ID A0A388L360_CHABU Unreviewed; 1372 AA.
AC A0A388L360;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CBR_g22954 {ECO:0000313|EMBL:GBG76736.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG76736.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG76736.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG76736.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(2018).
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|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:GBG76736.1}.
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DR EMBL; BFEA01000252; GBG76736.1; -; Genomic_DNA.
DR STRING; 69332.A0A388L360; -.
DR EnsemblPlants; GBG76736; GBG76736; CBR_g22954.
DR Gramene; GBG76736; GBG76736; CBR_g22954.
DR OMA; WERVGHR; -.
DR Proteomes; UP000265515; Unassembled WGS sequence.
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 CDD; cd17039; Ubl_ubiquitin_like; 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; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 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 SUPFAM; SSF54236; Ubiquitin-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|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000265515};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 13..128
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 485..1263
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 227..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1022
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 149242 MW; 335B25CA4FA9964D CRC64;
MNHLSDSVCS FDRSPSQEKE ELEKLLDESN YRRKEGDTYY VISAEWWQQW MEYVGSKDSK
KTKISYFNGK PGVIDNNKIA QGGENKSNFA HLKRGLEEQV DFCLVPEAVW DRLVRWYSGG
PALPRKVIAQ GEESCRQLIV ELHPLRVQIV RSQSGICEEL IISRKATVGE LKQRVADLLN
MEGKSFCLWD FFNEKKQKKL TDAVRTLEDY EIQDLQKVLV ESEGRCRGGD AEQDSFASTS
SSSPSPGASL SSAITSSSSL STGAALISEG SASTYVSHRL TSASVTASRM AMTSDIVEDD
VLGETAREGD LRGEGQESRR AAGLTSAHDS QTSSSAALAE QKQLGISAQS SSLPSSYSNG
SILPATRSGS LSSPPSNGLL SPQRQDQANN SLNRSQPTSA DNIAPSSSSS SGLDLGASSR
SKVGAGGGDA VETRALAAIG NNNGTGSGVS TSGGGFFRTG VMARLGWRDG GGGGGGSAGG
RGGLTGLQNL GNTCFMNSAL QCLAHTPQLV EYFLSDYVRE INLENPLGMR GEIARAFGEL
LREMILVGKS PVAPRHFKGT LARFAPQFSG YNQHDSQELL AFLLNGLHED LNRVRDKPYI
EQKDADGRPD EKVAIEAWAN HKARNDSIVV DICQGQYKST LVCPTCGKTS VTFDPFMYLS
LPLPAKTSRS MMVAVLSADG SVDPDTYTVS VPKQGTVEDL LEAVAKACDL DRETERMALV
QLQQGRILRP LDFMLQESIG TIKDEEPLVA YRVPCSVPRS RLVMILNRRE EGMYKGDWRM
FGVPLLGIAP EGGVTSAKEV VQVVKAALRP MQRRRGDLEN GFGAGGAAEE SRRMPGRKKQ
VQEREEEDGR RPSVNGKRGG PSPGDSMRVG GAAANGDAVP STSVDFESAE TNGTDGTTDI
SMEDGEDGVQ VDGPTAGGNE GSSAERRQQD CDDGEKRWTS KGLGGGGGKG GKGGGRVDME
NDGDYDNGDV MSEVSGVVPG AEVEMTEVVA DKGMAMVRRE DANDDGEVEE REEEEDSSGE
EDECPFLVSC MDDRGLHREG VVELDKPLPR NWVVRSCGWR CVALEWASPP PTGREEYDLQ
VLELISERLR VGGPSLAKRA RQESLSLYSC LEAFLSKESL GKDDMWYCPR CKEHRQATKK
LDLWRMPDIL VVHLKRFSFS HWWKRKLETF VDFPIRGLDV RQYVTRKRRR NGGTKQRGEK
SSCLYDLYAV SNHYGGMGGG HYTAYAKLVN DDLWYNFDDS YVSPMREEDV KSPAAYMLFY
KRVGKDDASD AEGDDVDVDI DDAVGEAGEE EEVDDVASLE GEGEGREASG LDSEELEEER
GERVITPPPD EDGTDSSPER ITAIANEEDV EEGNSGEMDT TVAVFPLSNG KG
//
