ID D8S9D0_SELML Unreviewed; 820 AA.
AC D8S9D0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=[Histone H3]-lysine(27) N-trimethyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_111860 {ECO:0000313|EMBL:EFJ18941.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ18941.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377608; EFJ18941.1; -; Genomic_DNA.
DR RefSeq; XP_002980071.1; XM_002980025.1.
DR AlphaFoldDB; D8S9D0; -.
DR STRING; 88036.D8S9D0; -.
DR EnsemblPlants; EFJ18941; EFJ18941; SELMODRAFT_111860.
DR Gramene; EFJ18941; EFJ18941; SELMODRAFT_111860.
DR KEGG; smo:SELMODRAFT_111860; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_011060_0_0_1; -.
DR InParanoid; D8S9D0; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 559..657
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 672..787
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 365..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 91908 MW; E4BA710E2EF3518F CRC64;
MAALSATFTR LKKQVAFERQ AYVKARMDAN SERLQGFCTH LLALSSSRAV NNRNHADNDM
LNTRIQKALN KLGTDPAAAD QQCGSQDDSS APILFNNSGG KSIVKPVRLQ TVQKTPPYTT
WIFLDRNQRM AEDQSVVGRR RIYYDSAENE ALICSDSEEE QVEEEEEKRD FSKGDDFLIR
ATVQEHGSSK MVFKALADCL DAKPSEIEAR YEILAKDGDK LKSEEKHDLL SAMDSFDNLF
CRRCLVFDCR LHGCSQPVII PFDKQTPLNK TGELPSVPCG PCCFHLPRLS SHHDATSSGV
ESKPVPVEST APAIEKSWQV PDSKDKGVAT EPVAKTVDKP PEAPKKSFKD KSVTALRRLL
LKRKATRHTD DDTNEARKKH HVEGSHAEVG DGSGNATRGE NTGASMYLKK LVSKKLYAQR
KWKGSQITTV KRPPPVIKES EDVMQSISKN LTLYDSNWNT LEKDLYETGL QIFGRDSCLI
SRNLLRGMKS CAEVGEFMQL EAAVNWKLNE ETKLQQDGNT VIEDATIDRS RSRLYNGRRR
GRVRRLKYTW KSVGYPAIRK RLVDGKDGCR QYTPCSCSES CGKQCSCHRN GTCCEKYCGC
SKNCKNRFRG CHCAKSQCSS RQCPCFAAGR ECDPDVCRNC WIGCGDGSQG GPPARGDSYE
CRNMKLLLKQ QQRVLLGRSD VAGWGAFLKT PVNKHDYLGE YTGELISHRE ADKRGKIYDR
ENSSFLFNLN DQYVLDACRK GDKLKFANHS PNPNCYAKVI MVAGDHRVGI FAKERISAGE
ELFYDYRYEA DRAPPWARKP EDGQKNDEAA SGSGRAQKTA
//
