ID G2Q768_THET4 Unreviewed; 667 AA. AC G2Q768; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 61. 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=MYCTH_73315 {ECO:0000313|EMBL:AEO55646.1}; OS Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) OS (Sporotrichum thermophile). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces. OX NCBI_TaxID=573729 {ECO:0000313|EMBL:AEO55646.1, ECO:0000313|Proteomes:UP000007322}; RN [1] {ECO:0000313|EMBL:AEO55646.1, ECO:0000313|Proteomes:UP000007322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799 RC {ECO:0000313|Proteomes:UP000007322}; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M., RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P., RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S., RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., RA Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi RT Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(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; CP003002; AEO55646.1; -; Genomic_DNA. DR RefSeq; XP_003660891.1; XM_003660843.1. DR AlphaFoldDB; G2Q768; -. DR STRING; 573729.G2Q768; -. DR GeneID; 11505584; -. DR KEGG; mtm:MYCTH_73315; -. DR VEuPathDB; FungiDB:MYCTH_73315; -. DR eggNOG; KOG2589; Eukaryota. DR HOGENOM; CLU_013724_0_0_1; -. DR InParanoid; G2Q768; -. DR OMA; FANHDCG; -. DR OrthoDB; 1705992at2759; -. DR Proteomes; UP000007322; Chromosome 1. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. 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; IPR004827; bZIP. 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; PS00036; BZIP_BASIC; 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:UP000007322}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 116..230 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT REGION 283..432 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 450..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 612..667 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 349..384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 450..475 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..501 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 503..518 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..655 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 667 AA; 73548 MW; 24C057C44BD1151B CRC64; MPRIATATSK KQSLTFAQLA AYDDILTDAL IDRVYYWTTI PKNRPSYHPS RGVREEEIAK IIQTHLIVEP NLAVAEEKLL STDGLRKFHD SLKTAKERED FRSHLRRYMS IYLPDCPFEV NATNRYTIES YEASITARRP IRRNEAIKYL AGIQVTVTPE EEAQLALRKK DFSLVVSSRS KLTSLFMGPA RFANHDCSAN ARLVTGGQAG IQIFACRDIA VGEEITVTYS ESYFGENNCE CLCQTCEEKG VNGWRPEDGV LSVHRSIEDS PFDVDQGYSL RSRKRDRSLS VAGSRTSSVT PDIRPRIPKG SRRRSMVGDR ASTTDSLDGE NLAMSNASLK RKLDTAGLSS PPLTPSKRSQ PDRYSTAPAS SSISRGSSAV GSAGDSVVSE DGKSALTEVT SPEPDKPGPL LSPELSPVKQ SDAPIGQLVG GRLPHLPLTS AETLKSTSIL PTTESDPMQG PVGNASTTAS SPPDPESTPA NDPNDEAATV TSASATRRRK RGISNQPAAD RPRRRRVPGD YTLTPLLLSE PETAWIHCTN CNTAFVQKDA YFTKANCYRC ERHSKLYGYV WPKTAPEGKH DKEARVLDHR EINRFLHPED EAIIRGRKPW RERLTGASAE PTSGEERGQE SLRREPDRSK PRASSDLEAP ARRSGRIRRA SARALGE //