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Database: UniProt/SWISS-PROT
Entry: EZ1_MAIZE
LinkDB: EZ1_MAIZE
Original site: EZ1_MAIZE 
ID   EZ1_MAIZE               Reviewed;         931 AA.
AC   Q8S4P6;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   05-DEC-2018, entry version 98.
DE   RecName: Full=Histone-lysine N-methyltransferase EZ1;
DE            EC=2.1.1.43;
DE   AltName: Full=Enhancer of zeste protein 1;
GN   Name=EZ1; Synonyms=MEZ1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
OC   Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Seed;
RX   PubMed=11950982; DOI=10.1104/pp.010742;
RA   Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G.,
RA   Phillips R.L., Kaeppler H.F., Kaeppler S.M.;
RT   "Sequence relationships, conserved domains, and expression patterns
RT   for maize homologs of the Polycomb group genes E(z), esc, and E(Pc).";
RL   Plant Physiol. 128:1332-1345(2002).
CC   -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some
CC       PcG multiprotein complex, which methylates 'Lys-27' of histone H3,
CC       leading to transcriptional repression of the affected target
CC       genes. PcG proteins are not required to initiate repression, but
CC       to maintain it during later stages of development (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
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; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00909};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:11950982}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00909}.
DR   EMBL; AF443596; AAM13420.1; -; mRNA.
DR   RefSeq; NP_001105078.1; NM_001111608.1.
DR   UniGene; Zm.10343; -.
DR   ProteinModelPortal; Q8S4P6; -.
DR   STRING; 4577.GRMZM2G157820_P02; -.
DR   PaxDb; Q8S4P6; -.
DR   EnsemblPlants; Zm00001d036296_T001; Zm00001d036296_P001; Zm00001d036296.
DR   GeneID; 541954; -.
DR   Gramene; Zm00001d036296_T001; Zm00001d036296_P001; Zm00001d036296.
DR   KEGG; zma:541954; -.
DR   MaizeGDB; 754841; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000083511; -.
DR   KO; K11430; -.
DR   OMA; CAVNSRE; -.
DR   OrthoDB; EOG09360260; -.
DR   Proteomes; UP000007305; Chromosome 6.
DR   ExpressionAtlas; Q8S4P6; baseline and differential.
DR   Genevisible; Q8S4P6; ZM.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR025778; Hist-Lys_N-MeTrfase_EZ.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR22884:SF237; PTHR22884:SF237; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00317; SET; 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   Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    931       Histone-lysine N-methyltransferase EZ1.
FT                                /FTId=PRO_0000213998.
FT   DOMAIN      565    615       SANT.
FT   DOMAIN      664    763       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      778    893       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS      3      8       Poly-Ala.
FT   COMPBIAS    675    750       Cys-rich.
SQ   SEQUENCE   931 AA;  103769 MW;  4F3CD84B17783B6C CRC64;
     MEAEAAAAVV ASSASASASA GRSRPSSSAA QVTSNSAVRA GEENAASLYV LSVIDSLKKR
     ITADRLTYIK NRIGENKTNI SSYTQRTYNL SKNRQISTSK GTDSASNLLT KRQDDALCTL
     HSLDIIPVDK DGGTFQDESP FSSSNVMFGG NLGPKNAIIR PIKLPEVPKL PPYTTWIFLD
     RNQRMTEDQS VLGRRRIYYD TSCGEALICS DSEDEAIEDE EEKKEFKHSE DHIIRMTVQE
     CGMSDAVLQT LARHMERAAD DIKARYEILH GEKTKDSCKK GTEHNVKVED LYCDKDLDAA
     LDSFDNLFCR RCLVFDCKLH GCSQDLVFPT EKQPAWSGVD DSVPCGIHCH KLASEPDAAA
     GADHMLFDVE EPTHSSDNVM NQPGSNRKKN GSSGRKTKSQ QSESSSTARV ISESSDSEVH
     PISNKSPQHS PSPSKVKIGP KGGIRKITNR RIAERILMSV KKGQREMASS DSNFVSGYLL
     ARDMKLRSDT RNGNKELIVS SQQSSPSTRS SKKKSTPQIG NSSAFAEAHN DSTEEANNRH
     SATDGYDSSR KEEFVNENLC KQEVYLRSWK AIEQGLLVKG LEIFGRNSCL IARNLLGGMK
     TCKDVFQYMN YIENNSASGA LSGVDSLVKG YIKGTELRTR SRYFRRRGKV RRLKYTWKSA
     GYNFKRITER KDQPCRQYNP CGCQSTCGKQ CPCLSNGTCC EKYCGCPKIC KNRFRGCHCA
     KSQCRSRQCP CFAADRECDP DVCRNCWVGC GDGTLGVPNQ RGDNYECRNM KLLLKQQQRV
     LLGRSDVSGW GAFLKNSVSK HEYLGEYTGE LISHKEADKR GKIYDRENSS FLFNLNNEYV
     LDAYRMGDKL KFANHAPDPN CYAKVIMVTG DHRVGIFAKE RILAGEELFY DYRYEPDRAP
     AWARKPEASG AKDDGQPFNG RAKKLAQNNR G
//
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