ID A0A453I2W6_AEGTS Unreviewed; 1123 AA.
AC A0A453I2W6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:AET4Gv20426900.40, 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:AET4Gv20426900.40}
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; A0A453I2W6; -.
DR STRING; 200361.A0A453I2W6; -.
DR EnsemblPlants; AET4Gv20426900.40; AET4Gv20426900.40; AET4Gv20426900.
DR Gramene; AET4Gv20426900.40; AET4Gv20426900.40; AET4Gv20426900.
DR Proteomes; UP000015105; Chromosome 4D.
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:SF941; 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:UP000015105};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 59..184
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 204..528
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1123 AA; 131159 MW; 66934FC4A65D4130 CRC64;
VYLTRLAVVS PTSQENDEML VAHQELATAD ADTAQPMEVV AQTEAASTAE SQPSEDPQTS
RFTWTIASFT RLNGKKHYSD VFVVGGYKWR VLIFPKGNNV EHLSMYLDVA DSANLPYGWS
RSAQFSLSVV NQIDQKYTTR KDTQHQFSAR ESDWGFTSFM PLSELYDPSR GYLVNDTIVV
EAEVAVRKMV DYWTYDSKKE TGYVGLKNQG ATCYMNSLLQ TLYHIPYFRK AVYHMPTTEN
DMPSGSIPLA LQSLFYKLQY SDNSVATKEL TKSFGWDTYD SFMQHDVQEL NRVLCEKLED
KMKGTVVEGT IEQLFEGHHI NYIECINVDY KSNRKESFYD LQLDVKGCRD VYASFDKYVE
VERLEGDNKY HAENHGLQDA KKGVLFLDFP PVLQLQLKRF EYDYMRDTMV KINDRYEFPL
QLDLDRDDGK YLAPDADRSI RNLYTLHSVL VHSGGVHGGH YYAFIRPTLA DQWYKFDDER
VTKEDTKKAF EEQYGGEEEL PQINPGFNNT PFKFTKYSNA YMLVYIRESD KEKIMCNVDE
KDIAEHLRIR LKKEQEEKEH KKKEKAEAHL YTIIKIARDE DLKEQTGKDI YFDLVDHEKV
RSFRIQKQLP FSTFKEEVAK EYGIPVQFQR FWLWAKRQNH TYRPNRPLNP HEEMQSVGQL
REISNKAQNA ELKLFLEVEF GLDLQPLPPP EKSKEDILLF FKLYNPEKEV LCFVGRLFVK
ALGKPSDILR KLTEMAGFTP DEEIELYEEI KFEPNVMCEH IDKKLTFRAS QLEDGDIVCF
QKSPKADSGT QVRYPDIPSF LEYVHNRQVV HFRSLEKPKD DEFCLELSKL HTYDDVVERV
ARQLGLDDPA KIRLTSHNCY SQQPKPQPIR YQGVEHLLDM LVHYNQTSDI LYYEVLDIPL
PELQFLKTLK VAFHHATKEE VVIHSIRLPK NSTIADVIID LKTKVDLSSP TAELRVLEVF
YHKIYKIFPL HEKIENINDQ YWTLRAEEVP EEEKNPSQHD RLIHVYHFTK DPLQNQQIQN
FGDPFFLAIC EGETLAEVKG RIQRKLQVPD EEFSKWKFAF ISMNRPDYLQ DSDVVSARFQ
RRDVYGAWEQ YLGLEHTDTA PKRAYTANQD SVQALHCCQT VFL
//
