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http://purl.uniprot.org/unirules/MF_03181#construct-template-56http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_03181#construct-var-5
http://purl.uniprot.org/unirules/MF_03181#construct-template-56http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_03181#construct-template-56http://spinrdf.org/sp#object"Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs."xsd:string
http://purl.uniprot.org/unirules/MF_03181#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_03181#construct-template-56
http://purl.uniprot.org/unirules/MF_03181#construct-template-list-56http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_03181#construct-template-56