ID A0A154PP19_DUFNO Unreviewed; 749 AA.
AC A0A154PP19;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=WN55_05188 {ECO:0000313|EMBL:KZC13636.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC13636.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC13636.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC13636.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC13636.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-2015) 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};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KQ435007; KZC13636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A154PP19; -.
DR STRING; 178035.A0A154PP19; -.
DR Proteomes; UP000076502; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd19218; SET_EZH2; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR048358; EZH1/2_MCSS.
DR InterPro; IPR044439; EZH2_SET.
DR InterPro; IPR041343; PRC2_HTH_1.
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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR Pfam; PF21358; Ezh2_MCSS; 1.
DR Pfam; PF18118; PRC2_HTH_1; 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; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KZC13636.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZC13636.1}.
FT DOMAIN 507..608
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 615..730
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 173..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 85910 MW; 30B015BCD7ECFD7F CRC64;
MSKAKISAEW RKRVKSEYMR LRQMKRYKRA DEVKIAWNQN RKVMSVEQKR WTDGKAMWLA
MQDIPPHVSC MKKAEITSSD GDVQTCPVKI ISAVTPIPTM YTWAPIQQNF MVEDETVLHN
IPYMGDEILD QDGTFIEELI KNYDGKVHGD RESGFMDDSI FVDLVNALAQ YEKDDKEREH
TKKGKEKEED KDKRDSSSIK AEVKSEKSSE DVKTEVNPFP TMHIFNAISS MFPDKGRPEE
LKEKYIELTE RSDPNVLPPE CTPNIDGVNA KSVPREQTMH SFHTLFCRRC FKYDCFLHRL
QVCHPGPNLQ KRKGPDLKPF SEPCGTECYM HLEGMKEKLA AQAADIKDEE SDEKRGAPRK
VRKQASVDSG NEASSEDSND SNKYSQGGGC QDFKQNVNKE TRPEETMEDQ TQPENQVPFT
LLGLDKRIKT ENELSWTGSE QSLFRALHKA FPGNPCALAQ IMLTKTCQEV YRFAQKEASD
IPAIENLKDF TPPRKKKKKH RLWSMHCRKI QLKKDSGANH VHNFAPCDHP GRQCDNSCPC
IQAQNFCEKF CQCSSECQNR FPGCRCKAQC NTKQCPCYLA VRECDPDLCQ TCGADQFHIT
KISCKNVSVQ RGLHKHLLMA PSDVAGWGIF LKESAAKNEF ISEYCGEIIS QDEADRRGKV
YDKYMCSFLF NLNNDFVVDA TRKGNKIRFA NHSINPNCYA KVMMVNGDHR IGIFAKRAIQ
PGEELFFDYR YGPTEQLKFV GIEREMEFL
//
