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 03-AUG-2022, entry version 111.
DE RecName: Full=Histone-lysine N-methyltransferase EZ1;
DE EC=2.1.1.356;
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; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; 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 for
RT 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 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 (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00909};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11950982}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00909}.
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DR EMBL; AF443596; AAM13420.1; -; mRNA.
DR RefSeq; NP_001105078.1; NM_001111608.1.
DR AlphaFoldDB; Q8S4P6; -.
DR SMR; Q8S4P6; -.
DR STRING; 4577.GRMZM2G157820_P02; -.
DR PaxDb; Q8S4P6; -.
DR EnsemblPlants; Zm00001eb271490_T005; Zm00001eb271490_P005; Zm00001eb271490.
DR GeneID; 541954; -.
DR Gramene; Zm00001eb271490_T005; Zm00001eb271490_P005; Zm00001eb271490.
DR KEGG; zma:541954; -.
DR MaizeGDB; 754841; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_011060_0_0_1; -.
DR OrthoDB; 875190at2759; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; Q8S4P6; baseline and differential.
DR Genevisible; Q8S4P6; ZM.
DR GO; GO:0005677; C:chromatin silencing complex; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; IEA:EnsemblPlants.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblPlants.
DR GO; GO:1990110; P:callus formation; IEA:EnsemblPlants.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0009294; P:DNA-mediated transformation; IEA:EnsemblPlants.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
DR GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0009909; P:regulation of flower development; IEA:EnsemblPlants.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IEA:EnsemblPlants.
DR GO; GO:1900055; P:regulation of leaf senescence; IEA:EnsemblPlants.
DR GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IEA:EnsemblPlants.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR GO; GO:0010048; P:vernalization response; IEA:EnsemblPlants.
DR Gene3D; 2.170.270.10; -; 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; PTHR45747; 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; SSF82199; 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; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..931
FT /note="Histone-lysine N-methyltransferase EZ1"
FT /id="PRO_0000213998"
FT DOMAIN 565..615
FT /note="SANT"
FT DOMAIN 664..763
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 778..893
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
