ID A0A0L8FI64_OCTBM Unreviewed; 708 AA.
AC A0A0L8FI64;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=OCBIM_22019292mg {ECO:0000313|EMBL:KOF63359.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF63359.1};
RN [1] {ECO:0000313|EMBL:KOF63359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF63359.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF63359.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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; KQ431076; KOF63359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8FI64; -.
DR STRING; 37653.A0A0L8FI64; -.
DR EnsemblMetazoa; Ocbimv22019292m; Ocbimv22019292m.p; Ocbimv22019292m.g.
DR OMA; EIDMADW; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; IPR024928; E3_ub_ligase_SMURF1.
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 PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 136..169
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 166..199
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 240..273
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 280..313
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 374..708
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 24..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 676
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 708 AA; 81497 MW; 3823346EF05AAE59 CRC64;
MNSFTYSNFT FTVQIFYSST PSGSSSAGAS TSSGRGAEGG HSPKGIQLQN GVAPSPVSPL
ASSSSHMPSG ATAGAVGGST GGASAGVAAV AVAAHVTSDG ACGTVPNYAS QQASSQTPPT
QAQVQAQAQQ LQQPQDPLPI GWQMRFDPQG RVYYVDHNTR TTTWERPLPH GWERRVDSRN
RVYYVDHNTR TTTWQKPSMD MVLNWQQWQQ WRNNRSMEHL QQRFLYPQNP MLASETDTQD
ALPQGWEKRV DANGRVYFVN HKNRTTQWED PRTQGTLQED PLPEGWEMRY TTENVRYFVD
HNTRTTTFQD PRGGPCKGPK GPFGVPIQYE RSFRWKLGQF RYLCHSNALQ GHVKITVSRD
NLFEDSFTQI MRLAPYDLRR RLYIIFKGEE GLDYGGVARE WFFHLSHEVL NPMYCLFEYA
STKNYSLQIN PASSVNPDHL LYFKFIGRFI AMALYHGKFI DSGFTLPFYK RMLNKKLTIK
DIETIDQEFH NSLMWIKENN IEECGLELYF CGDFDILGKL EQHELKPNGA ELRVSEENKD
EYISLMTNWR FTRGVEEQTK AFLDGFSEVV PLQWLQYFDE RELELMLCGM QEIDVDDWEK
NTIYRHYQKT SKQIVWFWKF VRDLDNEKRT RLLQFVTGTC RLPVGGFSEL MGSNGPQRFC
IEKVGKETWL PRSHTCFNRL DLPPYKSYEQ LTEKLTYAIE ETEGFGQE
//
