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Database: UniProt
Entry: W7HVS1_9PEZI
LinkDB: W7HVS1_9PEZI
Original site: W7HVS1_9PEZI 
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
//
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