ID A0A151GF68_9HYPO Unreviewed; 1413 AA.
AC A0A151GF68;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=DCS_07707 {ECO:0000313|EMBL:KYK55743.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK55743.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK55743.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK55743.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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:KYK55743.1}.
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DR EMBL; LAYC01000003; KYK55743.1; -; Genomic_DNA.
DR STRING; 98403.A0A151GF68; -.
DR InParanoid; A0A151GF68; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000076580; Chromosome 03.
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; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; 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 Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1066..1413
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 270..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1381
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1413 AA; 156866 MW; 28BF27CD3AE0D2CD CRC64;
MDSPRRSGIA KTFVQYLLNR SRREMTRMKI TGPATDSCVV TTDVQLTKTG LVSSTISPMV
VDVMFNGHRV AMMHLPEIKT STRGAKFTIQ QQKVRILDKT HFKAFLQSVI ADEATSIRLE
NGQCTATTLN IKVCCNFCLD IPIKGMGGPK AKIAWVDRRG DDIMVLIMIE NPGPVELEHG
TTIFELRNEG EEIMALLRGS LQIAQGTSDC ILRGKLRAGA APTSMIKLVG VCAESEDAGA
WSHETAQYFD LLLAVKPEFM QVLGSTFSDV HADTSSEEPE NHTLQPGGSW PPHTRPMSNP
FPSFFSSKKK KQDSNGRDPP DVSVYDVGTM AEASSKKPTQ RRPPGSKDFA MGNCMTCSSL
VRWPKELKVF KCTICASIND LVPADNIIRR KASSERGSGF GRDPAATHQR GKPISTQYCK
RLVRQCTHSY LTRTLGEKLG ASSQTCMNPS KRPLPNNRQP RPTDAMQGHG RISAEKHIFP
AFNGSACTND SKHIVDQELP VHLNPSRSRS PLPRSYSLSY SENPGLRRET SQAASTGPRR
NVSTTSDPGP KRIFKPLEEY IVACFSSLDC VNSSFMTPAP RPPGRQGIDP PIRTKPLNPR
ETQIPRQDAH ETTRDAMQTE DLVSELDPKM LLLGDFAENG MWWTGGGGPS SAATADTATM
KRVASASSTS VPSKTPQVNW RELDDWYSSV INPAEGWFAV YEEVSQLSTV ATLSERDLQD
LERDFLQAQE HVQRVLLKAT ELLLKRPGRP ISDPANLRFL LIALENPLLY SEAPPFQGIL
QPDHGPSVPS KAVSSENASL PSSGLLSGQH SGVIKRIIGI MSNVSTECHN RMIAWFAKYP
TARFTRTKEL ISGFLTYRML RQSDRTLPAE VDITAGLIPE MPAGRSVGAI LHAEIGSSSK
RVKEPGRMIA YSDDWQIKAA SRVLALLFAA NNLQSVRHGD EVLSASNEVQ PPAARDGVRG
SGQLLPTSDF YNLMLDNADL VGDFEAWESK RAKFSFCQYP FLLSIWAKTK ILEYDARRQM
QNKARDAFFD SIMTRRNIQQ YLNLEVRRDC LVDDSLKAVS EVIGSGSEDA KKALRITFTG
EEGIDGGGLR KEWFLLLVRE VFNPDHGMFM YDEDSHYCYF NPNSFETSDQ FFLVGVVMGL
AIYNSTILDV ALPPFAFRKL LASAPAHGQG ASAHPKPTMK YTLDDLSEYR PRLARGLRQL
LEFDGDVEEV FSLNFVIDVD KYGTTGQVPL CPGGERMAVT AVNRREYVDL YVRYILDGAV
TRQFEPFKRG FYTVCGGNAF SLFRPEEVEL LIRGSDEALD IAALRAVAEY DNWGSRRPDG
ESPVVGWFWQ TFEEANPEDQ RKLLLFITGS DRIPAMGAAM LPIKLSCLGD DCGRYPIART
CFNMLSLWLY GSKERLEAML WRAVKESEGF GLK
//
