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The nucleotidyl-transferase domain is a conserved catalytic domain present in a large enzyme superfamily involved in nucleotide group transfers. Enzymes harboring this domain include DNA and RNA polymerases, poly(A) polymerases, and enzymes conferring antibiotic resistance, among others. The domain features a signature α/β fold and conserved carboxylate residues crucial for catalysis and divalent ion coordination. NTase domain-containing proteins are essential in processes such as nucleic acid metabolism, signal transduction, chromatin remodeling, immunological diversity (V(D)J recombination), and stress/defense responses. The NTase fold superfamily encompasses nearly 43 human genes, with roles in health and disease ranging from immunity to neurodevelopment and cancer. Targeting specific enzymes with NTase domains is an important therapeutic strategy in antiviral, antibacterial, and chemotherapeutic contexts[1][2][3][5][6].
Inhibition of nucleotidyl-transferase catalytic activity (e.g., DNA/RNA polymerase inhibitors, OAS inhibitors) Modulation of nucleotide transfer to disrupt genetic replication, repair, or editing Blockade of antibiotic resistance enzyme function
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