Abstract

We have developed a method for rapidly finding patterns of conserved amino acid residues (motifs) in groups of functionally related proteins. All 3-amino acid patterns in a group of proteins of the type aa1 d1 aa2 d2 aa3, where d1 and d2 are distances that can be varied in a range up to 24 residues, are accumulated into an array. Segments of the proteins containing those patterns that occur most frequently are aligned on each other by a scoring method that obtains an average relatedness value for all the amino acids in each column of the aligned sequence block based on the Dayhoff relatedness odds matrix. The automated method successfully finds and displays nearly all of the sequence motifs that have been previously reported to occur in 33 reverse transcriptases, 18 DNA integrases, and 30 DNA methyltransferases.

Keywords

IntegrasesBiologyGeneticsAmino acidSequence motifPeptide sequenceDNASequence (biology)Computational biologySequence alignmentBase sequenceGene

Affiliated Institutions

Related Publications

Publication Info

Year
1990
Type
article
Volume
87
Issue
2
Pages
826-830
Citations
206
Access
Closed

External Links

View on DOI.org

Social Impact

Altmetric
PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

206
OpenAlex

Cite This

Hamilton O. Smith, T M Annau, Srinivasan Chandrasegaran (1990). Finding sequence motifs in groups of functionally related proteins.. Proceedings of the National Academy of Sciences , 87 (2) , 826-830. https://doi.org/10.1073/pnas.87.2.826

Identifiers

DOI
10.1073/pnas.87.2.826