Dbf4 motifs: conserved motifs in activation subunits for Cdc7 kinases essential for S-phase

Biochem Biophys Res Commun. 2000 Aug 18;275(1):228-32. doi: 10.1006/bbrc.2000.3281.

Abstract

Dbf4 and its related molecules were originally identified as cyclin-like partners for Cdc7 kinases, essential for S-phase. Recent reports and database search indicate the presence of multiple Dbf4-related molecules with distinct functions. We have identified three stretches of amino acids which are conserved in various Dbf4-related molecules and possibly play distinct functions in binding to and activation of the catalytic subunits as well as in interactions with other proteins. Discovery of conserved motifs for this possible new protein family would serve as a useful framework for future identification of new members of this family as well as for probing their functions.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • BRCA1 Protein / chemistry
  • Cell Cycle Proteins / metabolism*
  • Conserved Sequence*
  • Enzyme Activation
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Protein Binding
  • Protein-Serine-Threonine Kinases / metabolism*
  • S Phase*
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment
  • Zinc Fingers

Substances

  • BRCA1 Protein
  • Cell Cycle Proteins
  • Dbf4 protein, S cerevisiae
  • Fungal Proteins
  • Macromolecular Substances
  • Saccharomyces cerevisiae Proteins
  • CDC7 protein, S cerevisiae
  • Protein-Serine-Threonine Kinases