ID W7HVS1_9PEZI Unreviewed; 728 AA.
AC W7HVS1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=DRE_03234 {ECO:0000313|EMBL:EWC47614.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC47614.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC47614.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC47614.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI966409; EWC47614.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HVS1; -.
DR HOGENOM; CLU_002173_5_4_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
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:UP000024837};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 371..728
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 696
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 728 AA; 82781 MW; A2B5FB774722F87A CRC64;
MTAGDQLAAQ IFHLVDASSE SLNQDRQGAR RDPPLTREEA EDLEADIDEA RDHLERVLLK
AIEHLLKRPG KPLRTPEDLR TLLIIMGCPL LHQSRGGKKS LFERERLRMR SEVQTRNKPQ
PKSTSASGGP GRHSSIIKRI LGLISNLPNE AHHYFVSWVS RLKEPDFRKL VEFAGSFITY
RLTRQFGKQM SQGAAERIRG VVYSEDWQIK AASKVLSLLA AANTSAMLKT RDTDLPLESW
FNTASEDYEP EITSEANLAR QRALARGYVI PTSDFYNSML DYADLIADFD QWESKSSKFS
FCQYPFLLSM GSKIQILEYD AKRQMEVKAR EAFFNSIGLR RTFNQYLLLR VRRDCLVEDS
LKRISESVGS AAGDIKKGLK IEFEGEDGID IGGLRKEWFL LLIRDIFDPR HGMFVYDDDS
RFCYFNPNTF EATEQYFLVG VLLGMAIYNS TILDVALPPV VFKKLLSPNS PVSTSTKFST
PSPTARLPFN STLEDLAFFR PALARGLRQL LEFDGDVEST FCRDFVVEVD RYGQITQVPL
VPGGENRPVT NENRKEFVDL YAQYLLDNSV ARQFEPFKRG FWTVCGGNAL SLFQPDEIEL
LVRGSDEPLD ISALRAVAQY ENWNSSPQDV NVVKWFWESF EEATPEMQRM LLSFMTGSDR
IPAMGIANMV LKVVYGGPSS VHGHKKAERY PIARTCFNSI TLWGWESKEK LDKLLWRAVT
ESEGFGLK
//