ArticleJournal of molecular biology2021
A Fifth of the Protein World: Rossmann-like Proteins as an Evolutionarily Successful Structural unit.
Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
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- Predicting the metalloproteome of Deinococcus indicus DR1 through integrative structure and function annotation.Biodegradation · 2026Article
- Ngt-1: A glycosyltransferase that confers resistance to three distinct antibiotic classes.The Journal of biological chemistry · 2026Article
- Structural insights into urocanate reductase using room-temperature X-ray crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- Family-level specialization in protein domain insertion architectures.Protein science : a publication of the Protein Society · 2026Article
- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
- RNA-binding activity of PHGDH drives amyloid-beta production in a human brain organoid model of sporadic Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Versatile NTP recognition and domain fusions expand the functional repertoire of the ParB-CTPase fold beyond chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Investigation of a cryptic ligand binding site on Plasmodium falciparum Hsp90.Bioorganic & medicinal chemistry · 2025Article
- DrugDomain 2.0: comprehensive database of protein domains-ligands/drugs interactions across the whole Protein Data Bank.bioRxiv : the preprint server for biology · 2025Article
- In silico approach on structural and functional characterization of heat shock protein from Sulfobacillus acidophilus.Journal of applied genetics · 2025Article
- An Evolutionary Study in Glyphosate Oxidoreductase Gox Highlights Distinct Orthologous Groups and Novel Conserved Motifs That Can Classify Gox and Elucidate Its Biological Role.Journal of xenobiotics · 2025Article
- Piecing Together the History of Protein Folds From a Fragmented Evolutionary Record.Genome biology and evolution · 2025Article
- Leveraging AI to explore structural contexts of post-translational modifications in drug binding.Journal of cheminformatics · 2025Article
- Article
- Tubulin Polymerization Promoting Proteins: Functional Diversity With Implications in Neurological Disorders.Journal of neuroscience research · 2025Review
- Leveraging AI to Explore Structural Contexts of Post-Translational Modifications in Drug Binding.bioRxiv : the preprint server for biology · 2025Article
- Refinement and curation of homologous groups facilitated by structure prediction.Protein science : a publication of the Protein Society · 2025Article
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5 authors.
Funding
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.
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