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Database: UniProt
Entry: A0A2K6PUW4_RHIRO
LinkDB: A0A2K6PUW4_RHIRO
Original site: A0A2K6PUW4_RHIRO 
ID   A0A2K6PUW4_RHIRO        Unreviewed;       695 AA.
AC   A0A2K6PUW4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
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:ENSRROP00000020316.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000020316.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000020316.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A2K6PUW4; -.
DR   Ensembl; ENSRROT00000044493.1; ENSRROP00000020316.1; ENSRROG00000034033.1.
DR   GeneTree; ENSGT00940000155013; -.
DR   Proteomes; UP000233200; 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; 1.20.58.1880; -; 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:UP000233200};
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          454..554
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          561..676
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          171..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..186
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  79619 MW;  8FA3388ECC3536EF CRC64;
     MGQTGKRSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW
     KQRRIQPVHI LTSCSVTSDL DFPTQVIPLK TLNAVASVPI MYSWSPLQQN FMVEDETVLH
     NIPYMGDEVL DQDGTFIEEL IKNYDGKVHG DRECGFINDE IFVELVNALG QYNDDDDDDD
     GDDPEEREEK QKDLEDHRDD KESRPPRKFP SDKIFEAISS MFPDKGTAEE LKEKYKELTE
     QQLPGALPPE CTPNIDGPNA KSVQREQSLH SFHTLFCRRC FKYDCFLHPF HATPNTYKRK
     NTEAALDNKP CGPQCYQHLE GAKEFAAALT AERIKTPPKR PGGRRRGRLP NNSSRPSTPT
     INVLESKDTD SDREAGTETG GENNDKEEEE KKDETSSSSE ANSRCQTPIK MKPNIEPPEN
     VEWSGAEASM FRVLIGTYYD NFCAIARLIG TKTCRQVYEF RVKESSIIAP APAEDVDTPP
     RKKKRKHRLW AAHCRKIQLK KGQNRFPGCR CKAQCNTKQC PCYLAVRECD PDLCLTCGAA
     DHWDSKNVSC KNCSIQRGSK KHLLLAPSDV AGWGIFIKDP VQKNEFISEY CGEIISQDEA
     DRRGKVYDKY MCSFLFNLNN DFVVDATRKG NKIRFANHSV NPNCYAKVMM VNGDHRIGIF
     AKRAIQTGEE LFFDYRYSQA DALKYVGIER EMEIP
//
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