ID A0A182E0J1_ONCOC Unreviewed; 771 AA.
AC A0A182E0J1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=NOO_LOCUS1469 {ECO:0000313|EMBL:VDK64238.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t01469-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t01469-RA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t01469-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK64238.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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 ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR EMBL; UYRW01000187; VDK64238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182E0J1; -.
DR STRING; 42157.A0A182E0J1; -.
DR WBParaSite; nOo.2.0.1.t01469-RA; nOo.2.0.1.t01469-RA; nOo.2.0.1.g01469.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
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; 3.
DR Gene3D; 2.20.70.10; -; 2.
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; 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:SF440; E3 UBIQUITIN-PROTEIN LIGASE NEDD-4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
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; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 3..140
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 203..236
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 296..329
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 346..379
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 436..770
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 738
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 771 AA; 88819 MW; 4DD3EFD2BC5400E8 CRC64;
MSPSEAPGVL VYGLPDTEQD TELLRVRVVR AGGLSKRDIF GVCDPYAVVL LKREGSTATR
EPIWNEEFVF RVVREDCILT VQVFDERHDS SGIQLIQGLT SGSVNVLPVM RFYTRDNFLG
MVQIDLSLVR IPYEVVGVPV PEASYILNPR SHRFYSSVQG IICLSLSYVT NSTQLGAELI
SANDDSDWEQ LSTSSLTNRQ GPTSLPEGWE ERQDANGRTF YVNHISRTTQ WMRPTRSGTE
SDLDETEQEN ALRRNYESRW QGSSEEHVED NIANLEAGLR TKFESGGRVD PNDGRGLLPQ
GWDMQVAPNG RTFFIDHIHK TTTWIDPRDG QASATYLKEV RSDELGELPP GWEKRVHADG
RIFYIDHNTR RTQWEDPRFE NTNIAGPAVP YSRDYKCKYE YLRSHLPKSP TNMKCEITVR
RIQLFEDSYR QIMQLSPTVL RAKLWIEFEN ETGLDYGGVA REWFYLLSHD IFSPYYGLFE
YSATDNYTLQ INPHSETCNP EHLSYFHFIG RVIGIAIYHG KLLDAFFIRP FYKMMLGKPI
TLNDMESVDN EYFNSLIYIK DNNPEDLDLH FAVDEDVFGQ MKSVELREGG AEEKVTDTNK
DEYIDLIIKW RFVSRVEEQM KALMKGIHEL IPPNLLSIFD PNELELLVCG LQKIDVKDWK
DNTLYKGGYS PSHPVIQNFW KCLLAFNNEM RARLLQFVTG TSRVPMNGFR ELYGSNGPQK
FTIERWGNTD MLPRAHTCFN RIDLPPYTNF HQMKERLTTA IENSEIFSGV D
//