Abstract
AbstractThe structure of many proteins consists of a combination of discrete modules that have been shuffled during evolution. Such modules can frequently be recognized from the analysis of homology. Here we present a systematic analysis of the modular organization of all sequenced proteins. To achieve this we have developed an automatic method to identify protein domains from sequence comparisons. Homologous domains can then be clustered into consistent families. The method was applied to all 21,098 nonfragment protein sequences in SWISS‐PROT 21.0, which was automatically reorganized into a comprehensive protein domain database, ProDom. We have constructed multiple sequence alignments for each domain family in ProDom, from which consensus sequences were generated. These nonredundant domain consensuses are useful for fast homology searches. Domain organization in ProDom is exemplified for proteins of the phosphoenolpyruvate: sugar phosphotransferase system (PEP:PTS) and for bacterial 2‐component regulators. We provide 2 examples of previously unrecognized domain arrangements discovered with the help of, ProDom.
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Dates
Type | When |
---|---|
Created | 15 years, 1 month ago (July 12, 2010, 1:35 a.m.) |
Deposited | 1 year, 10 months ago (Oct. 24, 2023, 8:04 a.m.) |
Indexed | 1 month, 4 weeks ago (July 7, 2025, 8:04 a.m.) |
Issued | 31 years, 6 months ago (March 1, 1994) |
Published | 31 years, 6 months ago (March 1, 1994) |
Published Online | 16 years, 8 months ago (Dec. 31, 2008) |
Published Print | 31 years, 6 months ago (March 1, 1994) |
@article{Sonnhammer_1994, title={Modular arrangement of proteins as inferred from analysis of homology}, volume={3}, ISSN={1469-896X}, url={http://dx.doi.org/10.1002/pro.5560030314}, DOI={10.1002/pro.5560030314}, number={3}, journal={Protein Science}, publisher={Wiley}, author={Sonnhammer, Erik L.L. and Kahn, Daniel}, year={1994}, month=mar, pages={482–492} }