ID A0A103YM22_CYNCS Unreviewed; 914 AA.
AC A0A103YM22;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=Ccrd_010044 {ECO:0000313|EMBL:KVI11543.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI11543.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI11543.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI11543.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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}.
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:KVI11543.1}.
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DR EMBL; LEKV01000086; KVI11543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103YM22; -.
DR STRING; 59895.A0A103YM22; -.
DR EnsemblPlants; KVI11543; KVI11543; Ccrd_010044.
DR Gramene; KVI11543; KVI11543; Ccrd_010044.
DR OMA; RRKHALM; -.
DR Proteomes; UP000243975; 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 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, ECO:0000313|EMBL:KVI11543.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 14..142
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 320..895
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 62..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 102456 MW; B64E6147E2C10FA5 CRC64;
MVEASPTGCS STELSPEEEL QMITAISMAT EPQTKVGDTF CLISRRWWQN WLDFVTHNKT
VSANEGSSSE HQDLGSSSTP KRPSSIDNSD LIYEAASENP TMGIELHDTL VEHTDYILVP
EVTWNQLCAW YGGGPKLARK VISSGQSQTE LSVEVYPLRL RLHLMPKGDQ CAIRISKKET
IRDLHKKACE IFVLNLEQVS IWDYYSHRKH ALMNDLDKSL DDANIQMDQD ILVEVIDNGG
GCTSDAQENG FAKNESSVLV EPSKTNYSIA GGFSASKGIP KNCNSELSQF QNLSSAIRES
EDKTPVSVGV STRGSSGGLT GLLNFGNTCF MNSAIQCLVH TPEFARYFRE DYHQEINWHN
PLGMVGELAL AFGEVLRKLW APGRTPFAPR QFKAKLARFA PQFSGYNQHD SQELLAFLLD
GLHEDLNRVK HKPYIKSRDA DGRPDEEVAD EYWANHIARN DSIIVDVCQG QYKSTLVCPV
CEKVSVTFDP FMYLSLPLQS TTTRTMTVTV FSCDGSALPA TCTVIVPKQG RCKDLIQALS
NACALKHNEK VFLVEIRNHL IHRFLEDPLM SLFSIKDDDH LSAYKIPKET GNARGTTGWK
AYGTPLVFPV SCDATITRGD IQLIVHTMLS PMLRAEPVHS DISDADPSSV ASDLTSVKKA
SIIDGKENDD SKTPSLKLPL KLVDGNNACI DLSVGEERTV RLPSTSMSVL LFIDWSPKLL
KRYDTHYLEK LPEVFKYGPA KKTRTEPLSL YTCLEAFLRE EPLVPEDMYC PQCKERRQAS
KKLDLWRLPE VLVIHLKRFS YSRSMKHKLE TFVNFPIHDF DLTNYIANKN NSGRQVYELY
ALTNHFGSMG SGHYTAHIKL IDENRWYNFD DSHISPVNED DVKSNAAYVL FYRRVKAEEN
GPGCCAGGNS SLHK
//
