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Nucleic Acids Research 2006 34(Database Issue):D257-D260; doi:10.1093/nar/gkj079
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Nucleic Acids Research, 2006, Vol. 34, Database issue D257-D260
© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org


Article

SMART 5: domains in the context of genomes and networks

Ivica Letunic, Richard R. Copley1, Birgit Pils2, Stefan Pinkert2, Jörg Schultz2 and Peer Bork*

EMBL Meyerhofstrasse 1, 69012 Heidelberg, Germany 1Wellcome Trust Centre for Human Genetics Roosevelt Drive, Oxford OX3 7BN, UK 2Bioinformatik, Biozentrum, Am Hubland, University of Wuerzburg 97074 Wuerzburg, Germany

*To whom correspondence should be addressed. Tel: +49 6221 387 8526; Fax: +49 6221 387 517; Email: bork{at}embl.de

Received September 13, 2005. Revised October 11, 2005. Accepted October 11, 2005.

The Simple Modular Architecture Research Tool (SMART) is an online resource (http://smart.embl.de/) used for protein domain identification and the analysis of protein domain architectures. Many new features were implemented to make SMART more accessible to scientists from different fields. The new ‘Genomic’ mode in SMART makes it easy to analyze domain architectures in completely sequenced genomes. Domain annotation has been updated with a detailed taxonomic breakdown and a prediction of the catalytic activity for 50 SMART domains is now available, based on the presence of essential amino acids. Furthermore, intrinsically disordered protein regions can be identified and displayed. The network context is now displayed in the results page for more than 350 000 proteins, enabling easy analyses of domain interactions.


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