Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 60,161 bioRxiv papers from 267,433 authors.
Understanding the relationship between amino acid sequence and protein function is a long-standing problem in molecular biology with far-reaching scientific implications. Despite six decades of progress, state-of-the-art techniques cannot annotate 1/3 of microbial protein sequences, hampering our ability to exploit sequences collected from diverse organisms. In this paper, we explore an alternative methodology based on deep learning that learns the relationship between unaligned amino acid sequences and their functional annotations across all 17929 families of the Pfam database. Using the Pfam seed sequences we establish rigorous benchmark assessments that use both random and clustered data splits to control for potentially confounding sequence similarities between train and test sequences. Using Pfam full, we report convolutional networks that are significantly more accurate and computationally efficient than BLASTp, while learning sequence features such as structural disorder and transmembrane helices. Our model co-locates sequences from unseen families in embedding space, allowing sequences from novel families to be accurately annotated. These results suggest deep learning models will be a core component of future protein function prediction tools.
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