A0A2S6BY91 · A0A2S6BY91_9PEZI

  • Protein
    Histone-lysine N-methyltransferase, H3 lysine-79 specific
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.

Miscellaneous

In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Activity regulation

Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular Functionhistone H3K79 trimethyltransferase activity
Biological ProcessDNA damage checkpoint signaling
Biological ProcessDNA repair
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone-lysine N-methyltransferase, H3 lysine-79 specific
  • EC number
  • Alternative names
    • Histone H3-K79 methyltransferase

Gene names

    • ORF names
      CBER1_10311

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS538.71
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetidae > Mycosphaerellales > Mycosphaerellaceae > Cercospora

Accessions

  • Primary accession
    A0A2S6BY91

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-30Disordered
Compositional bias9-30Polar residues
Domain117-435DOT1
Region380-432Disordered
Compositional bias389-432Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    469
  • Mass (Da)
    53,356
  • Last updated
    2018-07-18 v1
  • Checksum
    EEC6C27C56EFD184
MGIMASMMTRNQKRKQQTESFNNTHQEATNTSGDVLLQELRWLLHGGHANFTAFLPSTPTHQDEPMGRYAGPFLARLHHSADNYDPAPNNTLYLRYPPSGAIERFTLSKRTHKHTHRHARPLDPIDDIVRTIQVFHIQVGKLTSPEIDTMGRMIYRTFEHFINTNNFYPLQRLITNLTDPAFFPLATHLSLSPPFDLTTHFLAQLHDRIIADAAHNLSRPSTSKNLEPTYGELLPPFLQTLFLQTNLNENSTYLDLGSGVGQTCLQASLTTGCLSYGIERESRSAGLAALHLGQFHERTKLWGLATEQENFEDRIVLRLGDFLKLECVKEWLGRADVVLVNNLKLEPETDLALVRMLGGREGVRKGTRVISTRGLVPVGRTRSGSKVGGKRKRGLEDDCEGKRRKVEKEKTNGKREKMQPQPEENEGENDIMAVRCGEDEKWTWKEYVYEAGSVSWKNKSDFYYISVRK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-30Polar residues
Compositional bias389-432Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PNEN01001696
EMBL· GenBank· DDBJ
PPJ52442.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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