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Database: UniProt
Entry: A0A0B1SGM3_OESDE
LinkDB: A0A0B1SGM3_OESDE
Original site: A0A0B1SGM3_OESDE 
ID   A0A0B1SGM3_OESDE        Unreviewed;       292 AA.
AC   A0A0B1SGM3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE            EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
DE   Flags: Fragment;
GN   ORFNames=OESDEN_17263 {ECO:0000313|EMBL:KHJ83041.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Strongyloidea; Chabertiidae; Oesophagostominae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ83041.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ83041.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ83041.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC       E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfers the ubiquitin to targeted substrates.
CC       {ECO:0000256|RuleBase:RU369009}.
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|RuleBase:RU369009};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU369009}.
CC   -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC       {ECO:0000256|RuleBase:RU369009}.
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DR   EMBL; KN575566; KHJ83041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1SGM3; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053660; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
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; IPR045322; HECTD1/TRIP12-like.
DR   PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE HECTD1; 1.
DR   PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369009};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..292
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        280
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT   NON_TER         292
FT                   /evidence="ECO:0000313|EMBL:KHJ83041.1"
SQ   SEQUENCE   292 AA;  33169 MW;  11972B23525582CD CRC64;
     MFRVLGIFLA KVLQDGRLVD LPLARPFLKL IVSPHLSEAE EPSLDRVLSL DDFEEVHPVK
     GGFLKELRAL AQRKRAIENE PMLDREAKRR KIDELKLCIH GTRCRVEDLA LNFTVNPPSS
     VFDYEEMELV EGGADMDVTM DNVELYVQKC ADFYLNTGII NQMRAFRDGF DRVFGLRALR
     SYSPEEVQRL LSGEQCPEWT REDVLNYTEP KLGYTKDSPG FLRFVDVMVE LNPQERKNFL
     QFATGCSSLP PGGLANLHPR LTVVRKVESG DGSYPSVNTC VHYLKLPEDS SA
//
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