ID A0A1S4DJS0_TOBAC Unreviewed; 971 AA.
AC A0A1S4DJS0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=LOC107830540 {ECO:0000313|RefSeq:XP_016513623.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016513623.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016513623.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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|ARBA:ARBA00000707,
CC 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 RefSeq; XP_016513623.1; XM_016658137.1.
DR AlphaFoldDB; A0A1S4DJS0; -.
DR SMR; A0A1S4DJS0; -.
DR STRING; 4097.A0A1S4DJS0; -.
DR PaxDb; 4097-A0A1S4DJS0; -.
DR GeneID; 107830540; -.
DR KEGG; nta:107830540; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000084051; Unplaced.
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, ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 59..184
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 204..506
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 971 AA; 113181 MW; 847B46E496919B4E CRC64;
MTMLNPQPLD QQEEEEMLVP HSDLVEGPQP LVEGPQPMEV APAENASTGE SQAADEPQAS
RFTWTIDNFS RLSVKKLYSE AFVVGSYKWR VLIFPKGNNV DCLSMYLDVA DSSTLPYGWN
RYAQFSLAVV NQINPKYSVK KETQHQFNQR ESDWGFTSFM LLSDLYDPNK GYLVNDKVVI
EADVAVRKVI DYWTYDSKKE TGYVGLKNQG ATCYMNSLLQ TLYHIPYFRK AVYHMPTTEN
DMPSGSIPLA LQSLFYKLQY SDTSVATKEL TKSFGWDTYD SFMQHDVQEL NRVLCEKLED
KMKGTVVEGT IQKLFEGHHM NYIECINVDF KSTRKESFYD LQLDVKGCRD VYASFDKYVE
VERLEGDNKY HAEEHGLQDA KKGVLFIDFP PVLQLQLKRF EYDFMRDTMV KINDRYEFPL
ELDLDRENGK YLSPDADRSV RNLYTLHSVL VHSGGVHGGH YYAFIRPTLS DQWYKFDDER
VTKEDLKRAL EEQYGGEEEV YVANSRSKLC LVVTCFDLDL LLLLQLPQTN PGFNNTPFKF
TKYSNAYMLV YIRESDKDKI ICDVGEKDIA EHLRIRLKKE QEEKEDKRRY KAQAHLYTII
KVARDEDLRE QIGKEIYFDL VDHDKVRSFR IQKQMPFNLF KEEVAKELGI PVQFQRFWIW
AKRQNHTYRP NRPLTPQEEL QTVGQLREVS NKTNNAELKL FLEVDLGLDL VPSPPPDKSK
DDILLFFKLY DPEKEELQYV GRLFVKSTSK PIEILPKLNE LAGFAPDQEI DLFEEIKFEP
SVMCERLDKK ASFRFSQIED GDIICFQKKA SPEVEEQVRF PDVPSYLEYV KNRQIVHFRA
LEKPKEDDFC LELAKSDTYD DVVERVAQRL GVDDPSKIRL TPHNCYSQQP KPNPIKYRSV
DHLVDMLIHY NQISDILYYE VLDIPLPELQ CLKTLKVAFH HSTKDEVEIL NVRLPKQSTV
GDVLNEIKSK V
//
