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Based on its similarity structurally to the RNA recognition motif this domain is thought to be RNA binding .
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 enzyme at the heart of the polyadenylation machinery, is a template-independent RNA polymerase that specifically incorporates ATP at the 3' end of mRNA. The crystal structure of bovine poly(A) polymerase bound to an ATP analogue at 2.5 A resolution has been determined [PUBMED:10944102]. The structure revealed expected and unexpected similarities to other proteins. As expected, the catalytic domain of poly(A) polymerase shares substantial structural homology with other nucleotidyl transferases such as DNA polymerase beta and kanamycin transferase.
Martin G, Keller W, Doublie S; , EMBO J 2000;19:4193-4203.: Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. PUBMED:10944102 EPMC:10944102.