ID H3ANA1_LATCH Unreviewed; 750 AA.
AC H3ANA1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000256|ARBA:ARBA00024111};
DE EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN Name=EZH2 {ECO:0000313|Ensembl:ENSLACP00000011122.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011122.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000011122.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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; AFYH01150065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01150074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3ANA1; -.
DR STRING; 7897.ENSLACP00000011122; -.
DR Ensembl; ENSLACT00000011205.1; ENSLACP00000011122.1; ENSLACG00000009785.1.
DR eggNOG; KOG1079; Eukaryota.
DR GeneTree; ENSGT00940000155013; -.
DR HOGENOM; CLU_011342_0_0_1; -.
DR InParanoid; H3ANA1; -.
DR OMA; CYMHLEG; -.
DR TreeFam; TF314509; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009785; Expressed in chordate pharynx and 6 other cell types or tissues.
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 GO; GO:0048511; P:rhythmic process; 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; IPR021654; EZH1/EZH2.
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:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE EZH2; 1.
DR Pfam; PF21358; Ezh2_MCSS; 1.
DR Pfam; PF11616; EZH2_WD-Binding; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
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:UP000008672};
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 507..609
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 616..731
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 342..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 85631 MW; A5A2F91D100BFB60 CRC64;
RRTMGQTGRK SEKGPVCWRR RVKSEYMRLR QLKRFRRADE VKSMFNSNRQ KIQEKTEILN
QEWKQRRIQP VHIMTSVSSL RGTRECSVMS DLDFPKQVIP LKTLNAVASV PIMYSWSPLQ
QNFMVEDETV LHNIPYMGDE VLDQDGTFIE ELIKNYDGKV HGDRGETLFF NGVIFTDLKA
GLTQRSDADS SSAGHDANGL CQHKRSIRPS RPCKESQAPR KFPSDKIFEA ISSMFPDKGT
AEELKEKYKE LTEQQLPGAL PPECTPNIDG PNAKSVQREQ SLHSFHTLFC RRCFKYDCFL
HPFHATPNTY KRKNTETIVE TKPCGPECYQ YLEGAREFAA SLTAERIKTP PKRTGGRRRG
RLPNSTSRPS TPTVNVSEAK DTDSDREAGT ETGGENNDKE EEEKKEETSS SSEANSRCQT
PVKIKMSMDP PENVEWSGAE ASMFRVLIGT YYDNFCAIAR LIGTKTCRQV YDFRVKESTI
IAPVPTEDAD TPPRKKKRKH RLWAAHCRKI QLKKDGSSNH VYNYQPCDHP RQPCDNSCPC
VIAQNFCEKF CQCSSECQNR FPGCRCKAQC NTKQCPCYLA VRECDPDLCL TCGACDHWDS
KNVSCKNCSI QRGSKKHLLL APSDVAGWGI FIKEPVQKNE FISEYCGEII SQDEADRRGK
VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF ANHSVNPNCY AKVMMVNGDH RIGIFAKRAI
QTGEELFFDY RYSQADALKY VGIEREMEIP
//