Domain shuffling creates new protein architectures by combining domains in new arrangements during evolution. A binding domain joined to a catalytic domain can bring an existing chemistry to a new substrate or location. The domains need not retain identical behaviour after recombination because interfaces, linkers and regulation can change. Comparing domain arrangements therefore complements whole-sequence similarity when reconstructing functional evolution. [ref]
Exploring structural diversity across the protein universe with The Encyclopedia of Domains by Andy M. Lau and others. 2024, domain structures and multidomain architectures
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