ID A0A251P7T2_PRUPE Unreviewed; 851 AA.
AC A0A251P7T2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=PRUPE_5G132600 {ECO:0000313|EMBL:ONI07638.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI07638.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI07638.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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 EMBL; CM007655; ONI07638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251P7T2; -.
DR EnsemblPlants; ONI07638; ONI07638; PRUPE_5G132600.
DR Gramene; ONI07638; ONI07638; PRUPE_5G132600.
DR Proteomes; UP000006882; Chromosome g5.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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:SF46; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10-RELATED; 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 Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 1..68
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 245..833
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 851 AA; 96387 MW; D1DC7E807147152B CRC64;
MDLLSSKIVA RPGPIDNSDI VVNESEGNDL QLNRMLVEER DYVLVSQEVW EKLSDWYKGG
PALPRKLISQ GDVHKNLMVE VYPLCLKFID SRDNSQTVIR LSKKASVQEL YEKVCTLRGI
EQQKAHIWDY FNMQKYTLLD ASNQTLEQLN LQMDQEILLE VQVDGNHSSQ FSMDPTGNEL
ALVPIEPSRS SMTIAGGPTL SNGHSMDYSY NLPQGSALSS SASADTDDKC YVYNPMKKGD
RGGLAGLQNL GNTCFMNSSI QCLVHTPPLV EYFLQDYSDE INTENPLGMH GELALAFGEL
LRKLWSSGRT TIAPRAFKGK LARFAPQFSG YNQHDSQELL AFLLDGLHED LNRVKNKPYI
ETKDSDGRPD EEVADECWKN HRARNDSLIV DVCQGQYKST LVCPVCSKIS ITFDPFMYLS
LPLPSTVTRS MTVTVVYGDG RGLPMPYTLT LIKDRCIKDL IAALGTACCL KSDESLMLAE
VYEHRIYRYL DNLSEPLSSI KNDDRIVAYR YSKEEAAFKT RLEIIYRWQE KSTSDSLKGQ
RKLFGTPLVA YLGEDKLSGV DIDRAVSRIL SPLKRAVKLN SIKENGLVSQ GIDEASNSHN
SRPMDNIELE ETSSGELSFH LFLADERGSS CKPIEKYMHI SSGKPIKIFL DWTNQEDEVY
DASYLKDLPE VHKNGFTAKK TRQEAISLFT CMEAFLKEEP LGPDDMWYCP KCKEHRQATK
KLDLWMLPEV LVFHLKRFSY SRYSKNKLDT LVTFPIHNLD LSQYVMNKDG KPHLYELYAI
SNHYGGLGGG HYTAYAKLID ENRWYHFDDS HVSPVNETDI KTSAAYVLFY RRVKSGQKIG
EAESSGTHME S
//
