Evidence for a second conserved arginine residue in the integrase family of recombination proteins

Protein Eng. 1992 Jan;5(1):87-91. doi: 10.1093/protein/5.1.87.


This study was designed to search for new regions of similarity in the integrase family of recombination proteins which consists of 28 members found in bacteria and yeast. A computer method based on an information content analysis has been used to align local regions of homology in the set of unaligned protein sequences from this family. Among the aligned regions with high information content were those containing the known conserved histidine, arginine and tyrosine residues. In addition, a new region was identified containing another arginine residue that appears to be conserved in all members of the family. To test further the importance of this newly identified arginine residue, mutants in the Cre protein from phase P1, a member of this integrase family, have been constructed which alter this residue. The mutations which change arginine to lysine and arginine to cysteine depress catalytic activity but not site-specific binding to the lox site. This result is expected for a conserved active site residue. This computer analysis also provides a means for searching for new members of the integrase family.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Bacteriophages / enzymology*
  • DNA Nucleotidyltransferases / chemistry*
  • DNA Nucleotidyltransferases / genetics
  • Integrases
  • Molecular Sequence Data
  • Multigene Family*
  • Mutagenesis, Site-Directed
  • Recombination, Genetic*
  • Sequence Alignment / methods
  • Sequence Homology, Nucleic Acid
  • Structure-Activity Relationship
  • Viral Proteins*


  • Viral Proteins
  • Cre recombinase
  • DNA Nucleotidyltransferases
  • Integrases