{
  "@type": "dcat:Dataset",
  "accessLevel": "public",
  "bureauCode": [
    "009:25"
  ],
  "contactPoint": {
    "@type": "vcard:Contact",
    "fn": "NIH",
    "hasEmail": "mailto:info@nih.gov"
  },
  "description": "Background\n          Viral DNA-binding proteins have served as good models to study the biochemistry of transcription regulation and chromatin dynamics. Computational analysis of viral DNA-binding regulatory proteins and identification of their previously undetected homologs encoded by cellular genomes might lead to a better understanding of their function and evolution in both viral and cellular systems.\n        \n        \n          Results\n          The phyletic range and the conserved DNA-binding domains of the viral regulatory proteins of the poxvirus D6R/N1R and baculoviral Bro protein families have not been previously defined. Using computational analysis, we show that the amino-terminal module of the D6R/N1R proteins defines a novel, conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain is suggested to be homologous to the fungal DNA-binding APSES domain. We provide evidence for the KilA-N and APSES domains sharing a common fold with the nucleic acid-binding modules of the LAGLIDADG nucleases and the amino-terminal domains of the tRNA endonuclease. The amino-terminal module of the Bro proteins is another, distinct DNA-binding domain (the Bro-N domain) that is present in proteins whose domain architectures parallel those of the KilA-N domain-containing proteins. A detailed analysis of the KilA-N and Bro-N domains and the associated domains points to extensive domain shuffling and lineage-specific gene family expansion within DNA virus genomes.\n        \n        \n          Conclusions\n          We define a large class of novel viral DNA-binding proteins and their cellular homologs and identify their domain architectures. On the basis of phyletic pattern analysis we present evidence for a probable viral origin of the fungus-specific cell-cycle regulatory transcription factors containing the APSES DNA-binding domain. We also demonstrate the extensive role of lineage-specific gene expansion and domain shuffling, within a limited set of approximately 24 domains, in the generation of the diversity of virus-specific regulatory proteins.",
  "distribution": [
    {
      "@type": "dcat:Distribution",
      "description": "Visit the original government dataset for complete information, documentation, and data access.",
      "downloadURL": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC88810/",
      "mediaType": "text/html",
      "title": "Official Government Data Source"
    }
  ],
  "identifier": "https://healthdata.gov/api/views/gvnw-kb7h",
  "issued": "2025-07-14",
  "keyword": [
    "dna-binding-proteins",
    "domain-shuffling",
    "nih",
    "transcription-regulation",
    "viral-proteins"
  ],
  "landingPage": "https://healthdata.gov/d/gvnw-kb7h",
  "modified": "2025-09-06",
  "programCode": [
    "009:033"
  ],
  "publisher": {
    "@type": "org:Organization",
    "name": "National Institutes of Health"
  },
  "theme": [
    "NIH"
  ],
  "title": "Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors"
}