ID S4NQT8_9NEOP Unreviewed; 72 AA.
AC S4NQT8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
DE Flags: Fragment;
OS Pararge aegeria (speckled wood butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge.
OX NCBI_TaxID=116150 {ECO:0000313|EMBL:JAA79434.1};
RN [1] {ECO:0000313|EMBL:JAA79434.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA79434.1};
RX PubMed=23622113; DOI=10.1186/1471-2164-14-283;
RA Carter J.M., Baker S.C., Pink R., Carter D.R., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RT "Unscrambling butterfly oogenesis.";
RL BMC Genomics 14:283-283(2013).
RN [2] {ECO:0000313|EMBL:JAA79434.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA79434.1};
RA Carter J.-M., Baker S.C., Pink R., Carter D.R.F., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RL Submitted (MAY-2013) 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; GAIX01013126; JAA79434.1; -; Transcribed_RNA.
DR AlphaFoldDB; S4NQT8; -.
DR UniPathway; UPA00143; -.
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:0009966; P:regulation of signal transduction; IEA:UniProt.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670:SF19; E3 UBIQUITIN-PROTEIN LIGASE HECTD1; 1.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..72
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 50
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 72
FT /evidence="ECO:0000313|EMBL:JAA79434.1"
SQ SEQUENCE 72 AA; 8005 MW; 7CF0F5212CD48C03 CRC64;
MSWRERKAFL QFATGCSSLP PGGLANLHPR LTVVRKVDAG DGSYPSVNTC VHYLKLPEYS
CKEVLRERLL AA
//
