ID N1P9N1_YEASC Unreviewed; 910 AA.
AC N1P9N1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=CENPK1137D_2833 {ECO:0000313|EMBL:EIW10215.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW10215.1};
RN [1] {ECO:0000313|EMBL:EIW10215.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW10215.1};
RA Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM001528; EIW10215.1; -; Genomic_DNA.
DR AlphaFoldDB; N1P9N1; -.
DR HOGENOM; CLU_002173_2_3_1; -.
DR Proteomes; UP000013192; Chromosome VII.
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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 578..910
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 878
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 910 AA; 105522 MW; BC1584DCAAD2A1C6 CRC64;
MLNFTGQTRR RNVNLGNRTR NSKKDLLEKA KRERERRAQD KLKEDASKTI QKSIRRHFSN
VRLFKNTFTS SQLVHMIPAY GGKLIYYISQ YDLQQLLKLS HNFLSSYPNS LGNRQLLSLL
KLYQDDALVA ETLSDLNMDC PTVDEFLDSL SVYLCRASSL SYSSASKLAD VIEAWEVMHS
SASISIFSIS IGSYEKRPFA LQFYCILAER NLLPQLINTN PILWDNMAKT YSHCSKGGQK
NIAKLLIPNF NNHIAPSVLR SDNDYVLKFY EKAFIDEVIA TTANYVSDED HVKNLMCYIA
SSPNQSCKNS VLITLLSNKD FVRRLSWEFF HTKFNASKTE AHPLFSVLAQ LIDMHLLIST
DRELLDYNSV IPIEELKKFT STLKDFTFRQ YWELPKSERN PMLKEAVPLL SKVYERDSRL
HFLSTENNPT YWENSEKQFL NLRFYEELQE YEDLYREHLE EESDEDMEKE IDLDKERPPL
KSLLLNKMKK RLKSSLRFRK LEILLELPFF IPFEERVDLF YMFIALDKKR LSLDDDHNLI
NMFTPWASTG MRKQSAIISR DNVLEDAFNA FNSIGERFKA SLDVTFINEF GEEAGIDGGG
ITKEFLTTVS DEGFKDPKHE LFRTNDRYEL YPSVVYDATK LKYIWFLGKV VGKCLYEHVL
IDVSFADFFL KKLLNYSNGF LSSFSDLGSY DSVLYNNLIK LLNMTTDEIK SLDLTFEIDE
PESSAKVVDL IPNGSKTYVT KDNVLLYVTK VTDYKLNKRC FKPVSAYHGG LSVIIAPHWM
EMFNSIELQM LISGERDNID LDDLKSNTEY GGYKEEDQTI VDFWEVLNEF KFEEKLNFLK
FVTSVPQAPL QGFKALDPKF GIRNAGTEKY RLPTASTCVN LLKLPDYRNK TILREKLLYA
INSGARFDLS
//