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Database: UniProt
Entry: A0A1S4AJF4_TOBAC
LinkDB: A0A1S4AJF4_TOBAC
Original site: A0A1S4AJF4_TOBAC 
ID   A0A1S4AJF4_TOBAC        Unreviewed;       791 AA.
AC   A0A1S4AJF4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN   Name=LOC107798286 {ECO:0000313|RefSeq:XP_016476744.1};
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_016476744.1};
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_016476744.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-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|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308,
CC       ECO:0000256|RuleBase:RU366025}.
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DR   RefSeq; XP_016476744.1; XM_016621258.1.
DR   AlphaFoldDB; A0A1S4AJF4; -.
DR   GeneID; 107798286; -.
DR   OMA; PRFCEKF; -.
DR   OrthoDB; 166948at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02658; Peptidase_C19B; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR016308};
KW   Protease {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR016308};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          157..267
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          309..789
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          605..646
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          664..704
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          578..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        318
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   ACT_SITE        751
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ   SEQUENCE   791 AA;  87795 MW;  6A47F8A1008D1999 CRC64;
     MEVLRSNLGR VRIPEPTTRI YKHECCISFD TPKSEGGLFV DMNAFLAFGK DYVGWNYEKT
     GNPVYLHIKQ TKKTEDAEDR PSKKPTLLAI GIDGGFDNSE PQYEEAYEIV ILPDYVTLPF
     PSVELPEKVR LAVDAVLLAE GAERKEQLAS WTADKKLVSK YATDLLQLDN GVVVPPVGWK
     CAKCDKTENL WLNLTDGTIL CGRKNWDGTG GNDHAVNHYR ETGYPLAVKL GTITADLEGA
     DVFSYPEDES VVDPLLAQHL AHFGIDFSSL QKTEMTTAER ELDQNINFDW NRIQETGEDV
     EPLFGPGYTG LVNLGNSCYL AATMQVVFSM RSFCLKYYSD QSLKAAFSMA PADPTVDLNM
     QLTKLAHGLL SGKYSAPVLE KQEGIRPRMF KSVIAASHPE FSTMRQQDAL EFFLHFIDQV
     ERMNSGKPDF DPSRSFKFGI EERLQCPSGK VAYNRRNDYI LSLNIPLEKA INKKELAEFQ
     NLKSKKAAEG KELSADEIVR PRVSLKDCLD CFSAPEEVHE FYSTALKART TAIKTAGLTS
     FPDYLVLHMR KFVMEEGWVP KKLDVYIDVP ETIDVSGMRS NGIQPGEELL PDSDAGDGEQ
     STKLLANEDI VAQLVSMGFN LLHCQKAAIN TSNSGVEAAM NWLLEHMNDS DIDAPISQNV
     QNPDIDQSKI DTLLSLGFEE KLACRALKAS GGDVERATEW IFSNPSASAA SDMDAATSGG
     AAVDPLLPDG GGRYRLLGFV SHIGTSTQCG HYVAHIHKDG RWVIFNDEKV GVSKNPPLDM
     GYLYFFERLE S
//
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