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   24-JAN-2024, entry version 113.
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.Q8S4P4; -.
DR   PaxDb; 4577-GRMZM2G043484_P02; -.
DR   GeneID; 541955; -.
DR   KEGG; zma:541955; -.
DR   MaizeGDB; 754846; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   InParanoid; Q8S4P4; -.
DR   OrthoDB; 902834at2759; -.
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 H3K27 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
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; IPR001005; SANT/Myb.
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:SF14; HISTONE-LYSINE N-METHYLTRANSFERASE EZA1; 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; 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
//