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Database: UniProt
Entry: A0A3Q3X759_MOLML
LinkDB: A0A3Q3X759_MOLML
Original site: A0A3Q3X759_MOLML 
ID   A0A3Q3X759_MOLML        Unreviewed;       685 AA.
AC   A0A3Q3X759;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000256|ARBA:ARBA00024111};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000021249.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000021249.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A3Q3X759; -.
DR   STRING; 94237.ENSMMOP00000021249; -.
DR   Ensembl; ENSMMOT00000021605.1; ENSMMOP00000021249.1; ENSMMOG00000016160.1.
DR   OMA; CYMHLEG; -.
DR   Proteomes; UP000261620; Unplaced.
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:SF18; 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:UP000261620};
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          442..544
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          551..666
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          276..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  78642 MW;  26C2AD0DA238FAFD CRC64;
     MVLTGKRSEK GPACWKRRVK SEYMRLRQLK RFRRADEVKS MFSTNRQKIM ERTDILNQEW
     KTRRIQPVHI MTSVGSLRGT REVEDETVLH NIPYMGDEIL DQDGTFIEEL IKNYDGKVHG
     DRECGFINDE IFVELVSALA QYSDNEDDEE EEEHDYKKFP SDKIFEAISS MFPDKGSTEE
     LKEKYKELTE QQLPGALPPE CTPNIDGPNA RSVQREQSLH SFHTLFCRRC FKYDCFLHPF
     HATPNTYKRK NLENLVDSKP CGIDCYMCLD GMASEYPTGV VPERSKTPSK RTVGRRRGRL
     PNSSSRPSTP TISSETKDTD SDREGSKEDE RENEKDDEDK KDENTSSSEG NSRCQTPVKL
     KLTGEAEAVE WSGAEASLFR VLIGTYYDNF CAIARLIGTK TCRQVYEFRV KESSIIARAP
     AEDEDTPPRK KKRKHRLWAT HCRKIQLKKD GSSNHVYNYQ PCDHPRQPCD SSCPCVTAQN
     FCEKFCQCSS ECQNRFPGCR CKAQCNTKQC PCYLAVRECD PDLCLTCGAA DHWDSKNVSC
     KNCSIQRGAK KHLLLAPSDV AGWGIFIKEP VQKNEFISEY CGEIISQDEA DRRGKVYDKY
     MCSFLFNLNN DFVVDATRKG NKIRFANHSV NPNCYAKVMM VNGDHRIGIF AKRAIQTGEE
     LFFDYRYSQA DALKYVGIER EMEIA
//
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