Matrix protein. Nucleocapsid protein p14: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. Capsid protein. NC-dUTPase has dUTPase activity, thereby preventing incorporation of uracil into DNA. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. dUTP + H2O = diphosphate + dUMP + H(+) Magnesium ions are required for NC-dUTPase activity. Inhibited by pepstatin A. Homodimer; when myristoylated. Homodimer (By similarity). NC-dUTPase is a homotrimer (PubMed:8091672). Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Gag-p27 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101. Released by autocatalytic processing. Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. Specific enzymatic cleavages in vivo yield mature proteins. Produced by -1 ribosomal frameshifting between gag-pro.