Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4. a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Composed of two subunits. One is encoded by the phage and the other is encoded by the host thioredoxin. Interacts with DNA primase/helicase; this interaction is essential for the coordination of DNA unwinding and nucleotide polymerization on duplex DNA. Interacts with the ssDNA-binding protein. Part of the replicase complex that includes the DNA polymerase, thioredoxin, the primase/helicase and the single-stranded DNA binding protein. Belongs to the DNA polymerase type-A family.