ID   Q3L8A6_MAIZE            Unreviewed;       931 AA.
AC   Q3L8A6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   03-MAY-2023, entry version 88.
DE   SubName: Full=Enhancer of zeste-like 1 {ECO:0000313|EMBL:AAR31181.1};
GN   Name=mez1 {ECO:0000313|EMBL:AAR31181.1};
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 {ECO:0000313|EMBL:AAR31181.1};
RN   [1] {ECO:0000313|EMBL:AAR31181.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Springer N.M., Thompson A.R., Kaeppler S.M.;
RT   "The maize PcG gene, Mez1, shows imprinted expression throughout endosperm
RT   development.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000090};
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DR   EMBL; AY422167; AAR31181.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3L8A6; -.
DR   SMR; Q3L8A6; -.
DR   ExpressionAtlas; Q3L8A6; baseline and differential.
DR   GO; GO:0005677; C:chromatin silencing complex; IEA:EnsemblPlants.
DR   GO; GO:0031519; C:PcG protein complex; IEA:EnsemblPlants.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031507; P:heterochromatin formation; IEA:EnsemblPlants.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IEA:EnsemblPlants.
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; 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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 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   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          664..763
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          778..893
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..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;  103785 MW;  E7240887777F7CFE 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 KLASEPDSAA
     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
//