| Description | This entry represents a domain found at the C-terminal of DNA primase from Acidithiobacillus ferrooxidans (RepB), Mobilization protein A from Escherichia coli (MobA) and similar sequences mainly found in proteobacteria. This domain adopts a helical configuration [ ].RepB is a DNA-primase produced by P4-like phages. It is a zinc-independent primase unlike Pri-type primases. It takes up a dumbbell shaped consisting of an N-terminal catalytic domain separated by a long α-helix plus tether and a C-terminal helical-bundle domain. Primases are necessary for phage replication. RepBprime primases recognise both ssiA and ssiB, ie only 1 single-stranded primase initiation site on each strand, independently of each other and then synthesise primers that are elongated by DNA polymerase III. The phage is thus replicated exclusively in leading strand mode [].MobA is part of the relaxosome complex that is responsible for plasmid transfer during conjugation. It unwinds DNA and catalyses the cleavage of one of the DNA strands at oriT. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. The primase activity of MobA is essential for the synthesis of primers that will initiate the DNA replication events necessary to form the double-stranded plasmid in the recipient cell [ , ]. | Name | RepB/MobA-like, C-terminal domain |
| Short Name | RepB/MobA-like_C | Type | Domain |
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