ID A0D438_PARTE Unreviewed; 482 AA.
AC A0D438;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=GSPATT00013270001 {ECO:0000313|EMBL:CAK77805.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK77805.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK77805.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK77805.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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};
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DR EMBL; CT868285; CAK77805.1; -; Genomic_DNA.
DR RefSeq; XP_001445202.1; XM_001445165.1.
DR AlphaFoldDB; A0D438; -.
DR STRING; 5888.A0D438; -.
DR EnsemblProtists; CAK77805; CAK77805; GSPATT00013270001.
DR GeneID; 5030987; -.
DR KEGG; ptm:GSPATT00013270001; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_002173_9_1_1; -.
DR InParanoid; A0D438; -.
DR OMA; PRSHACF; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 144..482
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 448
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 482 AA; 56939 MW; 42E960AB3D307312 CRC64;
MGCCCSIKSP SQTTLGREVE CPKCQQLFPS YTTNHAVKIQ NFNLKFNDHL DNCLMSSQQN
INKTEDYRGI KYWEKVQNEQ GFQWVLKEYN PSLQINEQNI SSEPFGQKQV WFRAKLEKLR
IPWQNGCTIL SVSQNHLLET SIESIMKLKS RLLHGELKIK FQEDQKVQDA GGLLREWSTS
ILQQLVEMEY LQKTETKELT YKFNPNIQSN TIDKRQLFSF LGIIVGKCLF ERIPLSSFLD
RTIIKHILRQ KVTLEDIKYF DEDLFYSWQY LLNNNIDQLD LYFQLEYIGK TINLKENGCE
IKVTNSNVQE YVNLNIFFYT QQFLEPYLSD FLTGFYQVIP KTLLRIFNPQ ELEMILFGLP
FIDLQDWSKY TIYKECSAED YFIQWFWQIL SAWNQAELSQ FLRFCTGSTR VPVEGFSKLE
SNRGEISYFC IQASEFDKDN PYPKAHTCFN RLELPKYQEL ETMEVFLKAT IHEALEGQFG
LE
//
