ID A0A1Y2DZC6_9PEZI Unreviewed; 1108 AA. AC A0A1Y2DZC6; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 27-NOV-2024, entry version 21. DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485}; DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485}; GN ORFNames=BCR38DRAFT_343583 {ECO:0000313|EMBL:ORY64454.1}; OS Pseudomassariella vexata. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella. OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY64454.1, ECO:0000313|Proteomes:UP000193689}; RN [1] {ECO:0000313|EMBL:ORY64454.1, ECO:0000313|Proteomes:UP000193689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY64454.1, RC ECO:0000313|Proteomes:UP000193689}; 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 -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885}; 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:ORY64454.1}. 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; MCFJ01000007; ORY64454.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1Y2DZC6; -. DR STRING; 1141098.A0A1Y2DZC6; -. DR InParanoid; A0A1Y2DZC6; -. DR OrthoDB; 5471864at2759; -. DR Proteomes; UP000193689; Unassembled WGS sequence. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:TreeGrafter. DR CDD; cd00078; HECTc; 1. DR FunFam; 3.30.2160.10:FF:000004; probable E3 ubiquitin-protein ligase HERC4 isoform X1; 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:UP000193689}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PROSITE-ProRule:PRU00104}. FT DOMAIN 759..1108 FT /note="HECT" FT /evidence="ECO:0000259|PROSITE:PS50237" FT REGION 1..99 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 130..149 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 171..192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 234..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 300..337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 573..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..31 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 56..75 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..149 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..252 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..321 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1076 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104" SQ SEQUENCE 1108 AA; 124881 MW; 091CC4292DDAE994 CRC64; MDVFRNPHGQ LQHHAESSST DDDDIRFSKP KPKSRPARHS RSMSHPITSL FSKKKKPASD GVDDDSTDDD TTHARGQLGL RTSMAPPGPR RRSADSVKGN CMTCGSQVSW PKEVDAFRCS ICVTINDLKP FNPPRRDEKG SEPPRPISLE HTKFLVREGL RCALNSFLVG RAPKDRNGTS DAGPSGPLSR VAGDYFSQKQ DRPISIHRSP PVLIPSPVFD GHTEVSFEMN PLRQLAGPSR SNSTSYPDAR SSGLPSKPQK REPVGIDGCR IFKPLEDYLA TSFNSYACIN ASFVARRKSF SSRPVGAQPR TRRQSFKSAP IDTPRNRRGS RSDPVNTDTL VSELDAKMLL VGDIAENGSW WTGGQEIQPL RAQSWRLNEP QPIANARSPQ IDWKEATAWY HSVINAGESW TDVYGELVQK DPTKTLSELD GQNFEQLVLA AQEHLQRVLL KCTENFLKRP GRLLKEPQDS RFLLLFLANP LLLHGHKTYA GVCQHLRKEP RAPEDAYTVG RHSVIIKRIL GILSHLPDPC HHHFVGWFSR LPEHIFLQIK DLVSSFVTYR LVRANEKRSE PKVDLTGGLI PQMPSNRSSN NAASLHAALG TSQRSNKRKP VELKKTTYGD DWQMKAGAQV MALVFAANNV THVRRNEVSV RHAHGHLLAT SDFYNTLLDT MDFRADFEEW ESKKSKFSFC HYPFFLSIWT KIRILEFDAK RQMAHKAHQA LVDSVLTHRN FAQYISLRVR RDCLVEDSLR QVSQVVGSGS EEIKKGLRIE FDGEEGVDAG GLRKEWFLLL VREVFNPDHG LFVFDEDSQH CYFNPHTFET SDQYFLVGVV LGLAIYHSTI LDIALPPFAF RKLLAAAPAP STGITGLLRP PMTYSLSDLR EYRPRLAHGL KQLLEFEGDV ESTFCRDFVI ETEKYGTTIR TPLCPGGENM QVTNNNRHKF VELYVRYLLD TSVSRQFEPF KRGFFTVCAG NALSLFRPEE IELLVRGSDE PLDIATLRAV ATYTNWEPDK SSEPELEPTV DWFWKSFAAA SPADQRRLLS FITGSDRIPA MGAASLVIKI NCLGDDIGRY PTAQTCFNAL NLFRYRLQES LEVKLWGAVR ESEGFGLR //