DNA-directed DNA polymerase, family B, conserved site <p>DNA is the biological information that instructs cells how to exist in anordered fashion: accurate replication is thus one of the most importantevents in the life cycle of a cell. This function is performed by DNA-directed DNA-polymerases (<db_xref db="EC" dbkey="2.7.7.7"/>) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA, using a complementary DNA chain as a template. Small RNA molecules are generally used as primers for chain elongation, although terminal proteins may also be used for the <i>de novo</i> synthesis of a DNA chain. Even though there are 2 different methods of priming, these are mediated by 2 very similar polymerases classes, A and B, with similar methods of chain elongation. </p><p> A number of DNA polymerases have been groupedunder the designation of DNA polymerase family B.Six regions of similarity (numbered from I to VI) are found in all or a subsetof the B family polymerases. The most conserved region (I) includes a conservedtetrapeptide with two aspartate residues. Its function is not yet known.However, it has been suggested [<cite idref="PUB00004353"/>] that it may be involved in binding amagnesium ion. All sequences in the Bfamily contain a characteristic DTDS motif, and possess many functionaldomains, including a 5'-3' elongation domain, a 3'-5' exonuclease domain [<cite idref="PUB00000436"/>],a DNA binding domain, and binding domains for both dNTP's and pyrophosphate [<cite idref="PUB00010600"/>].</p>