RSDB: representative protein sequence databases have high information content

被引:32
作者
Park, J [1 ]
Holm, L
Heger, A
Chothia, C
机构
[1] European Bioinformat Inst, EMBL Outstn, Cambridge CB10 1SD, England
[2] Univ Cambridge, Ctr Mrc, LMB, Cambridge CB2 2QH, England
关键词
D O I
10.1093/bioinformatics/16.5.458
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Motivation: Biological sequence databases are highly redundant for two main reasons. 1. various databanks keep redundant sequences with many identical and nearly identical sequences 2. natural sequences often have high sequence identities due to gene duplication. We wanted to know how many sequences call be removed before the databases start losing homology information. Can a database of sequences with mutual sequence identity of 50% or less provide us with the same amount of biological information as the original full database ? Results: Comparisons of nine representative sequence databases (RSDB) derived from full protein databanks showed that the information content of sequence databases is not linearly proportional to its size. An RSDB reduced to mutual sequence identity of around 50% (RSDB50) was equivalent to the original full database irt terms of the effectiveness of homology searching. It was a third of the full database size which resulted in a six times faster iterative profile searching. The RSDBs are produced at different granularity for efficient homology searching. Availability: All the RSDB files generated ann the full analysis results are available through internet: ftp://ftp.ebi.ac.uk/pub/contrib/jong/RSDB/ http://cyrah.ebi. ac.uk:1111/Proj/Bio/RSDB Contact: jong@biosophy/org.
引用
收藏
页码:458 / 464
页数:7
相关论文
共 39 条
[1]  
Altschul SF, 1996, METHOD ENZYMOL, V266, P460
[2]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[3]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[4]   HIDDEN MARKOV-MODELS OF BIOLOGICAL PRIMARY SEQUENCE INFORMATION [J].
BALDI, P ;
CHAUVIN, Y ;
HUNKAPILLER, T ;
MCCLURE, MA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (03) :1059-1063
[5]   Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins [J].
Bateman, A ;
Birney, E ;
Durbin, R ;
Eddy, SR ;
Finn, RD ;
Sonnhammer, ELL .
NUCLEIC ACIDS RESEARCH, 1999, 27 (01) :260-262
[6]  
BLEASBY AJ, 1994, NUCLEIC ACIDS RES, V22, P3574
[7]   CONSTRUCTION OF VALIDATED, NONREDUNDANT COMPOSITE PROTEIN-SEQUENCE DATABASES [J].
BLEASBY, AJ ;
WOOTTON, JC .
PROTEIN ENGINEERING, 1990, 3 (03) :153-159
[8]   Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships [J].
Brenner, SE ;
Chothia, C ;
Hubbard, TJP .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (11) :6073-6078
[9]   A structural explanation for the twilight zone of protein sequence homology [J].
Chung, SY ;
Subbiah, S .
STRUCTURE, 1996, 4 (10) :1123-1127
[10]  
Doolittle R.F., 1986, Of Urfs and Orfs: A Primer on How to Analyze Derived Amino Acid Sequences