Skip Navigation

This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow FREE Full Text (Screen PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Corpet, F.
Right arrow Articles by Kahn, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Corpet, F.
Right arrow Articles by Kahn, D.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics Vol. 15 no. 12 1999
Pages 1020-1027
© 1999 Oxford University Press

Browsing protein families via the ‘Rich Family Description’ format

Florence Corpet 1, Jérôme Gouzy 2 and Daniel Kahn 2

1 Laboratoire de Génétique Cellulaire, Centre INRA de Toulouse, B.P. 27, 31326 Castanet Cedex, France
2 Laboratoire de Biologie Moléculaire des Relations Plantes-Microorganismes, I.N.R.A./C.N.R.S., B.P. 27, 31326 Castanet Cedex, France

Motivation: Multiple alignments of protein sequences are the basis of structural and functional analysis of protein families. It is however difficult even for an expert biologist to comprehend an alignment of more than 50 to 100 homologous sequences.

Results: This paper presents a browser for the analysis of multiple alignments of large numbers of protein sequences. Phylogenetic trees and consensus sequences are computed and used to summarise the alignments; these data are stored in a structure called Rich Family Description. Summary alignments and trees are displayed in HTML pages and can be developed or reduced by the user. This browser is used to display the ProDom domain families on the Web. Its zooming facilities allow extracting information from alignments of more than 1000 homologous sequences.

Availability: Programs are available free of charge on request from the authors. The ProDom database can be consulted at http://www.toulouse.inra.fr/prodom.html

Contact: fcorpet{at}toulouse.inra.fr

Received on April 30, 1999 ; revised on July 2, 1999 ; accepted on July 14, 1999

Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
T. Hotelier, L. Renault, X. Cousin, V. Negre, P. Marchot, and A. Chatonnet
ESTHER, the database of the {alpha}/{beta}-hydrolase fold superfamily of proteins
Nucleic Acids Res., January 1, 2004; 32(90001): D145 - 147.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
N. J. Mulder, R. Apweiler, T. K. Attwood, A. Bairoch, D. Barrell, A. Bateman, D. Binns, M. Biswas, P. Bradley, P. Bork, et al.
The InterPro Database, 2003 brings increased coverage and new features
Nucleic Acids Res., January 1, 2003; 31(1): 315 - 318.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
F. Chetouani, P. Glaser, and F. Kunst
FindTarget: software for subtractive genome analysis
Microbiology, October 1, 2001; 147(10): 2643 - 2649.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
N. Wicker, G. Rene Perrin, J. C. Thierry, and O. Poch
Secator: A Program for Inferring Protein Subfamilies from Phylogenetic Trees
Mol. Biol. Evol., August 1, 2001; 18(8): 1435 - 1441.
[Abstract] [Full Text] [PDF]


Home page
Protein Eng Des SelHome page
A. C. W. May
Optimal classification of protein sequences and selection of representative sets from multiple alignments: application to homologous families and lessons for structural genomics
Protein Eng. Des. Sel., April 1, 2001; 14(4): 209 - 217.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.