MOBIDB in 2025: integrating ensemble properties and function annotations for intrinsically disordered proteins

Damiano Piovesan(University of Padua), Alessio Del Conte(University of Padua), Mahta Mehdiabadi(University of Padua), Maria Cristina Aspromonte(University of Padua), Matthias Blum(European Bioinformatics Institute), Giulio Tesei(University of Copenhagen), Sören von Bülow(University of Copenhagen), Kresten Lindorff‐Larsen(University of Copenhagen), Silvio C. E. Tosatto(University of Padua)
Nucleic Acids Research
October 29, 2024
Cited by 71Open Access
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Abstract

The MobiDB database (URL: https://mobidb.org/) aims to provide structural and functional information about intrinsic protein disorder, aggregating annotations from the literature, experimental data, and predictions for all known protein sequences. Here, we describe the improvements made to our resource to capture more information, simplify access to the aggregated data, and increase documentation of all MobiDB features. Compared to the previous release, all underlying pipeline modules were updated. The prediction module is ten times faster and can detect if a predicted disordered region is structurally extended or compact. The PDB component is now able to process large cryo-EM structures extending the number of processed entries. The entry page has been restyled to highlight functional aspects of disorder and all graphical modules have been completely reimplemented for better flexibility and faster rendering. The server has been improved to optimise bulk downloads. Annotation provenance has been standardised by adopting ECO terms. Finally, we propagated disorder function (IDPO and GO terms) from the DisProt database exploiting sequence similarity and protein embeddings. These improvements, along with the addition of comprehensive training material, offer a more intuitive interface and novel functional knowledge about intrinsic disorder.


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