ID F9X4Z5_ZYMTI Unreviewed; 799 AA. AC F9X4Z5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific {ECO:0000256|ARBA:ARBA00018028}; DE EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178}; DE AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091}; DE Flags: Fragment; GN Name=SDG2404 {ECO:0000313|EMBL:EGP90208.1}; GN ORFNames=MYCGRDRAFT_20674 {ECO:0000313|EMBL:EGP90208.1}; OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch OS fungus) (Septoria tritici). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria. OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP90208.1, ECO:0000313|Proteomes:UP000008062}; RN [1] {ECO:0000313|EMBL:EGP90208.1, ECO:0000313|Proteomes:UP000008062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062}; RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070; RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F., RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A., RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A., RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J., RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B., RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B., RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A., RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R., RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J., RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H., RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H., RA Oliver R.P., Grigoriev I.V., Kema G.H.J.; RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola RT reveals dispensome structure, chromosome plasticity, and stealth RT pathogenesis."; RL PLoS Genet. 7:E1002070-E1002070(2011). CC -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys- CC 36' forming H3K36me3. Involved in transcription elongation as well as CC in transcription repression. {ECO:0000256|ARBA:ARBA00003901}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA- CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359; CC Evidence={ECO:0000256|ARBA:ARBA00000317}; CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. CC 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; CM001197; EGP90208.1; -; Genomic_DNA. DR RefSeq; XP_003855232.1; XM_003855184.1. DR AlphaFoldDB; F9X4Z5; -. DR STRING; 336722.F9X4Z5; -. DR EnsemblFungi; Mycgr3T20674; Mycgr3P20674; Mycgr3G20674. DR GeneID; 13400312; -. DR KEGG; ztr:MYCGRDRAFT_20674; -. DR eggNOG; KOG4442; Eukaryota. DR HOGENOM; CLU_008492_0_0_1; -. DR InParanoid; F9X4Z5; -. DR OMA; AQSQPCY; -. DR OrthoDB; 950362at2759; -. DR Proteomes; UP000008062; Chromosome 2. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd19172; SET_SETD2; 1. DR CDD; cd00201; WW; 1. DR Gene3D; 2.20.70.10; -; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1. DR InterPro; IPR006560; AWS_dom. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR025788; Set2_fungi. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR044437; SETD2/Set2_SET. DR InterPro; IPR013257; SRI. DR InterPro; IPR038190; SRI_sf. DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf. DR InterPro; IPR017923; TFIIS_N. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1. DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1. DR Pfam; PF17907; AWS; 1. DR Pfam; PF08711; Med26; 1. DR Pfam; PF00856; SET; 1. DR Pfam; PF08236; SRI; 1. DR SMART; SM00570; AWS; 1. DR SMART; SM00508; PostSET; 1. DR SMART; SM00317; SET; 1. DR SMART; SM00456; WW; 1. DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1. DR SUPFAM; SSF82199; SET domain; 1. DR SUPFAM; SSF51045; WW domain; 1. DR PROSITE; PS51215; AWS; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS51568; SAM_MT43_SET2_1; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. PE 4: Predicted; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000313|EMBL:EGP90208.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000008062}; KW Repressor {ECO:0000256|ARBA:ARBA00022491}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGP90208.1}. FT DOMAIN 66..121 FT /note="AWS" FT /evidence="ECO:0000259|PROSITE:PS51215" FT DOMAIN 123..240 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT DOMAIN 247..263 FT /note="Post-SET" FT /evidence="ECO:0000259|PROSITE:PS50868" FT DOMAIN 509..541 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT REGION 449..516 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 576..605 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 681..799 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 449..472 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 499..513 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 589..605 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 681..702 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 761..777 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 784..799 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:EGP90208.1" FT NON_TER 799 FT /evidence="ECO:0000313|EMBL:EGP90208.1" SQ SEQUENCE 799 AA; 89713 MW; E85679F80ECF020A CRC64; EEIVGGEIVV KAEPRGLKLS RSTSHKIEKR APQMYHEYED KTKEATSTFE LLSECTYANK YLGTTEHALE CDCSEEWDAP SRSNHACGED SDCINRATKM ECVADCNCGS KCQNMRFQRK KYANVDVIKT EKKGYGLRTQ TDLRPNDFIF EYIGEVIGEN VFRRRMQQYD EDGIKHFYFM SLTKGEFVDA TKRGNLGRFC NHSCNPNCYV DKWVVGDKLR MGIFAERAIQ AGEELVFNYN VDRYGAEPQP CYCGEANCTG YIGGKTQTER ATKLPNSIIE ALGIDDADAW DTAVAKRPRK KKAGEDDEEY VNNVEPRGLD EEGVNKVMSS LMQCKEKWIA VKLLTRIQRA DDEKVRNRVV RFHGYRILKT ALTNFADDVN VCLQIIDILE KMPRLTRNKI QDSKIEEAVE TLVTNADEGV SSRAKTLLAA WGKLEIAYRI PRMKRDPNAV VHDRKLDRLD RPERRKSRSV SKSPERIVAP TGPRNAPQRP NNFFGNARPP PRFRPPPPGA LPPGWFEAQA GPGQTYYYTQ NGTTTWQRPT IPASAAPPPP PPKAISQQQV LDDLIKNIVA TQKEVAPKPA SAAATPMITP KKERKEDKWR SLPEEKQKKL YEGTLSPHIM HVVAKYKHKL PKDELKRWAK EFAKQVVDSD FRKNKVADPN KIDDKKIKDV RKHAQTFFEK AVKKKQAAEA KRAGKDTSKD IGGNSAEDSP AAPGSPMLVE DNDDDDADQG REQDVAMSVD AIDAIDATPA TPTAAALKRL RGDESMTDAD NAFSKKQRTE SVEAFAPPPP PPPPPAGDD //