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Database: UniProt
Entry: A0A2I4FVS7_JUGRE
LinkDB: A0A2I4FVS7_JUGRE
Original site: A0A2I4FVS7_JUGRE 
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
//
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