Abstract
The Rossmann-like fold is the most prevalent and diversified doubly-wound superfold of ancient evolutionary origin. Rossmann-like domains are present in a variety of metabolic enzymes and are capable of binding diverse ligands. Discerning evolutionary relationships among these domains is challenging because of their diverse functions and ancient origin. We defined a minimal Rossmann-like structural motif (RLM), identified RLM-containing domains among known 3D structures (20%) and classified them according to their homologous relationships. New classifications were incorporated into our Evolutionary Classification of protein Domains (ECOD) database. We defined 156 homology groups (H-groups), which were further clustered into 123 possible homology groups (X-groups). Our analysis revealed that RLM-containing proteins constitute approximately 15% of the human proteome. We found that disease-causing mutations are more frequent within RLM domains than within non-RLM domains of these proteins, highlighting the importance of RLM-containing proteins for human health.
Original language | English (US) |
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Article number | 166788 |
Journal | Journal of Molecular Biology |
Volume | 433 |
Issue number | 4 |
DOIs | |
State | Published - Feb 19 2021 |
Keywords
- Rossmann-fold
- domains classification
- minimal Rossmann-like motif
- protein evolution
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology