Modeling the evolution of protein domain architectures using maximum parsimony.
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ABSTRACT: Domains are basic evolutionary units of proteins and most proteins have more than one domain. Advances in domain modeling and collection are making it possible to annotate a large fraction of known protein sequences by a linear ordering of their domains, yielding their architecture. Protein domain architectures link evolutionarily related proteins and underscore their shared functions. Here, we attempt to better understand this association by identifying the evolutionary pathways by which extant architectures may have evolved. We propose a model of evolution in which architectures arise through rearrangements of inferred precursor architectures and acquisition of new domains. These pathways are ranked using a parsimony principle, whereby scenarios requiring the fewest number of independent
SUBMITTER: Fong JH
PROVIDER: S-EPMC1858635 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
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