ID A0A453BLK1_AEGTS Unreviewed; 1001 AA.
AC A0A453BLK1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20556400.13, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20556400.13}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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 AlphaFoldDB; A0A453BLK1; -.
DR EnsemblPlants; AET2Gv20556400.13; AET2Gv20556400.13; AET2Gv20556400.
DR Gramene; AET2Gv20556400.13; AET2Gv20556400.13; AET2Gv20556400.
DR Proteomes; UP000015105; Chromosome 2D.
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:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 86..211
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 231..555
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 568..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 29..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 116334 MW; FFE0E62279AF1538 CRC64;
LAISTPPATH SRGGPHIAAG HPLVPSPVAM TISTPPPAPA EPQPQQEEEE VLVPHQELPN
GTQPMEVVPA EPAATVENQP TEDTPISRFT WTIDNLSRVN TKKLYSETFV VGGYKWRVLI
FPRGNNVEFL SMYLDVADSA VLPYGWTRYA QFSLSVVNQI HNKFTIRKET QHQFSARESD
WGFTSFMPLS ELYNPSRGYL VNDTCVIEAE VAVCKVVDYW SYDSKKETGY VGLKNQGATC
YMNSLLQTLY HIPYFRKAVY HMPTTENDMP SGSIPLALQS LFYKLQYNDS SVSTKELTKS
FGWDMHDSFM QHDVQELNRV LSEKLEDKMK GTVVEGTIQQ LFEGHHMNYI ECINVDFKST
RKESFYDLQL DVKGCQDVYA SFDKYVEVER LEGDNKYHAE QHGLQDAKKG VLFIDFPPVL
QLQLKRFEYD FMRDTMVKIN DRYEFPLQLD LDRDDGKYLS PDADRNVRNL YTLHSVLVHS
GGVHGGHYYA FIRPTLSDQW FKFDDERVTK EDAKRALEEQ YGGEEELPQT NPGLNNTPFK
FTKYSNAYML VYIRESDKDK IICNVDEKDI AEHLRIRLEK DREEKERRKK EKAEAHLYTI
IKVARDDDLT AQIGKDIYFD LVDHDKVPSF RIQKQMPFTQ FKEEVAKELG IPTQFQRFWL
WAKRQNHTYR PNRPLTPQEE ALTVGQLKEA ANKAHNAELK LFLEVELGLD LKPLTLPDKT
REDILLFFKL YDPEKEQLRY VGRLFVKASG RPQDILPKLR KMAGFLQDDD VELYEEIKFE
PNVMCEYIDN RIIFRSCQLE DGDIVCFQKS PKPDTADQFR YPDVPSFLVY IRNRQVVHFR
SLEKPKEDDF CLEMSKIFTY DEVVEKVAQQ LGVDDPSKIR LTSHNCYSQQ PKPQPIKYRG
VERLLDMLIH YNQTSDILYY EVLDIPLPEL QALKTLKVTY HHATKDEVSV HSIRLPKNST
VGDVLSDIKS KVDLSHPDAE LRLLEVFYHK IYKRYLHPVK R
//
