Literature DB >> 9322058

SEALS: a system for easy analysis of lots of sequences.

D R Walker1, E V Koonin.   

Abstract

We present a system of programs designed to facilitate sequence analysis projects involving large amounts of data. SEALS (System for Easy Analysis of Lots of Sequences) is a logically organized set of flexible, easily modifiable research tools, designed to run on open systems. Functionality is divided into approximately 50 commands which follow consistent syntax and semantics; wrappers are also provided for commonly used sequence analysis software to effect similar syntax for these programs. SEALS includes software for retrieving sequence information, scripting database search tools such as BLAST and MoST, viewing and analyzing search outputs, searching in and processing nucleotide and protein sequences using regular expressions, and constructing rational predictions of protein features. The system is designed to provide modular elements which can be combined, modified, and integrated with other methods in order to quickly design and execute computer experiments for sequence analysis projects at the scale of whole genomes.

Mesh:

Year:  1997        PMID: 9322058

Source DB:  PubMed          Journal:  Proc Int Conf Intell Syst Mol Biol        ISSN: 1553-0833


  64 in total

1.  Treble clef finger--a functionally diverse zinc-binding structural motif.

Authors:  N V Grishin
Journal:  Nucleic Acids Res       Date:  2001-04-15       Impact factor: 16.971

2.  Lineage-specific gene expansions in bacterial and archaeal genomes.

Authors:  I K Jordan; K S Makarova; J L Spouge; Y I Wolf; E V Koonin
Journal:  Genome Res       Date:  2001-04       Impact factor: 9.043

3.  Sialidase-like Asp-boxes: sequence-similar structures within different protein folds.

Authors:  R R Copley; R B Russell; C P Ponting
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

4.  The alpha-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family.

Authors:  H Zhang; N V Grishin
Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725

5.  Comparative genome analysis of the pathogenic spirochetes Borrelia burgdorferi and Treponema pallidum.

Authors:  G Subramanian; E V Koonin; L Aravind
Journal:  Infect Immun       Date:  2000-03       Impact factor: 3.441

6.  Common fold in helix-hairpin-helix proteins.

Authors:  X Shao; N V Grishin
Journal:  Nucleic Acids Res       Date:  2000-07-15       Impact factor: 16.971

7.  Systematic identification of novel protein domain families associated with nuclear functions.

Authors:  Tobias Doerks; Richard R Copley; Jörg Schultz; Chris P Ponting; Peer Bork
Journal:  Genome Res       Date:  2002-01       Impact factor: 9.043

8.  Essential genes are more evolutionarily conserved than are nonessential genes in bacteria.

Authors:  I King Jordan; Igor B Rogozin; Yuri I Wolf; Eugene V Koonin
Journal:  Genome Res       Date:  2002-06       Impact factor: 9.043

9.  Peptidase family U34 belongs to the superfamily of N-terminal nucleophile hydrolases.

Authors:  Jimin Pei; Nick V Grishin
Journal:  Protein Sci       Date:  2003-05       Impact factor: 6.725

10.  Evolution of photosynthetic prokaryotes: a maximum-likelihood mapping approach.

Authors:  Jason Raymond; Olga Zhaxybayeva; J Peter Gogarten; Robert E Blankenship
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2003-01-29       Impact factor: 6.237

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