Concomitant prediction of function and fold at the domain level with GO-based profiles

BMC Bioinformatics. 2013;14 Suppl 3(Suppl 3):S12. doi: 10.1186/1471-2105-14-S3-S12. Epub 2013 Feb 28.


Predicting the function of newly sequenced proteins is crucial due to the pace at which these raw sequences are being obtained. Almost all resources for predicting protein function assign functional terms to whole chains, and do not distinguish which particular domain is responsible for the allocated function. This is not a limitation of the methodologies themselves but it is due to the fact that in the databases of functional annotations these methods use for transferring functional terms to new proteins, these annotations are done on a whole-chain basis. Nevertheless, domains are the basic evolutionary and often functional units of proteins. In many cases, the domains of a protein chain have distinct molecular functions, independent from each other. For that reason resources with functional annotations at the domain level, as well as methodologies for predicting function for individual domains adapted to these resources are required.We present a methodology for predicting the molecular function of individual domains, based on a previously developed database of functional annotations at the domain level. The approach, which we show outperforms a standard method based on sequence searches in assigning function, concomitantly predicts the structural fold of the domains and can give hints on the functionally important residues associated to the predicted function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology / methods
  • Molecular Sequence Annotation*
  • Position-Specific Scoring Matrices
  • Protein Folding
  • Protein Structure, Tertiary*
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / physiology
  • Sequence Analysis, Protein
  • Vocabulary, Controlled


  • Proteins