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Database: UniProt
Entry: A0A3L6RX28_PANMI
LinkDB: A0A3L6RX28_PANMI
Original site: A0A3L6RX28_PANMI 
ID   A0A3L6RX28_PANMI        Unreviewed;       906 AA.
AC   A0A3L6RX28;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   SubName: Full=Histone-lysine N-methyltransferase EZ1 isoform X2 {ECO:0000313|EMBL:RLN11511.1};
GN   ORFNames=C2845_PM09G03980 {ECO:0000313|EMBL:RLN11511.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN11511.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLN11511.1}.
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DR   EMBL; PQIB02000006; RLN11511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6RX28; -.
DR   STRING; 4540.A0A3L6RX28; -.
DR   Proteomes; UP000275267; Chromosome 9.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:RLN11511.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RLN11511.1}.
FT   DOMAIN          640..739
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          754..869
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..895
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  100769 MW;  672473F8050A88C2 CRC64;
     MEAAAAAAAS SASASASAGR SRPSTSAAQV TSITGVRAEE ENAASPYVLT VIDSLKKRIT
     ADRLTYIKNR IGENKANLST FTQRTYNLSK NRQNNTSKGT DLAPNLLTKR QDDALCTLHS
     VDICPADKDG SNFQDESPFS SSNVILGGNL NAKNAIRPIK LPEASKLPPY TTWIFLDRNQ
     RMSEDQSVLG RRRIYYDASC GEALICSDSE DEAIEDEEEK KEFKHSEDCI IQMTVQECGM
     SDAARYEILH GEKTQDSCKK VTEQNARVED LYGDKDLDAA LDSFDNLFCR RCLVFDCKLH
     GCSQDLVFPT EKQQAWNGIA DSVPCGLHCH KQASEPDSVA AIDHMLIDGE EPTHPSGNAT
     NQPGTDRKKN GSSGRKTKSQ QSETSSTARA VSESSDSEVH PISNKSPQPS PSPSKVKIGP
     KGGIRKITNR RIAERILMSV KKGQREMASS DSNSVSESPL AARDTRILLR SDARNGNKES
     IVSSQDTPNT RSIRKKITPQ FGNSSASAEA QNDSMEEDGY DSSRKEEFVD ENICKQEDNF
     RSWKPIEQGL LVKGLEIFGR NSCLIARNLL GGMKTCRDVF QYMNYIENSS ASGTLSGVDS
     LVKGYIKGNE LRSRSRFFRR RGKVRRLKYT WKSAGYHSIR KRITERKDQP CRQYNPCGCQ
     SACGKQCPCL TNATCCEKYC GCSKICKNRF RGCHCAKSQC RSRQCPCFAA DRECDPDVCR
     NCWVGCGDGT LGVPNQRGDN YECRNMKLLL KQQQRVLLGR SDVSGWGAFL KNSVSKHEYL
     GEYTGELISH KEADKRGKIY DRENSSFLFN LNNEFVLDAY RMGDKLKFAN HSPDPNCYAK
     VIMVAGDHRV GIFAKERILA GEELFYDYRY EPDRAPAWAR KPEDSRGKDD GPSNGRAKKL
     AQNTRG
//
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