Authors
Xiaoyue Cui, Yuting Xiao, Maureen Stolzer, Dannie Durand
Published in
Bioinformatics advances. Volume 6. Issue 1. Pages vbag037. Epub Mar 02, 2026.
Abstract
Multidomain proteins are mosaics of domains, protein modules that are associated with a specific structure or function and are found in diverse combinations. This modular organization facilitates the evolution of novel protein functions, but the principles that govern the relationship between the domain content of a protein and its function is poorly understood. In particular, do domains always contribute the same function, or does the functional contribution of a domain depend on the neighboring domains in the protein? To answer this question, we used vector embeddings, which account for local contextual signals, to model the protein domain content of multidomain proteins. We observe that multidomain architectures that are semantically similar share more functional attributes than multidomain architectures selected based on domain content similarity, alone, suggesting that context is important for understanding the relationship between domain content and protein function. Surprisingly, vector semantics also identified multidomain architecture pairs with significantly high functional similarity, despite having no domains in common at all, suggesting that vector semantics may be discovering domain "synonyms". Taken together, our results underscore the importance of contextual models for understanding the interplay between domain architecture evolution and functional innovation in multidomain proteins.
The data and code used in this work are available at https://zenodo.org/records/15769961.
PMID:
41938593
Bibliographic data and abstract were imported from PubMed on 12 Sep 2026.
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