v5.1.0.3
Cicer data from the Legume Information System
Type | Domain |
Description | This domain is found in phage proteins, such as from Acinetobacter phage SH-Ab 15497 and from cyanophage S-2L, which are associated with PurZ, an enzyme that catalyses the synthesis of diaminopurine (Z), a DNA modification that gives phages an advantage for evading host restriction enzymes activity [ ]. This domain has dATP and/or dGTP pyrophosphohydrolase activity; it catalyses the hydrolysis of dATP/dGTP to pyrophosphate and dAMP/dGMP, respectively, with little or no activities for NTPs and pyrimidine dNTPs. In SH-Ab 15497, it has both a dATPase and a dGTPase activities, while in S-2L it is only a dGTPase, suggesting some flexibility in the strategy of these phages to incorporate Z instead of A in their genome []. Enzymes containing this domain supply dGMP as the substrate for PurZ, elevating dZTP level to promote Z incorporation [, ]. |
Short Name | dATP/dGTP_dipphydrolase_MazZ |