ID   K7K5W6_SOYBN            Unreviewed;       868 AA.
AC   K7K5W6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN   Name=100795451 {ECO:0000313|EnsemblPlants:KRH69214};
GN   ORFNames=GLYMA_02G012100 {ECO:0000313|EMBL:KRH69214.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH69214.1};
RN   [1] {ECO:0000313|EMBL:KRH69214.1, ECO:0000313|EnsemblPlants:KRH69214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH69214};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH69214.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH69214}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH69214};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH69214.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH69214.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000835; KRH69214.1; -; Genomic_DNA.
DR   RefSeq; XP_003519745.1; XM_003519697.3.
DR   AlphaFoldDB; K7K5W6; -.
DR   SMR; K7K5W6; -.
DR   STRING; 3847.K7K5W6; -.
DR   PaxDb; 3847-GLYMA02G01540-2; -.
DR   EnsemblPlants; KRH69214; KRH69214; GLYMA_02G012100.
DR   GeneID; 100795451; -.
DR   Gramene; KRH69214; KRH69214; GLYMA_02G012100.
DR   KEGG; gmx:100795451; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   HOGENOM; CLU_011060_0_0_1; -.
DR   InParanoid; K7K5W6; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000008827; Chromosome 2.
DR   ExpressionAtlas; K7K5W6; 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; 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; SM00717; SANT; 2.
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:UP000008827};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          606..705
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          719..834
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..861
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  97113 MW;  347670D66DB8BD6A CRC64;
     MVSKPTDSAS KPRKQLGEPA NDGIGSLSLE LNQLKKQIQA ERIVCIKEKI RSNEKKLQCH
     MSGVLSETST RGSSQTEENR KNPILSSRID HPLCKFSGFS PVWGDKDHNN QDVLSATSIK
     MPYIETLPPY TSWIFLDRNQ RMAEDQSVVG RRRIYYDQHG SEALICSDSE EELTEPEEEK
     HEFSEAEDRV IWMAFEEYGL NKEVPNIVSE FVGGTSLEIQ ERYKTIKEKN IGRLDQPSQN
     SGEYESTIGI CLEKSLSAAL DSFDNLFCRR CLIFDCRLHG CSQPLIYHSE KQTVWSDPEG
     DRKPCSDQCY LQLKVVKNVT EDSTSGSDQN KRTTITEEAD VILAPSIIEE PSNQSIIPFQ
     TEVDCHGSLN LNVPISVSVE KRKVLNQSDM SPRDSTLHPN DCQNSYKKLK AISDAVVTVN
     SDSSKKISLG ACGESIHTIT SAILDKSVKD NSIKLIDSSS TCPSDEQDKS IGDGPKDPTN
     ETEFKMSNSM EGIVDGMLSL SDWKPLEKEL YLKGVELFGR NSCLIARNLL PGLKTCMEIA
     SYMHSGGVSM PHGSIVAPSS IMEEKGKFDA DCTDQEMPSR SRLLRKRGKT RKFKYSWKSA
     GHPSIWKRIA DGKNQSCKQY TPCGCQSMCG KECTCINGGT CCEKYCGCSK SCKNRFRGCH
     CAKSQCRSRQ CPCFAAGREC DPDVCRNCWV SCGDGSLGEP PRRGEGQCGN MRLLLRQQQR
     ILLAKSDVAG WGAFLKNPVN KNDYLGEYTG ELISHREADK RGKIYDRANS SFLFDLNDQY
     VLDAYRKGDK LKFANHSSNP NCYAKVMLVA GDHRVGIFAK EHIDASEELF YDYRYGPDQA
     PPWARKPEGS KRDESTAPQG RAKKHQSH
//