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Database: UniProt
Entry: A0A2K6GEV6_PROCO
LinkDB: A0A2K6GEV6_PROCO
Original site: A0A2K6GEV6_PROCO 
ID   A0A2K6GEV6_PROCO        Unreviewed;       707 AA.
AC   A0A2K6GEV6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN   Name=EZH1 {ECO:0000313|Ensembl:ENSPCOP00000024756.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000024756.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000024756.1}
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; A0A2K6GEV6; -.
DR   Ensembl; ENSPCOT00000035440.1; ENSPCOP00000024756.1; ENSPCOG00000024585.1.
DR   GeneTree; ENSGT00940000156604; -.
DR   OMA; XEGAKEY; -.
DR   Proteomes; UP000233160; 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   CDD; cd00167; SANT; 1.
DR   CDD; cd19217; SET_EZH1; 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; IPR044438; EZH1_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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EZH1; 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   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
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          464..566
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          573..688
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          148..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  80778 MW;  A71B952A633D3F77 CRC64;
     MDIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
     KKLRVQPVQL MKPVSGHPFL KKVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG
     EEEMIPGSVL ISDAVFLELV DALNQYSDEE EEGHNDTSDG KQDDSKEDLP VTRKRKRHAI
     EGNKKSSKKQ FPNDMIFSAI ASMFPENGVP DDMKERYREL TEMSDPDALP PQCTPNIDGP
     NAKSVQREQS LHSFHTLFCR RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL
     LEGAKEYAML HNPRSKCSGR RRRRHHVVSA SCSNTSASAV AETKEGDSDR DTGNDWASSS
     SEANSRCQTP TKQKSSPAPP QLCVVEAPSE PVEWTGAEES LFRVFHGTYF NNFCSIARLL
     GTKTCKQVFQ FAVKESLILK LPTDELMNPS QKKKRKHRLW AAHCRKIQLK KDNSSTQVYN
     YQPCDHPDRP CDSTCPCIMT QNFCEKFCQC NPDCQNRFPG CRCKTQCNTK QCPCYLAVRE
     CDPDLCLTCG ASEHWDCKVV SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS
     EYCGELISQD EADRRGKVYD KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV
     VMVNGDHRIG IFAKRAIQAG EELFFDYRYS QADALKYVGI ERETDVF
//
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