Bioinformatics Advance Access originally published online on December 14, 2004
Bioinformatics 2005 21(8):1437-1442; doi:10.1093/bioinformatics/bti218
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
DbW: automatic update of a functional family-specific multiple alignment
Laboratoire de Biologie et Génomique Structurales, Institut de Génétique et de Biologie Moléculaire et Cellulaire, (CNRS/INSERM/ULP) BP 10142, 67404 Illkirch Cedex, France
*To whom correspondence should be addressed.
Motivation: Recent advances in gene sequencing have provided complete sequence information for a number of genomes and as a result the amount of data in the sequence databases is growing at an exponential rate. We introduce here a new program, DbW, to automate the update of a functional family-specific multiple alignment that tries to include relevant sequences. The program is based on the use of different sources of information: sequences and annotations in databases.
Results: The advantages of DbW are demonstrated using the 20 families of aminoacyl-tRNA synthetases, where DbW detects a maximum of homologous sequences in the Swiss-Prot and SPTREMBL databases. The global specificity of DbW in this test is 98.4% (1.6% of the sequences included in the alignment did not belong to the family according to their function), and the global sensitivity of DbW is estimated to be 95.2%. Thus, DbW provides a reliable basis for the many applications that rely on accurate multiple alignments, e.g. functional residue identification, 2D/3D structure prediction or homology modeling.
Availability: The DbW software is available for download at ftp://ftp-igbmc.u-strasbg.fr/pub/DbW/DbW.tar and online at http://titus.u-strasbg.fr/DbW
Contact: prigent{at}igbmc.u-strasbg.fr
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
A. Sheoran and E. A. First Activation of D-Tyrosine by Bacillus stearothermophilus Tyrosyl-tRNA Synthetase: 2. COOPERATIVE BINDING OF ATP IS LIMITED TO THE INITIAL TURNOVER OF THE ENZYME J. Biol. Chem., May 9, 2008; 283(19): 12971 - 12980. [Abstract] [Full Text] [PDF] |
||||
