ID G7YEN7_CLOSI Unreviewed; 1346 AA.
AC G7YEN7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CLF_106083 {ECO:0000313|EMBL:GAA51420.1}, CSKR_106845
GN {ECO:0000313|EMBL:KAG5447809.1};
OS Clonorchis sinensis (Chinese liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA51420.1, ECO:0000313|Proteomes:UP000008909};
RN [1] {ECO:0000313|EMBL:GAA51420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Henan {ECO:0000313|EMBL:GAA51420.1};
RX PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA Yu X.;
RT "The draft genome of the carcinogenic human liver fluke Clonorchis
RT sinensis.";
RL Genome Biol. 12:R107-R107(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Henan;
RA Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA Wu Z., Yu X.;
RT "The genome and transcriptome sequence of Clonorchis sinensis provide
RT insights into the carcinogenic liver fluke.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG5447809.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5447809.1};
RX PubMed=29454982;
RA Wang D., Korhonen P.K., Gasser R.B., Young N.D.;
RT "Improved genomic resources and new bioinformatic workflow for the
RT carcinogenic parasite Clonorchis sinensis: Biotechnological implications.";
RL Biotechnol. Adv. 36:894-904(2018).
RN [4] {ECO:0000313|EMBL:KAG5447809.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5447809.1};
RX PubMed=33677057;
RA Young N.D., Stroehlein A.J., Kinkar L., Wang T., Sohn W.M., Chang B.C.H.,
RA Kaur P., Weisz D., Dudchenko O., Aiden E.L., Korhonen P.K., Gasser R.B.;
RT "High-quality reference genome for Clonorchis sinensis.";
RL Genomics 0:0-0(2021).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007182}.
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DR EMBL; DF143151; GAA51420.1; -; Genomic_DNA.
DR EMBL; NIRI02000042; KAG5447809.1; -; Genomic_DNA.
DR Proteomes; UP000008909; Unassembled WGS sequence.
DR Proteomes; UP000286415; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE BAP1; 1.
DR Pfam; PF01088; Peptidase_C12; 2.
DR Pfam; PF18031; UCH_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAA51420.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008909};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 6..84
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 139..329
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 955..998
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 145688 MW; 360249F7303C0F4B CRC64;
MSQSEWRELE SDPGLFTLLL EDFGVKGVQV EEIYELSEEI KETVYGFIFL FRWDSCKKKA
SRRSGRGSAG SAASFFNTTV TQSASTFGQT TNDLFRSGGN LQKESSGARV RSTSGSIGEA
QFSLGLDENE RIESSDIPMH QMSSTESNEL FFARQTVQNS CATHALLSVL LNRPELDLGP
MLNEFQRATR YLPPEAKGMA IGNMPQLAQA HNRHAAPPIS LSLDSALSPP TMPEPSEAAA
AAASAALAST QGTPSNSLSA TDSSSSTGGR TESAQTDTFH FVCYVPFGGF LYELDGLKSD
PINHGPLRDP KIPNAWTTQC VEILRQRMQE QDVRYSLMAV VPDRRLRLTK RMCKLEQNRR
TIENILVEKA RFEAEQQAAV CQSLTNGPLQ NSPSAFVDST TGQCTRLKCE DVASSPSYRT
GAPQVISCVG DVTNNGAPES TAVSNTRDRF SPGDSSRSVQ TRSSTRAASA SVSRQTEQTS
GEMACSDSDQ PKPTANHNSV SNPPRSSTEF SRKRPSFNTI LDDVEWTCDR KKSLLEPNQT
HPLVTTKHSD PSADSADCSA SSDHFTKLLA SIVSADSPLL STLTETVVAE AKTYDVDLKD
DNGCTTKSEG IVNCETTLSR EELCSSRSDD QKCSPTGFFQ SHSGSVSLIK KELELEHGSL
CSPGLRVSTS YPNCVTCNHT GAGNQVGFSQ NHLLSDELTK PLTVDTEFWH STTSYAPSAR
YQPRNGLDKL DSPEKLNDLR PRTRALTRAR VNNGTNRSNN LSSNNASTTT TALLLRSQRA
TSDAALICKA SPGLVSSPIH SPPTQLEAPD REDRTGSPVP DEQITAVTSN RARLNGTDRT
CSARPASKYP TRSSTRRDTL ASHNLAQFRS QLSMVNSYSS TSNNSNALTS SSTVISNCLS
DTLHPDYLEG KTGSPLVHNP TVNTRSADCL GNNNSPLTIG ELQVLLKKIK EHWNHCSDAL
MEEETKRHTY RIDDARRVHD YVPFIRAYLR ALVKHDMLHT LVLQALQSAN SGSPNTSALP
TTGNRNSPRV PSTGFKTNSR QSEIDSRSAN NCFTNCSTDR STPNHGATPV KSVLNSVNPN
RTRLRARTRL SSTTPSNSVA AQTNSVHVTR KSRTLSESST ERLQISVTDE GFLDSAVSTI
EDVPTEQPLF ASAPSNSPAY ASSVNKTMAV SESANCQSEG DSTSELPTDS HSTASTIGVK
NPSDFGEAGS VPAVSYSPVM SSTNTGASYS SCGSPPQSPQ STSSSRSTYL RPRPFTSNTQ
TVPEGNISRK SLRPRAHVDQ NATESQSESG ESDGRKSRPS GRSSFRRKIP YALVRDLDVG
NGCKPAGTSS TLISSAPDRF RKRRLC
//
