ID M1CQH5_SOLTU Unreviewed; 1122 AA.
AC M1CQH5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=102593182 {ECO:0000313|EnsemblPlants:PGSC0003DMT400072539};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400072539, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400072539}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400072539};
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 RefSeq; XP_006339190.1; XM_006339128.2.
DR AlphaFoldDB; M1CQH5; -.
DR STRING; 4113.M1CQH5; -.
DR MEROPS; C19.A53; -.
DR PaxDb; 4113-PGSC0003DMT400072539; -.
DR EnsemblPlants; PGSC0003DMT400072539; PGSC0003DMT400072539; PGSC0003DMG400028223.
DR GeneID; 102593182; -.
DR Gramene; PGSC0003DMT400072539; PGSC0003DMT400072539; PGSC0003DMG400028223.
DR KEGG; sot:102593182; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_0_1_1; -.
DR InParanoid; M1CQH5; -.
DR OMA; NVECLSM; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
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:SF929; 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:UP000011115};
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"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 131785 MW; 9F3B5EF3A49776F6 CRC64;
MTMLNPQPLD QQEDEEMLVP HSELVEGPQP LVEGPQPMEV AAPENATTGE NQAVDEPQAS
RFTWTIDEFS RLSVKKLYSE PFVVGSYKWR VLIFPKGNNV ECLSMYLDVA ESATLPYGWN
RYAQFSLTVV NQINPKYSVK KETQHQFNQR ESDWGFTSFM LLSDLYDPNK GYLVNDKVVI
EADVAVRKVI DYWTYDSKKE TGYVGLKNQG ATCYMNSLLQ TLYHIPYFRK AVYHMPTTEN
DMPSGSIPLA LQSLFYKLQY SDTSVATKEL TKSFGWDTYD SFMQHDVQEL NRVLCEKLED
KMKGTVVEGT IQKLFEGHHM NYIECINVDF KSTRKESFYD LQLDVKGCRD VYASFDKYVE
VERLEGDNKY HAEAHGLQDA KKGVLFIDFP PVLQLQLKRF EYDFMRDTMV KINDRYEFPL
ELDLDRENGK YLSPDADRSV RNLYTLHSVL VHSGGVHGGH YYAFIRPTLS DQWYKFDDER
VTKEDNKRAL EEQYGGEEEL PQTNPGFNNT PFKFTKYSNA YMLVYIRESD KDKIICDVGE
KDIAEHLRIR LKKEQEEKED KRRYKAQAHL YTIIKVARDE DLREQIGKEI YFDLVDHDKV
RSFRIQKQLP FNLFKEEVAK ELGIPVQFQR FWIWAKRQNH TYRPNRPLTP QEELQTVGQL
REVSNKTTNA ELKLFLEVNC GLDLIPVPPP DKSKDDILLF FKLYDPEKEE LRYVGRLFVK
STSKPIEILP KLNELAGFAP DQEIELFEEI KFEPSVMCER LDRKASFRFS QIEDGDIICF
QKKAFPEVEE QVRFPDVSSY MEYVKNRQIV HFRALEKPKE DDFCLELAKS DTYDEVVERV
AQRLGVDDSS KIRLTPHNCY SQQPKPNPIK YRSVDHLVDM LIHYNQISDI LYYEVLDIPL
PELQCLKTLK VAFHHSTKDE IEILNVRLPK QSTVGDVLNE IKSKVELSHP NAELRLLEVF
YHKIYKIFPL SEKIENINDQ YWTLRAEEIP EEEKNLGPHD RLIHVYHFTK ETPQNQMQVQ
NFGEPFFLVI HEGETLAEIK VRIQKKLQVS DEEFSKWKFA FLSLGRPEYL QDSDIVSNRF
QRRDVYGAWE QYLGLEHADN TSKRPYINQN RHTFEKPVKI YN
//
