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EZ1_ORYSI
ID   EZ1_ORYSI               Reviewed;         895 AA.
AC   Q84UI6;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Histone-lysine N-methyltransferase EZ1 {ECO:0000305};
DE            Short=OsiEZ1 {ECO:0000303|PubMed:14527713};
DE            EC=2.1.1.356 {ECO:0000255|PROSITE-ProRule:PRU00909};
GN   Name=EZ1 {ECO:0000305}; Synonyms=SET1 {ECO:0000305};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Pusa Basmati;
RX   PubMed=14527713; DOI=10.1016/s0378-1119(03)00723-6;
RA   Thakur J.K., Malik M.R., Bhatt V., Reddy M.K., Sopory S.K., Tyagi A.K.,
RA   Khurana J.P.;
RT   "A POLYCOMB group gene of rice (Oryza sativa L. subspecies indica), OsiEZ1,
RT   codes for a nuclear-localized protein expressed preferentially in young
RT   seedlings and during reproductive development.";
RL   Gene 314:1-13(2003).
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 act by forming multiprotein complexes, which are required to
CC       maintain the transcriptionally repressive state of homeotic genes
CC       throughout development. PcG proteins are not required to initiate
CC       repression, but to maintain it during later stages of development (By
CC       similarity). Involved in histone methylation and transcription
CC       regulation (Probable). {ECO:0000250|UniProtKB:Q10MI4,
CC       ECO:0000305|PubMed:14527713}.
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   -!- SUBUNIT: Component of the polycomb repressive complex 2 (PRC2), which
CC       methylates 'Lys-27' residues of histone H3 (H3K27me3), leading to
CC       transcriptional repression of the affected target gene.
CC       {ECO:0000250|UniProtKB:Q10MI4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14527713}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, shoots, rachis, anthers
CC       and embryos. {ECO:0000269|PubMed:14527713}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in emerging young seedlings from 3 to 4
CC       days after seed imbibition. {ECO:0000269|PubMed:14527713}.
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; AJ421722; CAD18871.3; -; mRNA.
DR   AlphaFoldDB; Q84UI6; -.
DR   SMR; Q84UI6; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0016571; P:histone methylation; TAS:UniProtKB.
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   Chromatin regulator; Methyltransferase; Nucleus; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..895
FT                   /note="Histone-lysine N-methyltransferase EZ1"
FT                   /id="PRO_0000444466"
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..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..403
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"
FT   BINDING         861
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   895 AA;  99776 MW;  BB618FCD0E414FA2 CRC64;
     MASSSSKASD SSSQRPKRPD QGPSGKDAAG LVVLHGKLAQ LKRQVQSTRL AAIKERVEAN
     RKALQVHTCA LFDVAAAAEV ASRGAEGGNA LSRGAAEGHC RLVGWDSASG PGERELVHVQ
     EENLVAGTLV LSSSGGSGAS HRTVVQLAKL PVVDKIPPYT TWIFLDKNQR MADDQLVCRR
     RIYYDPIVNE ALICSESDDD VPEPEEEKHV FTEGEDQLIW KATQDHGLSR EVLNVLCQFV
     DATPSEIEER SEVLFEKYEK QSQSSYETDF QLFLGKTMDV ALDSFDNLFC RRCLVFDCRL
     HGCSQNLVFP SEKQPYGHGL DENKRPCGDQ RYLRRREVYQ DTCNDDRNAC TTYNTDSRSS
     SLKVSATILS ESEDSNRDED NIKSTSIVET SRSKITNSEY ADKSVTPPPG DASETENVSP
     DMPLRTLGRR KISKHASKSN DHSPDKRQKI YSSPFPFAMS VLNKQSVPEI GETCPDSIES
     AVDQLPSLDD PNKKISTKDM CAGSTTNTTE NTLRDNNNNL FISNKEHSIS HWSALERDLY
     LKGIEIFGKN SCLIARNLLS GLKTCMEVAS YMYNNGAAMA KRPLSGKSIL GDFAEAEQGY
     MEQDLVARTR ICRRKGRARK LKYTWKSAGH PTVRKRIGDG KQWYTQYNPC GCQQMCGKDC
     ACVENGTCCE KYCGCSKSCK NRFRGCHCAK SQCRSRQCPC FAASRECDPD VCRNCWVSCG
     DGSLGEPLAR GDGYQCGNMK LLLKQQQRIL LGKSDVAGWG AFIKNPVNRN DYLGEYTGEL
     ISHREADKRG KIYDRANSSF LFDLNEQYVL DAYRKGDKLK FANHSSNPNC YAKVMLVAGD
     HRVGIYAKDR IEASEELFYD YRYGPDQAPA WARRPEGSKK DEASVSHHRA HKVAR
 
 
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