ID   E9JVC9_9POAL            Unreviewed;       935 AA.
AC   E9JVC9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   13-SEP-2023, entry version 45.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC         COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC         Evidence={ECO:0000256|ARBA:ARBA00000090};
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DR   EMBL; GU384662; ADU32891.1; -; mRNA.
DR   EMBL; GU384664; ADU32893.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9JVC9; -.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd10519; SET_EZH; 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; 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; 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};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
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        377..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//