The bacterial recA protein [1,2,3,E1] is essential for homologous
recombination and recombinational repair of DNA damage. RecA has many
activities: it filaments, it binds to single- and double-stranded DNA, it
binds and hydrolyzes ATP, it is also a recombinase and, finally, it interacts
with lexA causing its activation and leading to its autocatalytic cleavage.
RecA is a protein of about 350 amino-acid residues. Its sequence is very well
conserved [3,4,5,E1] among eubacterial species. It is also found in the
chloroplast of plants .
The recA protein is closely related to:
Eukaryotic RAD51 protein. Promotes homologous pairing and strand exchange
Eukaryotic DMC1 protein. Participates in meiotic recombination.
Prokaryotic radA protein. Involved in DNA repair and in homologous
Bacteriophage uvsX gene product. Important in genetic recombination, DNA
repair, and replication.
As a signature pattern specific for the bacterial and chloroplastic recA
protein, we selected the best conserved region, a nonapeptide located in the
middle of the sequence and which is part of the monomer-monomer interface in a
We also developed two profiles. The first one covers the ATP binding domain
in the N-terminal part of the recA protein. The second one span the whole
monomer-monomer interface. These two profiles also pick up the recA-like
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