ID A0A369S3Q8_9METZ Unreviewed; 684 AA.
AC A0A369S3Q8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN ORFNames=TrispH2_007277 {ECO:0000313|EMBL:RDD40683.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD40683.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD40683.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD40683.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD40683.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDD40683.1}.
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DR EMBL; NOWV01000094; RDD40683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369S3Q8; -.
DR STRING; 287889.A0A369S3Q8; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
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; cd10519; SET_EZH; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR041355; Pre-SET_CXC.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR PANTHER; PTHR45747:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR Pfam; PF21358; Ezh2_MCSS; 1.
DR Pfam; PF18264; preSET_CXC; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:RDD40683.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDD40683.1}.
FT DOMAIN 421..542
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 549..664
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
SQ SEQUENCE 684 AA; 78919 MW; 28265E3C834C6144 CRC64;
MTEWNTKRFI RSEYSKLRHT RRIFHQQQAK SLYVENCSYV KEALKKRDDK LGNFHFLPVG
RHKSAVAKGN DSENYVSIYV KRINLEILQR TLVDVTPPPR FTFYKPVQKN YLVDDETELH
NIPYMGDEVL DQDGEFIEEL INNYDGKVHD SPAHDDNFND LLFVELVKII SGKYRSEKGQ
NSSSIDYQER VPPAIFTAVA KAFSDTNQFQ GSAEDLRDRF NSAIKRLFHT HKNTECAPDI
DGPDCKAVSR SESLHSFNTL FCRRCFKYDC CTHTWTGPPV KIRRKTPVNA SEAKSCGQKC
WLLEVDNIQG NSGATGSSNN IQLNGCNSTS VMIKSEIISE GNKSDSWTGA EISLFRVLQP
IYVNDYCTIA NLIQTKNCKQ VREYALQVLD EEHLMEKESK PVQNNIHKKK RRNMRVWVNH
CRKFQQRRGK DDTSQVITYT PCNHPNRPCD SSCPCIQTHN FCEKYCQCDR DYLYDYIKFV
CLIMEYCLAG KNRFPGCRCR AQCNTKQCPC VLAVRECDPD LCQQCGASKF DDYSNPSCKN
VLIQRGIKKH LLLAPSDIAG WGIFSRYEIH KNDFISEYCG EMISQDEADR RGKVYDKSKC
SFLFNLNNEF VVDATRKGNK IRFANHSTNP NCYAKVMMVN GDHRIGIYAK RDIQAGEELF
FDYRYGPTDA LKYVNIERDS TDLE
//
