Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA. Homooligomers. Forms double-helical filaments necessary for the formation of replication compartments within the host nucleus. Interacts with the origin-binding protein. Interacts with the helicase primase complex; this interaction stimulates primer synthesis activity of the helicase-primase complex. Interacts with the DNA polymerase. Interacts with the alkaline exonuclease; this interaction increases its nuclease processivity. In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments). Belongs to the herpesviridae major DNA-binding protein family.