ID E9JVC9_9POAL Unreviewed; 935 AA. AC E9JVC9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 02-SEP-2026, entry version 54. DE SubName: Full=Enhancer of zeste1 protein {ECO:0000313|EMBL:ADU32891.1}; GN Name=EZ1 {ECO:0000313|EMBL:ADU32891.1}; OS Eulaliopsis binata. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Ischaeminae; Eulaliopsis. OX NCBI_TaxID=673200 {ECO:0000313|EMBL:ADU32891.1}; RN [1] {ECO:0000313|EMBL:ADU32891.1} RP NUCLEOTIDE SEQUENCE. RA Zhang D., Hu C., Yao J.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some PcG CC multiprotein complex, which methylates 'Lys-27' of histone H3, leading CC to transcriptional repression of the affected target genes. PcG CC proteins are not required to initiate repression, but to maintain it CC during later stages of development. {ECO:0000256|ARBA:ARBA00056128}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = CC N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L- CC homocysteine + 3 H(+); Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, CC Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; CC EC=2.1.1.356; Evidence={ECO:0000256|ARBA:ARBA00048568}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = N(6)-methyl-L- CC lysyl-[histone] + S-adenosyl-L-homocysteine + H(+); CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU00909}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. EZ subfamily. CC {ECO:0000256|PROSITE-ProRule:PRU00909}. CC -!- SIMILARITY: Belongs to the histone-lysine methyltransferase family. EZ CC subfamily. {ECO:0000256|PROSITE-ProRule:PRU00970}. 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; GU384662; ADU32891.1; -; mRNA. DR AlphaFoldDB; E9JVC9; -. DR GO; GO:0031519; C:PcG protein complex; IEA:InterPro. DR GO; GO:0003682; F:chromatin binding; IEA:TreeGrafter. DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0031507; P:heterochromatin formation; IEA:TreeGrafter. DR CDD; cd10519; SET_EZH; 1. DR FunFam; 2.170.270.10:FF:000001; Putative histone-lysine N-methyltransferase EZH2; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR InterPro; IPR026489; CXC_dom. DR InterPro; IPR045318; EZH1/2-like. DR InterPro; IPR025778; Hist-Lys_N-MeTrfase_plant. DR InterPro; IPR058609; HTH_CLF-like. DR InterPro; IPR041355; Pre-SET_CXC. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR033467; Tesmin/TSO1-like_CXC. DR PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1. DR PANTHER; PTHR45747:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1. DR Pfam; PF25996; HTH_CLF_N; 1. DR Pfam; PF18264; preSET_CXC; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM01114; CXC; 1. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS51633; CXC; 1. DR PROSITE; PS51576; SAM_MT43_EZ; 1. DR PROSITE; PS50280; SET; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE- KW ProRule:PRU00909}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|PROSITE-ProRule:PRU00909}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00909}. FT DOMAIN 668..767 FT /note="CXC" FT /evidence="ECO:0000259|PROSITE:PS51633" FT DOMAIN 782..897 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT REGION 13..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..554 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 905..935 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..31 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..386 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 388..400 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..435 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..481 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 484..496 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 502..511 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 530..554 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 905..919 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 896 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00190" SQ SEQUENCE 935 AA; 104131 MW; DF1C89BB019AB4A0 CRC64; MEAAAAAAAA VASSASASAS AGRSRPSTSA AQVTSITDVR AGEENAVSPY ALSVIDSLKK RITADRLTYI KNRIGENKTS LSSYTQRTYN LSKNRQINTL KGTDLTSNLL TKRQDDALCT QHSLDVIQVD KDGVNFQDES LFSSSNVTFG GNLGPKNAIR PIKLSEVPKL PPYTTWIFLD RNQRMTEDQS VLGRRRIYYD ASCGEALICS DSEDEAIEDE EEKKEFKHSE DRIIRMTIQE CGMSDPVLQT LARYMERATD DVKARYEILH GEKTKDSCKK GSEHNAKVED LYCDKDLDAA LDSFDNLFCR RCLVFDCKLH GCSQDLVFPT EKQSAWSSVD DGVPCGIHCH KLAFLQEPDS VAGADHMLID VEEPAHSSDN VMNQPGPNRK KNGSSGRKTK SQQSESSSTA RLISESSDSE VHPISNKSPQ HSPSPSKVKI GPKGGIRKIT NRRIAERILM SAKKGQREMA SSDSNSVSGS SLARDMKLRS DTRNGNKELI VSSQQSSPST RSSKKKSTPQ IGNNSASAEA HNDSTEEANN RHSTTDGYDS SRKEEFVDEN ICKQEGYLRS WKAIEQGLLV KGLEIFGRNS CLIARNLLPG MKTCRDVFQY MNYIENSSAS GALSGVDSLV KGYIKGTELR TRSRYFRRRG KVRRLKYTWK SAGYHFIRKR ITERKDQPCR QYNPCGCQSA CGKQCPCLTN GTCCEKYCGC PKICKNRFRG CHCAKSQCRS RQCPCFAADR ECDPDVCRNC WVGCGDGTLG VPNQRGDNYE CRNMKLLLKQ QQRVLLGRSD VSGWGAFLKN SVSKHEYLGE YTGELISHKE ADKRGKIYDR ENSSFLFNLN NEYVLDAYRM GDKLKFANHA PDPNCYAKVI MVAGDHRVGI FAKERILAGE ELFYDYRYEP DRAPAWARKP EASGGKDDGQ PSNGRAKKLA QNTRG //