ID A0A436ZW83_9PEZI Unreviewed; 468 AA.
AC A0A436ZW83;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0000256|PIRNR:PIRNR009343};
DE EC=2.1.1.355 {ECO:0000256|PIRNR:PIRNR009343};
GN ORFNames=DFL_007429 {ECO:0000313|EMBL:RVD83025.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD83025.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD83025.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD83025.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000256|PIRNR:PIRNR009343};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009343}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000256|PIRNR:PIRNR009343}.
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:RVD83025.1}.
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DR EMBL; SAEB01000009; RVD83025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZW83; -.
DR STRING; 97331.A0A436ZW83; -.
DR VEuPathDB; FungiDB:DFL_007429; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR011381; H3-K9_MeTrfase_SUV39H1/2-like.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46223:SF3; HISTONE H3 (LYS9) METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009343; SUV39_SET; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR009343};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR009343};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR009343}; Nucleus {ECO:0000256|PIRNR:PIRNR009343};
KW Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR009343};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR009343};
KW Zinc {ECO:0000256|PIRNR:PIRNR009343, ECO:0000256|PIRSR:PIRSR009343-2}.
FT DOMAIN 26..84
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 224..293
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 296..436
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 452..468
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 97..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
SQ SEQUENCE 468 AA; 53425 MW; B5C2C15BC0234DEF CRC64;
MAEVEGLPTI VGSKSAETLQ PGAVEYEVSK IIDEKFVDTP VYLVRWKNYS KEHDSWEPYS
NIKNCEKVLQ KWELKKLAKQ KSQSQLLEIT SAGGDITVVK KRGPGRPKGS KDKEPRTRKS
RKRSRSESND SEVESVVSTK KSNSTTQSLQ KLQIYSPIGS DPSDKTPKHP DRLKFLKKLK
HLKGPEITVV NTVDTVPCPP LEFTFIDDYV YRDGVPVPNP DFNWGCRCKH AFGCQTTNTD
CECVEANHDD LQRLAYKHKG LLKYPTENAY AIHECNEKCA CNIRCPNKVV LKGRQVPLEI
FKTEHKGWGL RCPIDLDAGQ FIDRYIGEVI TEHEAERRTK IQENRGLTYL FDLDKFVEED
EEDSEGENGD ETTKKEVYCV DGADYGGVTR FINHSCEPNM MVHAVTHNRS DLRTYDLALF
TSRKIPAGEE LTFEYVRNDS WKPGDPIPED KMKFPCYCGA EKCYGWLF
//
