Abstract
The bacteriophage SPO1 DNA polymerase-encoding gene, which contains a self-splicing intron, has been sequenced and its amino acid (aa) sequence has been deduced. The aa sequence of SPO1 DNA polymerase shows a high degree of similarity with that of DNA polymerase I from Escherichia coli (PolI). Alignment with the sequences of Poll, and the φ29 and SPO1 DNA polymerases indicate that the aa residues that have been implicated in 3'→5' exonuclease activities are conserved.
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