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Database: UniProt
Entry: R0MHP0_NOSB1
LinkDB: R0MHP0_NOSB1
Original site: R0MHP0_NOSB1 
ID   R0MHP0_NOSB1            Unreviewed;       405 AA.
AC   R0MHP0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Ubiquitin-protein ligase E3A {ECO:0000313|EMBL:EOB13665.1};
GN   Name=UBE3A {ECO:0000313|EMBL:EOB13665.1};
GN   ORFNames=NBO_64g0046 {ECO:0000313|EMBL:EOB13665.1};
OS   Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS   (Pebrine of silkworm).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB13665.1, ECO:0000313|Proteomes:UP000016927};
RN   [1] {ECO:0000313|EMBL:EOB13665.1, ECO:0000313|Proteomes:UP000016927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX   PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA   Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA   Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA   Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA   Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT   "Comparative genomics of parasitic silkworm microsporidia reveal an
RT   association between genome expansion and host adaptation.";
RL   BMC Genomics 14:186-186(2013).
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DR   EMBL; KB908972; EOB13665.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0MHP0; -.
DR   STRING; 578461.R0MHP0; -.
DR   EnsemblFungi; EOB13665; EOB13665; NBO_64g0046.
DR   VEuPathDB; MicrosporidiaDB:NBO_64g0046; -.
DR   HOGENOM; CLU_002173_9_2_1; -.
DR   OMA; SSEDIQC; -.
DR   Proteomes; UP000016927; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; 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   InterPro; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 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   Ligase {ECO:0000313|EMBL:EOB13665.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016927};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          83..405
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        373
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   405 AA;  47226 MW;  042547EF479BFC1D CRC64;
     MNFREEFKFY RTKTKTPLRY SFVLPVHIKA ELIKAETNDM MKSSLQDSFF RALFEGHIGP
     YLFITVSRDN IYKESMDVVR CLNIEDVRKQ LRITFKCEEG VDSGGIRKEY FQLLSHEIKH
     DERLFYNNES TIWLRNDCLD MSAYMTIGKI LGIALYNNVL LNIPFPSVFF KKLLGKKTTF
     YDLKEIDPEL FCSLTNLKKL SEEDIAGLGL TFTINYTSSK NKTKTYNLTE DKSEKSVTKS
     NINSFVNRYA DFYINRSIYR QFEAIKKGFL FVIERETLFY LDHKELEKII MGSNDFDVHA
     LRSTASYTDY ESDSQIISWF WAIFESYGKK MRKKLLQFIT GNDRIPVAGA ASVKLIIMKN
     GCDTDRLPSS QTCFNTLLLP EYSSKKKLES KLRTALEMTA GFYLL
//
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