BAliBASE (Benchmark Alignment dataBASE): enhancements for repeats, transmembrane sequences and circular permutations

被引:130
作者
Bahr, A [1 ]
Thompson, JD [1 ]
Thierry, JC [1 ]
Poch, O [1 ]
机构
[1] Inst Genet & Biol Mol & Cellulaire, Lab Biol & Genom Struct, CNRS, INSERM,ULP, F-67404 Illkirch Graffenstaden, France
关键词
D O I
10.1093/nar/29.1.323
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
BAliBASE is specifically designed to serve as an evaluation resource to address all the problems encountered when aligning complete sequences, The database contains high quality, manually constructed multiple sequence alignments together with detailed annotations. The alignments are all based on three-dimensional structural superpositions, with the exception of the transmembrane sequences. The first release provided sets of reference alignments dealing with the problems of high variability, unequal repartition and large NIC-terminal extensions and internal insertions. Here we describe version 2.0 of the database, which incorporates three new reference sets of alignments containing structural repeats, transmembrane sequences and circular permutations to evaluate the accuracy of detection/prediction and alignment of these complex sequences. BAliBASE can be viewed at the web site http://www-igbmc.u-strasbg.fr/ BioInfo/BAliBASE2/index.html or can be downloaded from ftp://ftp-igbmc.u-strasbg.fr/pub/BAIiBASE2/.
引用
收藏
页码:323 / 326
页数:4
相关论文
共 19 条
[1]
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
[2]
Homology-based method for identification of protein repeats using statistical significance estimates [J].
Andrade, MA ;
Ponting, CP ;
Gibson, TJ ;
Bork, P .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 298 (03) :521-537
[3]
Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkp985, 10.1093/nar/gkh121, 10.1093/nar/gkr1065]
[4]
Computational approaches to identify leucine zippers [J].
Bornberg-Bauer, E ;
Rivals, E ;
Vingron, M .
NUCLEIC ACIDS RESEARCH, 1998, 26 (11) :2740-2746
[5]
Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method [J].
Cserzo, M ;
Wallin, E ;
Simon, I ;
vonHeijne, G ;
Elofsson, A .
PROTEIN ENGINEERING, 1997, 10 (06) :673-676
[6]
PROFILE ANALYSIS - DETECTION OF DISTANTLY RELATED PROTEINS [J].
GRIBSKOV, M ;
MCLACHLAN, AD ;
EISENBERG, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (13) :4355-4358
[7]
A simple method for predicting transmembrane α helices with better accuracy [J].
Gromiha, MM .
PROTEIN ENGINEERING, 1999, 12 (07) :557-561
[8]
A METHOD TO RECOGNIZE DISTANT REPEATS IN PROTEIN SEQUENCES [J].
HERINGA, J ;
ARGOS, P .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1993, 17 (04) :391-411
[9]
SOSUI: classification and secondary structure prediction system for membrane proteins [J].
Hirokawa, T ;
Boon-Chieng, S ;
Mitaku, S .
BIOINFORMATICS, 1998, 14 (04) :378-379
[10]
Prediction of membrane proteins based on classification of transmembrane segments [J].
Kihara, D ;
Shimizu, T ;
Kanehisa, M .
PROTEIN ENGINEERING, 1998, 11 (11) :961-970