The Study\nof Metalloproteome of DNA Viruses: Identification,\nFunctional Annotation, and Diversity Analysis of Viral Metal-Binding\nProteins

Metalloproteins are fundamental to diverse biological\nprocesses\nbut still lack extensive investigation in viral contexts. This study\nreveals the prevalence and functional diversity of metal-binding proteins\nin DNA viruses. Among a subset of 1432 metalloproteins, zinc and magnesium-binding\nproteins are notably abundant, indicating their importance in viral\nbiology. Furthermore, significant numbers of proteins binding to iron,\nmanganese, copper, nickel, mercury, and cadmium were also detected.\nHuman-infecting viral proteins displayed a rich landscape of metalloproteins,\nwith MeBiPred (964 proteins) and Pfam (666) yielding the highest numbers.\nInterestingly, many essential viral proteins exhibited metal-binding\ncapabilities, including polymerases, DNA binding proteins, helicases,\ndUPTase, thymidine kinase, and various structural and accessory proteins.\nThis study sheds light on the ubiquitous presence of metalloproteins,\ntheir functional signatures, subcellular placements, and metal-utilization\npatterns, providing valuable insights into viral biology. A similar\nmetal utilization pattern was observed in similar functional proteins\nacross the various DNA viruses. Furthermore, these findings provide\na foundation for identifying potential drug targets for combating\nviral infections.