ID W1P3G2_AMBTC Unreviewed; 852 AA.
AC W1P3G2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN ORFNames=AMTR_s00045p00168580 {ECO:0000313|EMBL:ERN02121.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN02121.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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; KI394661; ERN02121.1; -; Genomic_DNA.
DR RefSeq; XP_006840446.1; XM_006840383.2.
DR AlphaFoldDB; W1P3G2; -.
DR STRING; 13333.W1P3G2; -.
DR EnsemblPlants; ERN02121; ERN02121; AMTR_s00045p00168580.
DR GeneID; 18430224; -.
DR Gramene; ERN02121; ERN02121; AMTR_s00045p00168580.
DR KEGG; atr:18430224; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_011060_0_0_1; -.
DR OrthoDB; 902834at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005677; C:chromatin silencing complex; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; IEA:EnsemblPlants.
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:0003727; F:single-stranded RNA binding; IEA:EnsemblPlants.
DR GO; GO:1990110; P:callus formation; IEA:EnsemblPlants.
DR GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1900055; P:regulation of leaf senescence; IEA:EnsemblPlants.
DR GO; GO:0048587; P:regulation of short-day photoperiodism, flowering; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0010048; P:vernalization response; IEA:EnsemblPlants.
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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 589..688
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 703..818
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 344..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 96019 MW; BFE09F45E8261C14 CRC64;
MASLTPESSG EIKKPDGEQD KAFGALVSKV EKLINLVLDA RLSSIKERIE RNRKNLEVHT
FQLQALATLK KDDCSREHME AINMLSIRSE SALCQVGASD IVLGDRDNVN SQEEESSSVI
IFGNSSSGKS IIRPIRIPYI EKLPPYTSWI YLERNQRMAE DQSVVGRRRI YYDACGSEAL
ICSDSEEEFA EREEEKHEFS EGEDRILWNA IQGYGLKDEV LNTLSQFIDA SSFEIKARYE
TLVEQYEYKY SKKDGVKDKT DSEWSIHLNR SLSATLDSFD NLFCRRCLVF DCRLHGCSHG
LITPIDKQAP WSDAEESGVP CSNNCYLVEK EHVQDNSLEG FNKSKPGLNF EKETTPVSSS
NEESIADTDY RSITGKKKAG LKKGAMPMDR HNPSAKDILD PVSKRQKIMV ASDVVSVGRE
ALMVGDHGKG KTSFEAMNAN PTQKENMEGT PDCQESSFGD ETILLPEKPK TYLTRQSRSC
HESHEWSRME KDLYTKGLEI FGKNSCLIAR NLLSGLKTCK EVADYMLDDE AAMHPKFSSV
PNSSSDENGK PDADIMEQDM PARPRILRRR SRARKLKYTW KSAGHPSIRK RMADGKQQSC
KQYTPCGCDL ICGKECPCMN NGTCCEKYCG CPKICKNRFR GCHCAKSQCR SRQCPCFAAG
RECDPDVCRN CWVSCGDGTL GGPPLRGDNY NCGNMKLLLK QQQRILLGKS DVAGWGAFLK
NPVNRNDYLG EYTGELISHR EADKRGKIYD RANSSFLFNL NDQFVLDAFR KGDKLKFANH
SSNPNCYAKV MMVAGDHRVG IYAKEHIEAS EELFYDYRYE PDRAPIWARR PEGSTSKRDD
TSLSFGRAPK IA
//
