ProtIdent: a web server for identifying proteases and their types by fusing functional domain and sequential evolution information

Biochem Biophys Res Commun. 2008 Nov 14;376(2):321-5. doi: 10.1016/j.bbrc.2008.08.125. Epub 2008 Sep 5.

Abstract

Proteases are vitally important to life cycles and have become a main target in drug development. According to their action mechanisms, proteases are classified into six types: (1) aspartic, (2) cysteine, (3) glutamic, (4) metallo, (5) serine, and (6) threonine. Given the sequence of an uncharacterized protein, can we identify whether it is a protease or non-protease? If it is, what type does it belong to? To address these problems, a 2-layer predictor, called "ProtIdent", is developed by fusing the functional domain and sequential evolution information: the first layer is for identifying the query protein as protease or non-protease; if it is a protease, the process will automatically go to the second layer to further identify it among the six types. The overall success rates in both cases by rigorous cross-validation tests were higher than 92%. ProtIdent is freely accessible to the public as a web server at http://www.csbio.sjtu.edu.cn/bioinf/Protease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Computational Biology / methods*
  • Computer Communication Networks*
  • Databases, Protein
  • Evolution, Molecular
  • Humans
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / classification*
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein / methods*
  • Software*

Substances

  • Peptide Hydrolases