ID A0A388KY01_CHABU Unreviewed; 1110 AA.
AC A0A388KY01;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CBR_g19448 {ECO:0000313|EMBL:GBG74934.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG74934.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG74934.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG74934.1,
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:GBG74934.1}.
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DR EMBL; BFEA01000214; GBG74934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388KY01; -.
DR STRING; 69332.A0A388KY01; -.
DR EnsemblPlants; GBG74934; GBG74934; CBR_g19448.
DR Gramene; GBG74934; GBG74934; CBR_g19448.
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; cd00121; MATH; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR46236:SF35; TRAF-LIKE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR46236; TRAF-LIKE SUPERFAMILY PROTEIN; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 2.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 9..137
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 165..504
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 339..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..702
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 127057 MW; 42DFC34D0DDDD6CB CRC64;
MEGFQPSQSV SFRWVIENFT KLTVRKLYSH TFAAGGHSWR LLLFPKGNSY ESVQKLAVYV
DVPYSEWLEV GWSRNADFTL RAVNQRDPSL SIENSSSHKF HKGEADWGFR EFMPLKDLVD
PSKGFLVDGT VVIEAEVSVG GDVVKAQNDS RNAQVDDSRK ATGFVALRSK YTAASSFMNA
VLQTLYHLPY LRKAVYHMSM TECEKKVAST TAMPFALQCL FHKMQNSDAS VQTDDFATSS
DWDSWAATSF CLPYEGRKFL LIIFEQLERA MRWTGVAGTI QDLFQGHYVL SSCADFVDDV
AVKEKRRRIS FYDLELDVRG CKDVYESFDK YCSAGERLEG GGKRRRHPRP GGGNGAGVGE
GRRKGNRRIW FETFPTVLCL HLKRFEYDVE HDNMVKVNDR YEFPVQLDLD RDGGKYLASD
RDRSVRNLYT LYSVLAHSGG INNGRCQVFI RPMLLEQWYK SDDEGVRKED ARRAVEEQYG
GEEEMVTTPK TTSSNAYVLV YVREEDKGKV MCKVDDTTRI AKRCQSGGGV QQKVADWYAI
VKVAREEDFR EQIGWDILFD LVDFEKVGWF VIGSHSSFQT VKDQCAAIFH IPIQCQRFWL
WEKRKNHTYR LSRPLTPDEE MQIVKRLIDE RASTRGPNAG INLFLEKVPE NPEGVSGPIH
NRPTGKDDIL IFFKKYSPAA AASGEEEEEE EEGEEEEEEE EEELRYVGKM LVKGETKPCD
VMVQIKQLGV FKPNEEVILY EEIKFDPTVM CIPIDKTATF SSSGLEDGDI VCVQRAIAET
DIIKYRYPDV PSYLDYVRNR QVVRFHRLSE PNSTPHFVLE MSRQHTYDDV VQRVARHVGV
DDPGKIHLTA HNCFSQAPRS RPIKHEGGES LADMLAHHNR MSEILYYDVV NPRALELERW
KTLEVRFYNS RVEEVCVRNI RLPKESTVGE LIKETSDLVD LSNSASQLRI LEVSESKIRK
IFLPTEKLDN ISNHTGQILR AEEIPEEEKD LGNAEEGRLI HVCHVWQDSA AGSRGAQTFG
EPFCLAVREK ETLVIVKTRI KRKLAVPYDD FSKWKFACME RSAPLYLQDT DIVLSCFGKR
TQTDDDCEQY LGLEHADTAH RMSHRCDGPN
//
