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Database: UniProt
Entry: A0A093PJ75_9PASS
LinkDB: A0A093PJ75_9PASS
Original site: A0A093PJ75_9PASS 
ID   A0A093PJ75_9PASS        Unreviewed;       750 AA.
AC   A0A093PJ75;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000256|ARBA:ARBA00024111};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
DE   Flags: Fragment;
GN   ORFNames=N305_11138 {ECO:0000313|EMBL:KFW76913.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW76913.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW76913.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW76913.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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; KL669627; KFW76913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093PJ75; -.
DR   STRING; 328815.ENSMVIP00005014898; -.
DR   Proteomes; UP000053258; 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   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   ECO:0000313|EMBL:KFW76913.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258};
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:KFW76913.1}.
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          184..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..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"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW76913.1"
FT   NON_TER         750
FT                   /evidence="ECO:0000313|EMBL:KFW76913.1"
SQ   SEQUENCE   750 AA;  85936 MW;  0E736F5634EDABAE CRC64;
     RIIMGQTGKK SEKGPICWRK RVKSEYMRLR QLKRFRRADE VKSMFNSNRQ KILERTEILN
     QEWKQRRIQP VHIMTSVSSL RGTRECSVTS DIDFPKQVIP LKTLNAVASV PIMYSWSPLQ
     QNFMVEDETV LHNIPYMGDE VLDQDGTFIE ELIKNYDGKV HGDRECGFIN DEIFVELVNA
     LGQYSDDEDD DDGDDNPEER DDKQKDREGN RMEKESRPPR RFPSDKIFEA ISSMFPDKGT
     AEELKEKYKE LTEQQLPGAL PPECTPNIDG PNAKSVQREQ SLPSFHTLFC RRCFKYDCFL
     HPFHATPNTY KRKNTETALD NKPCGPHCYQ HLEGAKEFAA ALTAERIKTP PKRPGGRRRG
     RLPNNTSRPS TPTINVLESK DTDSDREAGT ETGGENNDKE EEEKKDETSS SSEANSRCQT
     PIKMKPNIEP PENVEWSGAE ASMFRVLIGT YYDNFCAIAR LIGTKTCRQV YEFRVKESSI
     IAPVPAEDVD TPPRKKKRKH RLWAAHCRKI QLKKDGSSNH VYNYQPCDHP RQPCDSSCPC
     VIAQNFCEKF CQCSSECQNR FPGCRCKAQC NTKQCPCYLA VRECDPDLCL TCGAADHWDS
     KNVSCKNCSI QRGSKKHLLL APSDVAGWGI FIKDPVQKNE FISEYCGEII SQDEADRRGK
     VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF ANHSVNPNCY AKVMMVNGDH RIGIFAKRAI
     QTGEELFFDY RYSQADALKY VGIEREMEIP
//
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