Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). Required for viral RNA replication (By similarity). Does not have any proteolytic activity (By similarity). Affects membrane integrity and causes an increase in membrane permeability. Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of rearranged membranous structures where viral replication takes place (By similarity). Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity). Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity). Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) ATP + H2O = ADP + H(+) + phosphate Interacts with capsid protein VP1 (By similarity). Interacts with capsid protein VP3 (By similarity). Interacts with capsid protein VP0 (By similarity). Interacts with capsid protein VP3 (By similarity). Interacts with capsid protein VP0 (By similarity). Interacts with capsid protein VP1 (By similarity). Homodimer (By similarity). Interacts with protein 2B (By similarity). Interacts with protein 2C (By similarity). Homodimer. Interacts with host ABCD3 (By similarity). Interacts with protein 2A (By similarity). Interacts with host ACBD3 (By similarity). Homodimer. Interacts with host ABCD3 (By similarity). Interacts with protein 2A (By similarity). Interacts with protein 3A (By similarity). Interacts with protein 3C (By similarity). Interacts with host ACBD3 (By similarity). Homodimer (By similarity). Interacts with host ABCD3 (via GOLD domain) and PI4KB; these interactions allow the formation of a viral protein/ACBD3/PI4KB complex in order to synthesize PI4P at the viral RNA replication sites (By similarity). Interacts with protein 2C (By similarity). Interacts with protein 3C (By similarity). Protein 3C: Interacts with protein 2A (By similarity). Protein 3C: Interacts with protein 2C (By similarity). Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The leader protein-VP0 junction is cleaved by 3C proteinase (By similarity). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (By similarity). Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase.