Protein kinase Spk1

Function Protein kinase Spk1 (Rad53) is a yeast serine/threonine protein kinase which phosphorylates proteins on serene, threonine and tyrosine. Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints. Rad53 phosphorylates proteins at serine, threonine and tyrosine residues. Structural highlights Rad53 contains phosphothreonine recognition domains: FHA1 at the N-terminal (residues 1-164) which selects for Asp at position +3 relative to phosphothreonine and FHA2 at the C-terminal (residues 573-730) which selects for Ile at position +3 relative to phosphothreonine. Two SCD - SQ/TQ-rich cluster domains – are flanking the kinase domain. SCD domain is associated with DNA-damage-response proteins. The yeast FHA1 domain interacts with peptide containing phosphothreonine.

spinqualitylabelsall models Structure of yeast Rad53 FHA1 domain (grey) complex with phosphothreonine peptide (green) (PDB code 2a0t). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of protein kinase Spk13D structures of protein kinase Spk1

Updated on 18-July-2016

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• Rad53 FHA1 domain
  • 1k3j – yRad53 FHA1 domain – yeast - NMR
    
  • 1g3g, 1j4o – yRad53 FHA1 domain (mutant) - NMR
    
  • 1j4p, 1j4q, 1k3n, 1k3q – yRad53 FHA1 domain + Rad9 peptide - NMR
    
  • 1g6g, 2a0t, 2jqi – yRad53 FHA1 domain + phosphothreonine peptide
    
• Rad53 FHA2 domain
  • 1qu5, 1dmz, 1fhq – yRad53 FHA2 domain – yeast - NMR
    
  • 1fhr, 1j4k, 1j4l, 1k2m, 1k2n – yRad53 FHA2 domain + Rad9 peptide - NMR
    
• Rad53 kinase and SCD2 domains
  • 4pdp – yRad53 kinase and SCD2 domain (mutant)
    
  • 4pds – yRad53 kinase and SCD2 domain (mutant) + AMPPNP