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    NCU06266 histone-lysine N-methyltransferase [ Neurospora crassa OR74A ]

    Gene ID: 3879023, updated on 6-Jun-2024

    Summary

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    Gene symbol
    NCU06266
    Gene description
    histone-lysine N-methyltransferase
    Locus tag
    NCU06266
    See related
    FungiDB:NCU06266; VEuPathDB:NCU06266
    Gene type
    protein coding
    RNA name
    histone-lysine N-methyltransferase
    RefSeq status
    PROVISIONAL
    Organism
    Neurospora crassa OR74A (strain: OR74A)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora
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    Genomic context

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    See NCU06266 in Genome Data Viewer
    Location:
    other: III
    Exon count:
    2
    Sequence:
    Chromosome: III; NC_026503.1 (2127490..2130283)

    Linkage Group III - NC_026503.1Genomic Context describing neighboring genes Neighboring gene hypothetical protein Neighboring gene hypothetical protein Neighboring gene autophagy protein 16 Neighboring gene vacuolar protein sorting-associated protein Neighboring gene FHA domain-containing protein Neighboring gene mitochondrial processing peptidase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_026503.1

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The genome sequence of the filamentous fungus Neurospora crassa. Galagan JE, et al. Nature, 2003 Apr 24. PMID 12712197
    2. Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Burge S, et al. Database (Oxford), 2012. PMID 22301074, Free PMC Article
    3. TreeGrafter: phylogenetic tree-based annotation of proteins with Gene Ontology terms and other annotations. Tang H, et al. Bioinformatics, 2019 Feb 1. PMID 30032202, Free PMC Article

    GeneRIFs: Gene References Into Functions

    General gene information

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    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables histone H3K79 methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    enables histone binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in DNA damage checkpoint signaling IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in DNA repair IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in regulation of transcription regulatory region DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in subtelomeric heterochromatin formation IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of nucleosome IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Names
    histone-lysine N-methyltransferase

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_026503.1 Reference assembly

      Range
      2127490..2130283
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_957777.2 → XP_962870.1  histone-lysine N-methyltransferase [Neurospora crassa OR74A]

      See identical proteins and their annotated locations for XP_962870.1

      Status: PROVISIONAL

      UniProtKB/Swiss-Prot
      Q7SB74
      Conserved Domains (1) summary
      pfam08123
      Location:330 → 530
      DOT1; Histone methylation protein DOT1
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q7SB74.1

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Molecular Biology Databases
    Research Materials