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
//
