Description

IPR014492 is a Poly(A) polymerase.

<p>Members of this group are poly(A) polymerases (polynucleotide adenylyltransferases, PAP, [ec:2.7.7.19]). In eukaryotes, polyadenylation of pre-mRNA plays an essential role in the initiation step of protein synthesis, as well as in the export and stability of mRNAs. Poly(A) polymerase, the central enzyme of the polyadenylation machinery, is a template-independent RNA polymerase that specifically incorporates ATP at the 3' end of mRNA [[cite:PUB00008708], [cite:PUB00016879]].</p> <p>The catalytic domain of poly(A) polymerase shares substantial structural homology with other nucleotidyl transferases such as DNA polymerase beta and kanamycin transferase [[cite:PUB00008708]]. The three invariant aspartates of the catalytic triad ligate two of the three active site metals. One of these metals also contacts the adenine ring. Other conserved, catalytically important residues contact the nucleotide. These contacts, taken together with metal coordination of the adenine base, provide a structural basis for ATP selection by poly(A) polymerase [[cite:PUB00008708]].</p> <p>The central domain of poly(A) polymerase shares structural similarity with the allosteric activity domain of ribonucleotide reductase R1, which comprises a four-helix bundle and a three-stranded mixed β-sheet. Even though the two enzymes bind ATP, the ATP-recognition motifs are different [[cite:PUB00008708]]. The C-terminal domain is predicted to be an RNA-binding domain because it folds into a compact domain reminiscent of the RNA-recognition motif fold [[cite:PUB00008708]].</p> <p>The C-terminal region beyond the predicted RNA-binding domain is only conserved in vertebrates and is dispensable for catalytic activity<i>in vitro</i>. The extended C-terminal domain of vertebrate PAPs is rich in serines and threonines, and enzyme activity can be down regulated by phosphorylation at multiple sites [[cite:PUB00016763], [cite:PUB00008708]]. The extreme C terminus of PAP is also the target for another type of regulation. The U1A protein, a component of the U1 snRNP which functions in 5 splice site recognition, is known to inhibit polyadenylation of its own mRNA by binding to PAP [[cite:PUB00016888]]. The C terminus of PAP is also involved in protein-protein interactions with the splicing factor U2AF65 [[cite:PUB00016888]] and the snRNP protein U1-70K [[cite:PUB00016881]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 15

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: