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Database: UniProt
Entry: Q8S4P4
LinkDB: Q8S4P4
Original site: Q8S4P4 
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   13-FEB-2019, entry version 92.
DE   RecName: Full=Histone-lysine N-methyltransferase EZ3;
DE            EC=2.1.1.43;
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; 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; AF443598; AAM13422.1; -; mRNA.
DR   RefSeq; NP_001105079.1; NM_001111609.1.
DR   UniGene; Zm.10341; -.
DR   ProteinModelPortal; Q8S4P4; -.
DR   SMR; Q8S4P4; -.
DR   STRING; 4577.GRMZM2G043484_P02; -.
DR   PaxDb; Q8S4P4; -.
DR   GeneID; 541955; -.
DR   KEGG; zma:541955; -.
DR   MaizeGDB; 754846; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000083511; -.
DR   KO; K11430; -.
DR   OrthoDB; 875190at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR025778; Hist-Lys_N-MeTrfase_EZ.
DR   InterPro; IPR001005; SANT/Myb.
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    895       Histone-lysine N-methyltransferase EZ3.
FT                                /FTId=PRO_0000214000.
FT   DOMAIN      528    578       SANT.
FT   DOMAIN      628    732       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      747    862       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS     75     78       Poly-Ala.
FT   COMPBIAS    650    719       Cys-rich.
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
//
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