The maturational protease (PR) processes both pPR-AP and pPR in a pathway that releases PR, pAP, and AP. Although pAP is sufficient for procapsid assembly, self-cleavage of pPR-AP to PR and release of a number of pAP and pPR-AP products are required for proper DNA encapsidation and production of nucleocapsids. Precise protease cleavage steps lead to the release of major capsid protein (MCP), inactivation of the protease, and orchestration of the replacement of the scaffold in procapsids with viral DNA. PR and AP, as well as pAP forms, are completely removed from nucleocapsids into which DNA has been packaged.