ID A0A2I4FVS7_JUGRE Unreviewed; 963 AA.
AC A0A2I4FVS7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=LOC109002451 {ECO:0000313|RefSeq:XP_018835754.1,
GN ECO:0000313|RefSeq:XP_018835756.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018835754.1};
RN [1] {ECO:0000313|RefSeq:XP_018835754.1, ECO:0000313|RefSeq:XP_018835756.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018835754.1,
RC ECO:0000313|RefSeq:XP_018835756.1};
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|ARBA:ARBA00037450, 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 RefSeq; XP_018835754.1; XM_018980209.1.
DR RefSeq; XP_018835755.1; XM_018980210.1.
DR RefSeq; XP_018835756.1; XM_018980211.1.
DR EnsemblPlants; Jr07_00500_p1; cds.Jr07_00500_p1; Jr07_00500.
DR GeneID; 109002451; -.
DR Gramene; Jr07_00500_p1; cds.Jr07_00500_p1; Jr07_00500.
DR KEGG; jre:109002451; -.
DR OrthoDB; 653068at2759; -.
DR Proteomes; UP000235220; Chromosome 7.
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 Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
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:SF18; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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 ECO:0000313|RefSeq:XP_018835754.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 19..148
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 331..939
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 108103 MW; AE51FB5816A96F79 CRC64;
MEGTMTEVSM CSSASSTELT PEEERIMIRD IALTAEANSK EGDSFYVITQ RWWQHWIEYV
NQDQQNNAND GSSLSEHGDL VGSSSPKRPA GIDNSDLIYD AASDDASMDI EIHDTLLEGR
DYVLLPQEVW NQLYSWYGGG PILARKVISS GLSQTELAVE VYPLRLQLHM MPKGDRSTIR
ISKKETIGEL HRKACEIFYL NLDQVCIWDY YGRRKHALMS DMDKTLDDAN IQMDQDILVE
VLNHVNGTAL AGSMTSVQDN GSSQREATSF LIEPSKSSLS IAGGWSASKG ASRSNIIELP
QNQNPSSLVR EVENAYGTSS VSTRGATGGL TGLLNLGNTC FMNSSIQCLV HTPEFARYFR
EDYHQEINWQ NPLGMVGELA LAFGELLRKL WAPGRMPVAP RSFKAKLARF APQFSGYNQH
DSQELLAFLL DGLHEDLNRV KHKPYLKSKD ADGRPDEEVA DEYWANHIAR NDSIIVDVCQ
GQFKSTLVCP VCNKVSITFD PFMYLSLPLQ LTITRTMTVT VFTCDGSALP SACTVTVPKQ
GRCRDLILAL SSACSLKQSE KLLLVEIRNH LIQKFLEDPL IMLSTIKDDD HLAAYKMPKL
EKNTKYLQLI HRRREQETSD AETTSGWKPY GTPLVSSISC DDLITRGNIQ LLVHKMLSPI
ARTESLGQTA ISNISTSRAA SDQCCDISSG EACMDSSTSN SLNKDGTNSE AVALLRLPLQ
LVDESNACID LSVGEDKPIR LSLSSTSILV YVDWSQKLLE KYDTHYLENL PEVFNGPPSK
KARTEPLSLY TCLEAFLREE PLVPEEMWYC PQCKEQRQAS KKLDLWRLPE VLVIHLKRFS
YSRSMKHKDL LKLETFVNFP IHDFDLTNYV ANKNNSQRQL YELYALTNHY GGMGGGHYTA
HIKLLDENRW YNFDDNHISH INEEEVKTAA AYVLFYRRVK TDDATASNGA QSCADVNNIS
SQK
//