ID X1ZG40_CAPTE Unreviewed; 766 AA.
AC X1ZG40;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EnsemblMetazoa:CapteP181994, ECO:0000313|Proteomes:UP000014760};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP181994}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; AMQN01013776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; X1ZG40; -.
DR EnsemblMetazoa; CapteT181994; CapteP181994; CapteG181994.
DR HOGENOM; CLU_014403_0_0_1; -.
DR OMA; NLCIFGP; -.
DR Proteomes; UP000014760; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd00078; HECTc; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11254:SF340; APOPTOSIS-RESISTANT E3 UBIQUITIN PROTEIN LIGASE 1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 114..144
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 428..766
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 733
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 766 AA; 87365 MW; 63F9E43B6B664B24 CRC64;
MNSNYAAYIA HHSRSKHSVV DFVTGKYLSP HHCKVIWDWE EPRQVGETVS FRIKFYQRNG
RPYKVSEGDQ LFVEVILGSL KMPCSISYGN SNSSKMDNSS NNHSNSNHSN IAKVSFTVHK
SGQYRIVIMV TGAPIKGSPF SKTFLPGPID PAKSGFVNQS SSVICQRGVP HQLQVEPKDE
FGNLCADISN IHQHIGYSMR LIEVIGNSKS CAANLQVTFD KALNSVVLQV CIEQEGCFRA
TVAYRGHKLK NGDFNILVLS PASYQRVNKS VAKKCHNVYY EARLVAYNND RLEKAKKIYC
YISPKQLTIK EYFMKIFPKR LYTFRVCPST KFQFLGLDRH YDTPTLLIED GCQAPVEIAS
KDRDVIASVF TIFLLKNIGG SETFKDKQDF FYHEVRQLHS KRIHERLPLK INRQELFKSS
LKATKNFSTS DWCRSFEIHF IGEQGVDWGG LRREWFELLS MALFEPGDNS LFTKFKDDNQ
ALVHPNPCPA NLKMKHYEFA GRIVGKCLYE SALGGIYKQF IKARFSRSFL AQLIGLRVNY
RYFEQDDPEL YNTKIKYIEE NDVDDMELVF AEEEYKDGRL DRVIELIPNG ARIAVTNINK
THYLNALAQF KLARRVQEEI DAFLKGLNEL IPDNLLSIFD ENELELLICG SSNYSITELR
ENHTISGSSA EFTQVLEWFW MIISGFTQED MGRLLQFTTG CSLLPPAGFA ELNPKFQITA
APTYGVLPTA HTCFNQICLP TYRSSEEMQQ ALMIAIREGN QGFALV
//
