CMAdb

CMAdb is the first dedicated database that systematically catalogs experimentally-validated CMA substrates, their predicted domain information, mapping their ‘CMA-targeting’ motifs and calculating their solvent accessibility, structural alignments, and reliability scores. Our database serves as a foundational resource for researchers investigating the mechanistic underpinnings of CMA and its implications in health and disease.

To support broader exploration, we developed an interactive web server that enables users to query proteins, retrieve all available PDB entries, identify homologous structures, perform structural superimposition with RMSD calculation, and highlight unresolved regions. For CMA substrates specifically, the server displays canonical and potential motif positions, and their solvent accessibility—providing a valuable platform for motif prediction and insights into CMA-mediated degradation.

Resolved in Same Protein: N/A
Resolved in homologous Protein: N/A
New Prediction: N/A
Experimentally Resolved Percentage: N/A
Legend
AlphaFold Predicted Region Experimentally Resolved Region Same-protein structural representation (%) Homolog-derived structural representation (%)
Graph Legend:
Original Protein Same Protein Homolog-derived Protein
AlphaFold pLDDT Score
50 60 70 80 90 100
Grey-colored regions represent sequence segments with available structural evidence, derived either from experimentally resolved structures of the query protein or from aligned experimentally resolved structures of homologous proteins. Regions without such structural evidence are colored according to the corresponding AlphaFold2 per-residue confidence (pLDDT) scores. Canonical KFERQ-type motifs are shown as ball-and-stick models. Colors indicate the sequential order of motif occurrences within each protein, with the same color scheme applied consistently across all proteins