IPR038419
Poly(A) polymerase, nucleotidyltransferase domain superfamily, Poxvirus
InterPro entry
Short name | PolyA_pol_nucTrfase_sf_Poxvir |
Overlapping entries |
Description
Poly(A) polymerase (
2.7.7.19) catalyses template-independent extension of the 3'-end of a DNA or RNA strand by one nucleotide at a time. The Poxvirus enzyme creates the 3'(poly)A tail of mRNAs, and is a heterodimer of a catalytic and a regulatory subunit. The Poxvirus enzyme creates the 3'(poly)A tail of mRNAs, and is a heterodimer composed of a catalytic (VP55, also known as PAP-L) and a regulatory subunit (VP39). VP55 comprises three domains: the N-terminal or N domain, the central or catalytic domain, and the C-terminal or C domain, all three domains having distinct topologies. The core comprises a mixed nine-stranded twisted β sheet, with the first seven strands being folded from one long (118 residue) polypeptide segment that follows the N domain and the last two strands originating from the extreme C-terminal-most 15 residues of the entire polypeptide chain. Of the four α-helices in the catalytic domain, the two longest (J and L) near the surface pack against one side of the β-sheet in a nearly parallel orientation to the β-strands
[1].
This entry represents the nucleotidyltransferase (central) domain of the catalytic subunit VP55
[1].
References
1.Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity. Moure CM, Bowman BR, Gershon PD, Quiocho FA. Mol. Cell 22, 339-49, (2006). View articlePMID: 16678106
Cross References
ENZYME
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.30.460.60