ID G7YT28_CLOSI Unreviewed; 831 AA.
AC G7YT28;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=CLF_109986 {ECO:0000313|EMBL:GAA56108.1};
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:GAA56108.1, ECO:0000313|Proteomes:UP000008909};
RN [1] {ECO:0000313|EMBL:GAA56108.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Henan {ECO:0000313|EMBL:GAA56108.1};
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; DF144159; GAA56108.1; -; Genomic_DNA.
DR AlphaFoldDB; G7YT28; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008909; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008909};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 250..283
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 282..315
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 375..408
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 411..444
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 497..831
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 196..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 799
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 831 AA; 95188 MW; 0C75A7D6897887EA CRC64;
MTSVLLRVNV VADWMRVRCL AHMSPNHSES ETVKLDVKIN KAVVNRAYGL VAETVLSTNR
PKFSIAYVVL DSNTPLPTST AVQAPEQLGG TTRSHRGWSP EFHQHSTVRA NVNQLLEFRL
IARRHSTDEG LVIGYCRLII RQAAEANGLR LDNKIFDLRI SRLPTDSVAF QAGIADLGKL
YVQLAANPRE LNDALNAGSL NQQTNRRTRS DSIHSSTATV PPPRPPTTYP AAPEPNGGPS
TPNGEDANDT PLPPHWERRV APNGRAYYLD HLTKTTTWVR PSPLPPGWER RLDAHGRVYY
VDHNTRTTTW QHPSPTLLSN IREWRQFSDS RSGVMQQDMD QRYANANWNA GSIGFNASSA
TATSAAATSG LDLLGPLPEG WERRVDPQGR SYFVNHTSRT TQWEDPRLQG PPLPRGWEVR
VTPEGCPFFL NHIQKITTFV DPRRGDANSV KKEWSFEHKV SCFRYLCHSN AVQGTTKINV
SRARLLEDSF DQFMQLNTHE LRRRLYITFE GEEGLDYGGL SREFFFKLSV ELLNPMYCLF
EYASGTNYSL QINPASSVNP EHLQYFRFVG RFIALALYHG RFIDNGFTLP FYKRMLHKKI
TLEDIQTVDQ MYYSSLRYIL ETNVDEVDMD LYFSDDYEVL GEVKTHELKP NGSTIKVTEE
NKSEYIDLIV NWRFSRGVEE QTEAFLQGVS DVFPLQWLQY FDERELELLL CGMQQLDVND
WEANTIYKKY TERCKEIQWF WQFVRELPQE KRVRLLQFVT GTCRIPVGGF KDLMGSNGPQ
RFCIEKVGDE RSLPRSHTCF NRLDLPPYKS YEQLKAKLTL AIDESEGFGQ E
//