ID A0A200RBM3_9MAGN Unreviewed; 939 AA.
AC A0A200RBM3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=BVC80_7291g2 {ECO:0000313|EMBL:OVA20111.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA20111.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA20111.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA20111.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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:OVA20111.1}.
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DR EMBL; MVGT01000147; OVA20111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200RBM3; -.
DR STRING; 56857.A0A200RBM3; -.
DR InParanoid; A0A200RBM3; -.
DR OrthoDB; 653068at2759; -.
DR Proteomes; UP000195402; 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: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, ECO:0000313|EMBL:OVA20111.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
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 324..919
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 661..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 105605 MW; FD5E8035002D899C CRC64;
MTIPDSGCFM DNDTSCLPCI PEEEKRIVRE LTEVAESNLK EGNLYYVLTN KWFMDWQRYT
GQDTGDYLLD EHSTGSQSSN GGLLEASYRP GQIDNADLVL GGSDAGWDDL EIHRTLEEGR
DYVLVPQEVW KKLHDWYKGG PALPRKLISQ GVVHKNFSVE VYPLTLQLID SRDDKNFVIR
ISKKASIREL YNRVCTLLEL DLGKVNIWDY FNGRKHSLLS VSDQTLEEAS LQMDQKILLE
MQRDGFHSSG FRMDSTGNEL ALVPIEPSRS SVTIAGGPTV SNGYSTGYGS NITHGNGLNS
PQTDAEDGYD HLSTMTKGGG GGLAGLQNLG NTCFMNSALQ CLVHTPPLVE YFLQDYSEEI
NKQNPLGLHG ELAIAFGELL RKLWSSGRQP IAPRAFKGKL ARFAPQFSGY NQHDSQELLA
FLLDGLHEDL NRVKNKPYIE AKDANGRPDE EVANECWENH KARNDSVIVD VCQGQYKSTL
VCPNCSKVSV TFDPFMYLSL PLPSMVSRAM TITVFYGDGR GLPMPYTVSV LKHGCLKDLL
QALSTGCCLK SDESLLLAEV YDHRIFRYLE NPFEPLSTIK DDERIVAYRV PKRQEGLTRL
EIIHRNKEKC MSDISNGVDS KLLGTPLVTC LAEGPLTGAD IQPLVHLMLV PLLRTSALPS
NQVHTSKKNA SGPVNGYNSQ TGLKDESTDS MELEQTSNGE SSFHLSLTDD KGLIRSPIDS
DFVFRQGQIV RVLLEWSDRE RELYDVSYLE DLPEVYKTGF TVKKTRQEAI SLFSCLEAFL
KEEPLGPDDM WYCPTCKEHR QATKKLDLWR LPEILVFHLK RFSYSRYLKN KLDTFVNFPI
RNLDLSKYVR SMGAPPQSHL YELYAISNHY GGLGGGHYSA YAKLIEGDRW YHFDDSHVSP
VSKDEIKTSA AYVLFYRRVK GEQEKAVAVG EPSNIRMPS
//
