ID G7YRC1_CLOSI Unreviewed; 999 AA.
AC G7YRC1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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_108192 {ECO:0000313|EMBL:GAA55501.1};
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:GAA55501.1, ECO:0000313|Proteomes:UP000008909};
RN [1] {ECO:0000313|EMBL:GAA55501.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Henan {ECO:0000313|EMBL:GAA55501.1};
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; DF144028; GAA55501.1; -; Genomic_DNA.
DR AlphaFoldDB; G7YRC1; -.
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; 2.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
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 197..332
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 531..565
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 572..605
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 666..999
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 388..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 967
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 999 AA; 112904 MW; 68E548902F6E3676 CRC64;
MRDSVSVAET ALSIAQRVVE VRKPSHHGKV QSLRDGTQSD VHRGCPHSAF LFNFVIDEIM
RRTLEGLQNP GVQIASDENL VDLDYTDDIV LVFEENNVQV FLDELTKVIP SFGMHFAPTM
SLSLRMGFNR VVSQLLRSVR NTGIVILAGE MNAQVGGTTT EKPIPHKIAK GSGTCRSGVK
ASFAWLKVWT QLPIMTQYSL SALASGESRR RQDFQNVVVT YTLRTTRKCF GPGFGLKHAA
LLLNSKGLFN KNGDLYIEIL VDNVVAYKTK TCLKNWNPTW NETASVVVSP SSKIRIRVFN
HFKYRPDILI AAGGIDLFRL LEEYNGVLSD CELKLPLSRG SEHRGSVLLI FDKLNIRNGD
PLHSRLRVAN LPDSGALTAN GISTSTASSV DMARSTSSTS TMTSSNSRAP LRTSNRNSLR
LTPMDVIEDS FWPSLIGSLF GLQPISSSSL AARPLPSSSS GSTDSSRDNR LTLPDRQRPR
TDWTEAGEWW ILDTGNSSPT ALPTSASTSP SSAKHSKLTS YFKQQTFSDS RPLPMGWERR
IDPASQRIYY VNHISKITQW EDPRERGMDE TQPLPRGWEK RYTPQGQRFF IDHNTRTTTF
IDPRTGQHAG SLGSLGVPLQ YERNFRAKLD YFRACCAHAM ISGQTKILVS RDNLLEDSFQ
LVSQMTATNL RRRLSITFLH EEGLDYGGVA REWFYRLSRE IFNPMFGLFE YTGKNYGLQI
NPGSHVNPNH LSYFRFVGRF IGMALFHGRC IDGGLTLTFY KRILGRKLTL EDLGLTDHEY
YQSLVFIRDN NIDKCDLELY FVASYDLLGA LHEDELIEGG KNIKVTEANK VEYISLMVDW
RFSRGISKQT EAVHKGIHEV LEPQWLQLFD ERELELLLSG MPEIDVADWE KNTVYLKYTR
SSKQIVWFWK FVQGLDNEKR ARLLQFVTGT CHLPLGGFAQ LVGSSGHQLF CIERTGDETW
LPRSHTCFNR LDLPPYTSFE QLKEKLQLAI EETRGFGQE
//
