ID   A0A1Y2HX81_9FUNG        Unreviewed;      1095 AA.
AC   A0A1Y2HX81;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN   ORFNames=BCR44DRAFT_75480 {ECO:0000313|EMBL:ORZ39216.1};
OS   Catenaria anguillulae PL171.
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX   NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ39216.1, ECO:0000313|Proteomes:UP000193411};
RN   [1] {ECO:0000313|EMBL:ORZ39216.1, ECO:0000313|Proteomes:UP000193411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PL171 {ECO:0000313|EMBL:ORZ39216.1,
RC   ECO:0000313|Proteomes:UP000193411};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORZ39216.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MCFL01000006; ORZ39216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2HX81; -.
DR   STRING; 765915.A0A1Y2HX81; -.
DR   OrthoDB; 5471864at2759; -.
DR   Proteomes; UP000193411; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000193411};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          770..1095
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          16..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1063
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1095 AA;  119709 MW;  3D821D7560CCB53F CRC64;
     MENIVSTLSN LFVRRQSTPN TSSPNPNPNG NGNVPGPSSA STPNLSSHPQ HQHLLSSAAN
     TNGNQFRGPR TSSAPPSPVH SQPHHLHSHH HQQQLQQQQQ QQQQQQQQYP GAVRIQQPVP
     PQQPVSSSYG SSSASIQSSS VNHRSQRPAI QGYGHPYPGP MAAPPGTGPG SSPVSVTSTA
     NGYSQQYAQA QMMAAHQQQQ QQQLKQQAEP MSKANCQCCR TELTFPQSVV SFRCSVCDYI
     NDLMVLPPPP VTPESAHLNQ PLTLSGLRDF LARKPSTPVI SHASSPASAS PTSASAADID
     SVFAAPTLGR KLPAVPPGAG TPPPLVQSTS SSPTVPPPPP PPPRPAVASS TESTPPHAPS
     SFPTSPASIA ANLSPSYASP SPPIPGRLAS GVQPLAYSHQ AALALDLARY LRHVFSQWHL
     LNASLLVDVR RSGAKADGIL VNLYAAQEAW KLIMAQPHAV HVAVLSAMQH LLMRLGRTVR
     EAGELGWLVI MLECPLLRRS TWTASTSQAD DHLRLSVLSR LLGHLSALPN HLHYHLVEWS
     LDWSPEDLTN KVDLMNQFLT HRLKACQPPR SELGEDGRLL AQHYTQDWQI IAVCRSMALL
     FSSNNKNRRI DLSTFYNTMV DLRVHLLRDF DAWERRQLPF SFCQYPFTLS LAAKLTLMDF
     EAKRAMFHKF REAVAAQGMA EIAQSMSNNN NNNPSAAGQP ASSGALGRVT SMRRVGTAGA
     LVGADGLASP SGVTGAPGYF PTREQQMPFV PLHIRRTHLV EDSLAQLADP HVDLKKRIRV
     QFAGEEGIDA GGLLREWLLL LVKDLFDAKY GMWVEPNPGS GIVWFNPACG DLQEYYLVGV
     VVGLAVYNST ILEVPLASPG FKKLLKHPVG LADLKVLDPE LVHGLNMLLE YTGDDVEDVF
     CREFVGEFEA YGQVYRVPLV ENGANIPVTK ANRKEFVNRL VEFKLTTSVA RQFDSFYNGV
     LRVLQGNALS LFRPEEIELL VRGSVEVDVA QLEVTAEYEG GFSEGHPTVR DLWEVLRGFD
     PVMRGKFLKF LTGTDRVPAT GVTLKIVCLG HEDSERLPVA HTCFNQLGLY TYWGRDKLRR
     KLLMAVCESE GFGLK
//