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Bioinformatics Advance Access originally published online on July 29, 2004
Bioinformatics 2004 20(18):3481-3489; doi:10.1093/bioinformatics/bth432
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Bioinformatics vol. 20 issue 18 © Oxford University Press 2004; all rights reserved.

DIVAA: analysis of amino acid diversity in multiple aligned protein sequences

Diane J. Rodi , Suneeta Mandava and Lee Makowski *

Combinatorial Biology Unit, Biosciences Division, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA

Received on February 26, 2004; revised on July 2, 2004; accepted on July 16, 2004
Advance Access Publication July 29, 2004

Motivation: Multiple alignments of proteins are an effective way of identifying conserved amino acids that provide clues to functional relationships among proteins. Quantitation of the abundances of amino acids found at each position in a sequence motif can provide a basis for understanding the structural and functional constraints at each point. Distribution of information across a motif has been used previously, but the non-intuitive nature of the analysis has limited its impact.

Results: Here, we introduce a quantitative measure of amino acid sequence diversity (DIVAA) that has a simple, intuitive meaning. Diversity, as a measure of sequence conservation or variation, is inextricably linked to the probability of selecting identical pairs from a distribution. We demonstrate its utility through the analysis of four populations: ATP-binding P-loops, hypervariable domains of kappa light chains, signal sequences, and the N- and C- termini of proteins. DIVAA provides a simple means to generate hypotheses concerning the contribution of individual residues to the functional and evolutionary relationships among proteins.

Availability: Access to DIVAA software is available at RELIC (http://relic.bio.anl.gov)

Contact: lmakowski{at}anl.gov

* To whom correspondence should be addressed.


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