDNKYQAE QHGLQDARKG VLFLDFPPVL QLQLKRFEYD YMRDTMVKIN DRYEFPLQLD
LDKDDGKYLT PDADRSIRNL YTLHSVLVHS GGVHGGHYYA FIRPTLSDQW YKFDDERVTK
EDTKKALEEQ YGGEEELPQV NPGFNNTPFK FTKYSNAYML VYIRESDKEK IMCNVDEKDI
AEHLRIRLKK EQEEKEHKKK EKAEAHLYTI IKVARDEDLK EQIGKNIYFD LVDHEKVRNF
RIQKQLPFNS FKEEVAKEYG IPVQSQRFWL WAKRQNHTYR PNRPLAPHEE AQSVGQLREV
SNKAHNAELK LFLEVELGLD LRPIRPPEKS KEDILLFFKL YNPEKEELRF VGRLFVKALG
KPSDILTKLN EMAGFSPNEE IELYEEIKFE PNVMCEHIDK KLSFRSSQLE DGDIISFQKP
SIPGGDTQVR YKDVPSFLEY VHNRQVVHFR CLEKPKEEEF CLELSKLHTY DDVVERVARQ
LGLDDPSKVR LTSHNCYSQQ PKPQPIRYRG VEHLLDMLVH YNQTSDILYY EVLDIPLPEL
QCLKTLKVAF HHATKDEVVI HSIRLSKNST ISDVITDLKT KVELSNPDTE LRLLEVFYHK
IYKIFPPHEK IENINDQYWT LRAEEIPEEE KNLTAQDRLI HVYHFMKDPN QNQIQNFGDP
FLLVIREGET AAEVMDRVQK KLRVPNEEFA KWKVAFISMN RPEYLQDIDA VSARFQRRDV
YGAWEQYLGL EHTDTTPKRS YTANQNRHTY EKPVKIYN
//
