ID A0A484BQY8_DRONA Unreviewed; 741 AA.
AC A0A484BQY8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=AWZ03_002265 {ECO:0000313|EMBL:TDG51178.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG51178.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG51178.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG51178.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG51178.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:TDG51178.1}.
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DR EMBL; LSRL02000010; TDG51178.1; -; Genomic_DNA.
DR RefSeq; XP_017957819.1; XM_018102330.1.
DR AlphaFoldDB; A0A484BQY8; -.
DR STRING; 7232.A0A484BQY8; -.
DR GeneID; 108652219; -.
DR OMA; CYMHLEG; -.
DR OrthoDB; 902834at2759; -.
DR Proteomes; UP000295192; 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; cd00167; SANT; 1.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000295192};
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}.
FT DOMAIN 500..600
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 607..722
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 172..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 84824 MW; 802A686652B4F88F CRC64;
MSSKEWKRVV KLEYMKIRQQ KRYKRADEIK EAWIKNWDEH NHNVQDLYCD SKVWQAKPYN
PPHVDCVKRA EVTSYNGPNS GPQRVPICVI NAVTPIPTMY TWAPTQQNFM VEDETVLHNI
PYMGDEVLDK DGKFIEELIK NYDGKVHGDK DPSFMDDAIF VELVHALMRS HNKDLEEPTS
SSSVKTETAT TSKVKEEDEK DVTPAIPEPA TEFPSAVEDE KEESFNADVT DTKGKVEKVK
EKLPFPAPII FQAISANFPD KGTAQELKEK YIELTEHQDP ERPQECTPNI DGIKAESVSR
ERTMHSFHTL FCRRCFKYDC FLHRLQGHAG PNLQKRRYPE LKAFAEPCSN SCYMLIDGMK
EKLAADSKTP PIDSCNEASS EDSNDSNSQF SNKDFNPENG KDNSIAVNSA EINSIMAGMM
NITSTQCVWT GADQALFRVL HKVYLKNYCA VAHNMLTKTC RQVYEFAQKE AAEFSFEDLR
QDFTPPRKKK KKQRLWSLHC RKIQLKKDSS SNHVYNYTPC DHAGPCDMNC SCIQTQNFCE
KFCNCSSDCQ NRFPGCRCKA QCNTKQCPCY LAVRECDPDL CQACGADQFK LTKITCKNVC
VQRGLHKHLL MAPSDIAGWG IFLKEGAQKN EFISEYCGEI ISQDEADRRG KVYDKYMCSF
LFNLNNDFVV DATRKGNKIR FANHSINPNC YAKVMMVTGD HRIGIFAKRA IQPGEELFFD
YRYGPTEQLK FVGIEREMEI V
//
