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.
MeSH Terms
Amino Acid Sequence
Base Sequence
DNA Modification Methylases/genetics
DNA Nucleotidyltransferases/genetics
Integrases
Mathematics
Models, Theoretical
Molecular Sequence Data
Probability
Proteins/genetics
RNA-Directed DNA Polymerase/genetics
Sequence Homology, Nucleic Acid
Software
Chemicals
Proteins
DNA Modification Methylases
DNA Nucleotidyltransferases
Integrases
RNA-Directed DNA Polymerase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Smith H O
Department of Molecular Biology and Genetics, School of Medicine, Johns Hopkins University, Baltimore, MD 21205.
Annau T M
Chandrasegaran S
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