EZ3_MAIZE
ID EZ3_MAIZE Reviewed; 895 AA.
AC Q8S4P4;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Histone-lysine N-methyltransferase EZ3;
DE EC=2.1.1.356;
DE AltName: Full=Enhancer of zeste protein 3;
GN Name=EZ3; Synonyms=MEZ3;
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; AF443598; AAM13422.1; -; mRNA.
DR RefSeq; NP_001105079.1; NM_001111609.1.
DR AlphaFoldDB; Q8S4P4; -.
DR SMR; Q8S4P4; -.
DR STRING; 4577.GRMZM2G043484_P02; -.
DR PaxDb; Q8S4P4; -.
DR PRIDE; Q8S4P4; -.
DR GeneID; 541955; -.
DR KEGG; zma:541955; -.
DR MaizeGDB; 754846; -.
DR eggNOG; KOG1079; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q8S4P4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
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:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
DR CDD; cd00167; SANT; 1.
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; IPR001005; SANT/Myb.
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..895
FT /note="Histone-lysine N-methyltransferase EZ3"
FT /id="PRO_0000214000"
FT DOMAIN 528..578
FT /note="SANT"
FT DOMAIN 628..732
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 747..862
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 100393 MW; 2659DCF992A08919 CRC64;
MASSSKASDS SSQRSKRSDQ GTGREAAPAS VVPIHGNLTQ LIRQIKSRRL LYIKEKLEAN
RKTLQRHSCS LFDVAAAAEV ASRGSDGGNA LSQRAAEGQF RLAGSDLAHG IGERDVVYMQ
EENLASGTLV LSSSGAAAQR TVVRFVKLPL VERIPPYTTW IFLDKNQRMA DDQSVVGRRR
IYYDPVGNEA LICSDSDEEI PEPEEEKHFF TEGEDQLIWR ATQEHGLNRE VVNVLCQFID
STPSEIEERS EVLFEKNEKN SGSSDKIERQ LSLDKTMDAV LDSFDNLFCR RCLVFDCRLH
GCSQNLVFPT EKQPYSFEPD ENKKPCGRQC YLRWRGGFQE IHDVGLSGCA TYNMESGTVS
HKVDVSIMSE SEDSNREKGN IRSMTLVGTS GSKIISSVSA EESTTPPSAD TSETENASSD
MPPSSLRKYK ISKRGPRYRE RSPGKRQKVF TSDISFASNI LNKLSIPEIR DTRLESREPG
GDKLQILDES TKKTSSKDIC GESPITTTEN MGIESKKVSS TKNFLEHTLS CWSALERDLY
LKGIEIFGKN SCLIARNLLS GMKTCMEVAN YMYNNGAAMA KRPLLNKSIS GDFAETEQDY
MEQDMVARTR IYRRRGRNRK LKYTWKSAGH PTVRKRIGDG KQWYTQYNPC VCQQMCGKDC
PCVENGTCCE KYCGCSKSCK NKFRGCHCAK SQCRSRQCPC FAASRECDPD VCRNCWVSCG
DGSLGEPPAR GDGYQCGNMK LLLKQQQRIL LGRSDVAGWG AFIKNPVNKN DYLGEYTGEL
ISHKEADKRG KIYDRANSSF LFDLNDQYVL DAYRKGDKLK FANHSSNPNC YAKVMLVAGD
HRVGIYAKEH IEASEELFYD YRYGPDQAPA WARRPEGSKK DEASVSHHRA HKVAR
