ID A0A314Y336_PRUYE Unreviewed; 941 AA.
AC A0A314Y336;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=Pyn_18134 {ECO:0000313|EMBL:PQP98650.1};
OS Prunus yedoensis var. nudiflora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQP98650.1, ECO:0000313|Proteomes:UP000250321};
RN [1] {ECO:0000313|EMBL:PQP98650.1, ECO:0000313|Proteomes:UP000250321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC TISSUE=Leaf {ECO:0000313|EMBL:PQP98650.1};
RA Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA Yu H.-J., Mun J.-H.;
RT "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PQP98650.1}.
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DR EMBL; PJQY01001877; PQP98650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314Y336; -.
DR STRING; 2094558.A0A314Y336; -.
DR Proteomes; UP000250321; Unassembled WGS sequence.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF75; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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, ECO:0000313|EMBL:PQP98650.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000250321};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 342..938
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 698..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 107187 MW; 89507F2DEC39C6D6 CRC64;
MTRLSEKLRL SLFLYKPTRF LSLNLLPNIS LSSTLHLCKS LARALASKTL AFFSSSSAMD
DPYWDLDFRP SFRSQRLRLH DDYDDDDRSN DDVSHNAVDK LYLVPYRWWK EVRTEDDQMG
GVLYTASTDD DAGSEIFLNL KKKDVAEEGF SGREYALVPE PTWCRALRRH NDFYAAAKDN
VSLFGAEIFL KDVFSLQIRL FVSWETNSLV VKISQRDNTV DSYKRACNIF SSEYVPLHIW
DFSGQTTQIF MNDSINLPND IPGQLNKEIL LELRLHGFSY YMKGRDWWSD EVADRHPSMD
SSTYGGSMKM NGSTDYVNPY LTPTNSLQSG TIYRGAGSLG LIGLENLGNT CFMNSAIQCL
VHTPKLVDYF LGDYRKDINY SNPLGMKGEL ALAFGELLRK LWAPGAKPVA PRMFKLKLAS
FAPQFSGYNQ HDSQELLAFL LDGLHEDLNR VKCKPYIEAQ DVEGRPDEEV AEEYWQNHLA
RNDSIIVDVC QGQYRSKLVC PVCSKVSVTF DPFMYLSLPL PSTTMRTMTL TVLSTDGTAL
PCTFTVTVPK SGRSLDLTNA LSTACSLRDD ETLMLAEVYK CRIFRLLEDP FDSLDLIRDG
DRLVAYRLPK DCETSLLVTF IHQQMDMCHN NGEMRLVPQA FGIPLVATLP GVCNGSDIRN
AFLKVLNPYL MSPGDVLNIF DDDFANEDSN ATTTTTTTTI MDNDADSDRE SRDEANSDTD
FQFYLPDAKE AIEDTLIEMN EPIVVSGLPK RLKVLVLWSD NMTKKYDTCL LNTLPEVFKP
QFFVRKPEES VSLYKCLKAF MKEEPLGPED MWYCPICKKP QQASKKLDLW RLPEILVIHL
KRFSYSNLFK NKLETFVDFP IYGLDLSPYI SHRNSQLSSQ YMLYAISNHY GGMGGGHYTA
FVHLGNGSWY EFDDEKVLPV GQERIRTSAA YVLFYRRVPD I
//
