ID A7EUD2_SCLS1 Unreviewed; 842 AA. AC A7EUD2; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Histone-lysine N-methyltransferase SET9 {ECO:0000256|ARBA:ARBA00015413}; DE EC=2.1.1.372 {ECO:0000256|ARBA:ARBA00024057}; DE AltName: Full=Histone-lysine N-methyltransferase set9 {ECO:0000256|ARBA:ARBA00014232}; DE AltName: Full=SET domain protein 9 {ECO:0000256|ARBA:ARBA00030653}; GN ORFNames=SS1G_08939 {ECO:0000313|EMBL:EDN93074.1}; OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) OS (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN93074.1, ECO:0000313|Proteomes:UP000001312}; RN [1] {ECO:0000313|Proteomes:UP000001312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312}; RX PubMed=21876677; DOI=.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). CC -!- FUNCTION: Histone methyltransferase that trimethylates 'Lys-20' of CC histone H4 to form H4K20me3. {ECO:0000256|ARBA:ARBA00001984}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) CC + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:64456, Rhea:RHEA-COMP:15554, Rhea:RHEA- CC COMP:15998, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.372; CC Evidence={ECO:0000256|ARBA:ARBA00023940}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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; CH476632; EDN93074.1; -; Genomic_DNA. DR RefSeq; XP_001590175.1; XM_001590125.1. DR AlphaFoldDB; A7EUD2; -. DR STRING; 665079.A7EUD2; -. DR GeneID; 5486457; -. DR KEGG; ssl:SS1G_08939; -. DR InParanoid; A7EUD2; -. DR OMA; FANHDCG; -. DR OrthoDB; 1705992at2759; -. DR Proteomes; UP000001312; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0042799; F:histone H4K20 methyltransferase activity; IBA:GO_Central. DR GO; GO:0140943; F:histone H4K20 trimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd10524; SET_Suv4-20-like; 1. DR Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR InterPro; IPR041938; Hist-Lys_N-MTase_N. DR InterPro; IPR025783; Set9_fungi. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR039977; Suv4-20/Set9. DR PANTHER; PTHR12977:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B-RELATED; 1. DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS51567; SAM_MT43_SUVAR420_1; 1. DR PROSITE; PS50280; SET; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW Reference proteome {ECO:0000313|Proteomes:UP000001312}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 115..229 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT REGION 251..409 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 431..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 575..596 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 691..728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 793..842 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..352 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..461 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 463..478 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 495..511 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 530..546 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 842 AA; 95916 MW; F5ABB9BE5B555992 CRC64; MPPKANQLKK ERLTLAQLCS YDDILTDALV DQVYYWTNIR KNRVAYHSSR GVREEDVTKI LQNSVIIEKN TTKAESQLLA LPGLNKFQQS LKSEKEKEDF RRHLKKYINI YLPDCPFEVS STNRYTVVTH EAAIVARREI RKGEVVKYLC GIQVVMTPEE EAHINNSRRD FSIVMSSRNK AASLFLGPAR FANHDCGANA RLMTTGSAGM EIIAVRDIEI GEEITVTYGD SYFGEDNCEC LCKTCEDNRE NGWAQDTDDS NETIPKLSIE HEPTPLDTPG YSLRRRRRLP SSVSGSRSES MTPDVNLRPQ VRKLPPRSRR SASSARNGRS FAMESPSSES TLPGSNVDEA NDDNLLSLAK SLKRVPSGDD SAAATPKRRR VSQSIERSPL RLLRGLDESS PSETMKRPKN QLIVKVEEFT PTSFYGNISS TALPSSASES RRASITSSPS GEGTGETDAT SVDEETIVVR DEKPASVGPK AKRQGYVKRG NHGGRRRGPL WEKEKLEKAK QSNKVSSVMQ RAASAPREAV LVSPNTSRQH PALQDDADSS ALSDLGSDME IDDSTMTISK KLPQPKIRRR RRGVVPPPTT DLDHAPNVRI PGDYVLTHAL LAEPASAWIN CKICEEPFVQ KDAYFTRSSC PRCERHSKLY GYMWPKTDKE GKHDEEERVL DHRTVHRFIK SSEEKDIRRR IGRGSTGSRE VTKEASATPV VSAKGDGNKK PKGGLLKVYG RKSERTRRDR FTLDEVFALV FDIVLILYIR GRMYECNYCG KEWSGLVVYC VECRVERREK REERREKREE RREKREERRE KREERREKRE ERREKREERR EKREERRDDI CD //