v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | The DNA terminal protein Gp3, found in a number of Bacillus phages, is linked to the 5' ends of both strands of the genome through a phosphodiester bond between the β-hydroxyl group of a serine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in the priming of DNA elongation [ ].This superfamily entry represents the C-terminal priming domain of the DNA terminal protein GP3 sequences from Phi-29 like bacteriophages. In the transition from the initiation to the elongation phases, the priming domain of terminal protein moves out of the active site as polymerase elongates the primer strand. The terminal protein dissociates from the polymerase after the incorporation of approximately six nucleotides [ ].This domain is a four-helix bundle with a left turning up-down-up-down topology. Serine-232, which provides the priming hydroxyl group for DNA synthesis, lies in a loop at the end of the domain closest to the active site of the DNA polymerase [ ]. |
| Short Name | DNA_terminal_Gp3_C |