Genomic sequences homologous to the protein kinase region of the bifunctional herpes simplex virus type 2 protein ICP10.

The large subunit of herpes simplex virus type 2 (HSV-2) ribonucleotide reductase (ICP10) consists of two functional domains. The amino (N)-terminal domain at residues 1-411 has serine/threonine-specific kinase activity (PK domain) and is encoded by a DNA fragment with transforming potential (15,17). The remaining region is required for ribonucleotide reductase activity (RR domain) (14, 15). Computer-assisted comparison of the ICP10 sequence to the EMBL database 21 has revealed sequences within the RR domain that are common to all RR1 proteins. Motifs homologous to the catalytic domains of all PKs were identified in the PK region (15). However, based on this database all other sequences were unique. Secondary structure analysis of the PK and RR junction region of ICP10 identified twist angle variations with helical periodicity characteristic of enhancer elements. Sequences homologous to a segment of the PK domain were amplified and cloned from human DNA using the polymerase chain reaction (PCR), suggesting that the PK domain may have originated from a cellular gene.