ID A0A0C2JB49_THEKT Unreviewed; 267 AA.
AC A0A0C2JB49;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=RF11_02062 {ECO:0000313|EMBL:KII66418.1};
OS Thelohanellus kitauei (Myxosporean).
OC Eukaryota; Metazoa; Cnidaria; Myxozoa; Myxosporea; Bivalvulida;
OC Platysporina; Myxobolidae; Thelohanellus.
OX NCBI_TaxID=669202 {ECO:0000313|EMBL:KII66418.1, ECO:0000313|Proteomes:UP000031668};
RN [1] {ECO:0000313|EMBL:KII66418.1, ECO:0000313|Proteomes:UP000031668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuqing {ECO:0000313|EMBL:KII66418.1};
RX PubMed=25381665; DOI=10.1093/gbe/evu247;
RA Yang Y., Xiong J., Zhou Z., Huo F., Miao W., Ran C., Liu Y., Zhang J.,
RA Feng J., Wang M., Wang M., Wang L., Yao B.;
RT "The genome of the myxosporean Thelohanellus kitauei shows adaptations to
RT nutrient acquisition within its fish host.";
RL Genome Biol. Evol. 6:3182-3198(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KII66418.1}.
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DR EMBL; JWZT01003532; KII66418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2JB49; -.
DR EnsemblMetazoa; KII66418; KII66418; RF11_02062.
DR OMA; MRERIYY; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000031668; 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 InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; 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:UP000031668};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..267
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 234
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 267 AA; 31638 MW; E1E00041154F374F CRC64;
MVESRQIDIY FSNIFFNKLF YPSHDIYLWN LEDIDPVLHN SLIYLLDYAS NNDSTLEDLD
IRFVWMNKDG SCDELCHNGS EILVTNQNIS TYIHKLINYK YIEGFDRIFS LIRDGLRYFV
PDLILWPTFY PEEFKILLSG DNQEWTLKDL EDHIIIQNYY TRTFPVIMNF FQILSEFNEE
ERKQFLMFMT SKTRLPFGGL ANLNPPLTIV PYFTEPNHPP FEVQDKYIPV AATCFHMLRL
PSYSSYEVLK SKLMYAIKEG QGVFGIE
//
