ID A0A453BM74_AEGTS Unreviewed; 727 AA.
AC A0A453BM74;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:AET2Gv20560500.2, 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:AET2Gv20560500.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR STRING; 200361.A0A453BM74; -.
DR EnsemblPlants; AET2Gv20560500.2; AET2Gv20560500.2; AET2Gv20560500.
DR Gramene; AET2Gv20560500.2; AET2Gv20560500.2; AET2Gv20560500.
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; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF68; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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:UP000015105};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 91..727
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 458..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 81885 MW; 07A7896509DC1843 CRC64;
MFNIDSQPVH VWDFSGQTNL ILMNEWNRSH QDYCHSEQEV VXXXXXXXXX NLLEVQVYAM
SDSLTFKIGG TSMNVDMSCG NFGRVSSMGL IGLENLGNTC FMNSSIQCLA HTTKLVDYFL
GDYDSDINRT NPLGLNGELA LAFGELLRSL WTNDRNTVAP HNFKAKIACF APQFSGFNQH
DSQELLAFLL DGLHEDLNQV KCKPYEEAKD ASGRPDEEVA DEYWRNHLAR NDSVIVDTCH
GQYKSTLTCP TCNKTSVTFD PFMYLSLPVP SMAKRTMTVT VFSTDGSREP FSYDVSVPKF
GTLSDLVQAL SAACSLGGDE SLLITEVYNN CIIRYLEEPS DSVSLLRDGD KLAAYRLPKQ
YEKSSLVVFT HKHFAEHSGV DNFVTPQMKE FEAPLLASLP EAVNGLTLQE IYLKLLNPFR
FSKIISSSTD CGRGDSDCAV YSMDAAGDCA VNLMDTTPSS SDGNVHSAQL EDGPERNQCN
DNSCEVMEGP SETYCGEADV SDKEAQTEQF GFYLTNERDD VQRTKIEMND LDLLEAKPNR
LHVSVNWQHS ASKQYDVSML NNLPEIHKLE VIPKGTEDSV ALHVCLEAFL KEEPLGPEDM
WYCPCCKKHQ QAMKKLDLWR LPEVLVIHLK RFSYTQFTRN KLETFVDFPI SDLDLSSYIT
TENEQPYNHY RLYAISSHYG NMGGGHYTAS IYQEGKGWHK FDDECVTPIS EDNIKTAAAY
VLFYRRE
//