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Database: UniProt
Entry: A0A2K5I8P5_COLAP
LinkDB: A0A2K5I8P5_COLAP
Original site: A0A2K5I8P5_COLAP 
ID   A0A2K5I8P5_COLAP        Unreviewed;       707 AA.
AC   A0A2K5I8P5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000012916.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000012916.1}
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; A0A2K5I8P5; -.
DR   Ensembl; ENSCANT00000035828.1; ENSCANP00000012916.1; ENSCANG00000029791.1.
DR   Proteomes; UP000233080; 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:UP000233080};
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          146..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        147..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  80689 MW;  E9688A9D99D8F948 CRC64;
     MEIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
     KKLRVQPVQS MKPVSGHPFL KKVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG
     EEEMIPGSVL ISDAVFLELV DALNQYSDDE EDGHNDTSDG KQDDSKEDLP VTRKRKRHAI
     EGNKKSSKKQ FPNDMIFSAI ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP
     NAKSVQREQS LHSFHTLFCR RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL
     LEGAKEYAML HNPRSKCSGR RRRRHHMVSA SCSNASASAV AETKEGDSDR DTGNDWASSS
     SEANSRCQTP TKQKASPAPP 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 ERETDVL
//
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