| Primary Identifier | IPR043031 | Type | Homologous_superfamily |
| Short Name | Viral_ssDBP_head |
| description | This entry includes the major DNA-binding protein (DBP, UL57 or ICP8) from Herpesviruses. DBP binds single-stranded DNA, and the region encompassing residues 368-902 contains the DNA-binding site []. UL5, UL8 and UL52 genes encode an essential heterotrimeric DNA helicase-primase that is responsible for concomitant DNA unwinding and primer synthesis at the viral DNA replication fork. DBP may stimulate DNA unwinding and enable bypass of cisplatin damaged DNA by recruiting the helicase-primase to the DNA []. DBP helps initiate DNA replication by binding to the origin-binding protein (UL9) []. It also reorganizes the host nucleus leading to the formation of prereplicative sites and replication compartments [].This superfamily represents the head domain found in Viral ssDNA-binding protein. The head domain interacts with the C-terminal domain (CTD) of the protein and gives the CTD structure. The CTD is involved in increasing the ssDNA binding protein's cooperativity when binding ICP8, which is believed to stimulate helicase activity. Structurally, this domain consists of 8 alpha helices []. |
