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Finding Sequence Motifs in Groups of Functionally Related Proteins
Hamilton O. Smith, Thomas M. Annau and Srinivasan Chandrasegaran
Proceedings of the National Academy of Sciences of the United States of America
Vol. 87, No. 2 (Jan., 1990), pp. 826-830
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2353604
Page Count: 5
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1990 National Academy of Sciences