ID A0A151GVD7_9HYPO Unreviewed; 1287 AA.
AC A0A151GVD7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=HECT domain-containing protein {ECO:0000313|EMBL:KYK61066.1};
GN ORFNames=DCS_02207 {ECO:0000313|EMBL:KYK61066.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK61066.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK61066.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK61066.1,
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:KYK61066.1}.
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DR EMBL; LAYC01000001; KYK61066.1; -; Genomic_DNA.
DR STRING; 98403.A0A151GVD7; -.
DR InParanoid; A0A151GVD7; -.
DR OrthoDB; 1820836at2759; -.
DR Proteomes; UP000076580; Chromosome 01.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
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; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
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; PF16558; AZUL; 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 934..1287
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1255
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1287 AA; 144664 MW; 6F3268CF7C9E6CAE CRC64;
MSPSNLHSMA GADLVEPAHG RRGDRKSRRG PLDQEDLIAG LWREAPFARL PHDAPQGLRD
LVQDVDNPHR VYTIHRASRR HGFQLLVARY VLQLREGCGN KQCSTSTCFT LRKRLVGKSP
IRRYSPNSAR TLAVYLASQD NPDRGLCPYL RRSNDPPVAV NTLVFSALFP LPASTTDQFP
KTQHSPKKDL HPDSSSSMSE QAAMPSVQGD ANREESPATA EPAPKLSIHE RATCKDHRSF
AAAAFGTVAF KMLEWLTPQG IEHISKELAE IGQVEPSPNA EGHDTTTVRE AHRSPDSRQS
LDGIPRQDGK PRSTKHIREK AVPISQQEEL APPTRTPAKP KHGSRGSVRA PSTSNRRASV
EPLPTPAPRE ESKSTPKSQP LNSFHPHTAR MAPNAMSRPL PEFPLKPAFF ENVPCLSPQP
VDDVVVDPGS SDKEDSDDLT DTVTSPLGSP LRSPAKVGVD VDDLVMDASE RRNCLLPQSL
PRLDVEVVDF ICDVFQEDYT FEKRFVGPLS PAESFPAPQN RQRKLAPRRR RSDSTVPRRQ
WKAFNEQTLF DVLSNPRSLV GSFTKDGKLY DSLTMWYCML RMTRVAPSLV LHSLWLAARC
LFVPPEALKS LRSQASNLFS GDAAPLTNFE ASCVMSVCLH ALVASAPYVT DTKTLFDMSR
IRSHGVVGGR GTAIRQPPSM CLEYEDAFSN DLALRLARRL FCAITARRYF VDVAECDSTV
DTECGDLDIL RPMLRQLDSL GSDAAHILEF APQDRLLHEA RMPTLLLDWA RTILLQDWDG
EPEFSSDGPF YGAMSLMETM YEKRDTLLVP DVQFRVDYFS DRLDTLEMPV AWTGFTSTRQ
RHHLLDYPYL FSPETAVTFF RSINFSKMSR TFEESSSLKT RMNAIVDPGS LVTNPHHKVV
LQDLLRTASS KYLVLDIGRQ TVIRDAFDQL WRRQERELLR PLKIHLGEDG GEEGFDSGGV
QQEFFRMAIA ECLDPTYGAF TIDERTRMAW FVPDSVVEDW KFEMMGLLVS LAVYNGLTLP
LTFPNALYRK LLGQSVNELY HVADGWPELA AGLTTLLEWD ENEGLIEDVF ARTYEFSVSS
FGTHITREMA KEHASWPRGL FGEPSVRSMV DEAPLVTNDN RNDYVSDYIR YLTDVSVRPQ
YLAFERGFRA CLDGKSLSLL SPATLQSLVE GVQEINISEL RRHARYVGWD SSHRTIKDFW
SIVKRYDDRL KRKLLEFVTA SDRVPVGGMR NLQFVVQRNG EETGKGGHLP TAYTCYGTLL
LPEYKDKDLL RERLGMALEN AQGFGFA
//
