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PMID: 1689055 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Finding sequence motifs in groups of functionally related proteins.

Smith HO, Annau TM, Chandrasegaran S

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
References (18)
18 references, click to expand
  1. Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains.
    Nature. 1989 Aug 10;340(6233):478-82 PMID: 2502717
  2. Simultaneous comparison of three protein sequences.
    Proc Natl Acad Sci U S A. 1985 May;82(10):3073-7 PMID: 3858804
  3. ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins.
    Proc Natl Acad Sci U S A. 1986 Feb;83(4):907-11 PMID: 2869483
  4. Sequence, internal homology and high-level expression of the gene for a DNA-(cytosine N4)-methyltransferase, M.Pvu II.
    Nucleic Acids Res. 1989 Jun 12;17(11):4161-75 PMID: 2662138
  5. Evolution of type II DNA methyltransferases. A gene duplication model.
    J Mol Biol. 1989 Mar 20;206(2):313-21 PMID: 2541254
  6. Spliced segments at the 5' terminus of adenovirus 2 late mRNA.
    Proc Natl Acad Sci U S A. 1977 Aug;74(8):3171-5 PMID: 269380
  7. A tool for multiple sequence alignment.
    Proc Natl Acad Sci U S A. 1989 Jun;86(12):4412-5 PMID: 2734293
  8. The integrase family of site-specific recombinases: regional similarities and global diversity.
    EMBO J. 1986 Feb;5(2):433-40 PMID: 3011407
  9. Nucleotide sequence of the DdeI restriction-modification system and characterization of the methylase protein.
    Nucleic Acids Res. 1987 Oct 26;15(20):8249-66 PMID: 2823226
  10. Nucleotide sequence and expression of the gene encoding the EcoRII modification enzyme.
    Nucleic Acids Res. 1987 Jan 12;15(1):313-32 PMID: 3029675
  11. Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.
    J Biol Chem. 1985 Mar 25;260(6):3350-4 PMID: 2982857
  12. Rapid and sensitive protein similarity searches.
    Science. 1985 Mar 22;227(4693):1435-41 PMID: 2983426
  13. Evidence for a repeating domain in type I restriction enzymes.
    EMBO J. 1985 May;4(5):1351-5 PMID: 2988943
  14. A thousand and one protein kinases.
    Cell. 1987 Sep 11;50(6):823-9 PMID: 3113737
  15. Origins and evolutionary relationships of retroviruses.
    Q Rev Biol. 1989 Mar;64(1):1-30 PMID: 2469098
  16. Predictive motifs derived from cytosine methyltransferases.
    Nucleic Acids Res. 1989 Apr 11;17(7):2421-35 PMID: 2717398
  17. Cloning, sequencing, in vivo promoter mapping, and expression in Escherichia coli of the gene for the HhaI methyltransferase.
    J Biol Chem. 1987 Apr 5;262(10):4770-7 PMID: 3549710
  18. Why genes in pieces?
    Nature. 1978 Feb 9;271(5645):501 PMID: 622185
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1990-01-00
Pages
826-30
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC53359
Subset
IM
Grants
NIGMS NIH HHS · GM42140 · United States
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