CDD: a database of conserved domain alignments with links to domain three-dimensional structure

被引:499
作者
Marchler-Bauer, A [1 ]
Panchenko, AR [1 ]
Shoemaker, BA [1 ]
Thiessen, PA [1 ]
Geer, LY [1 ]
Bryant, SH [1 ]
机构
[1] Natl Lib Med, Natl Ctr Biotechnol Informat, NIH, Bethesda, MD 20894 USA
关键词
D O I
10.1093/nar/30.1.281
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Conserved Domain Database (CDD) is a compilation of multiple sequence alignments representing protein domains conserved in molecular evolution. It has been populated with alignment data from the public collections Pfam and SMART, as well as with contributions from colleagues at NCBI. The current version of CDD (v.1.54) contains 3693 such models. CDD alignments are linked to protein sequence and structure data in Entrez. The molecular structure viewer Cn3D serves as a tool to interactively visualize alignments and three-dimensional structure, and to link three-dimensional residue coordinates to descriptions of evolutionary conservation. CDD can be accessed on the World Wide Web at http://www.ncbi.nlm.nih.gov/Structure/cdd/cdd.shtml. Protein query sequences may be compared against databases of position-specific score matrices derived from alignments in CDD, using a service named CD-Search, which can be found at http://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi. CD-Search runs reverse-position-specific BLAST (RPS-BLAST), a variant of the widely used PSI-BLAST algorithm. CD-Search is run by default for protein-protein queries submitted to NCBI's BLAST service at http://www.ncbi.nlm.nih.gov/BLAST.
引用
收藏
页码:281 / 283
页数:3
相关论文
共 13 条
  • [1] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    Altschul, SF
    Madden, TL
    Schaffer, AA
    Zhang, JH
    Zhang, Z
    Miller, W
    Lipman, DJ
    [J]. NUCLEIC ACIDS RESEARCH, 1997, 25 (17) : 3389 - 3402
  • [2] Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkp985, 10.1093/nar/gkh121, 10.1093/nar/gkr1065]
  • [3] Profile hidden Markov models
    Eddy, SR
    [J]. BIOINFORMATICS, 1998, 14 (09) : 755 - 763
  • [4] PROFILE ANALYSIS - DETECTION OF DISTANTLY RELATED PROTEINS
    GRIBSKOV, M
    MCLACHLAN, AD
    EISENBERG, D
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (13) : 4355 - 4358
  • [5] Henikoff S, 1997, PROTEIN SCI, V6, P698
  • [6] Hidden Markov models for detecting remote protein homologies
    Karplus, K
    Barrett, C
    Hughey, R
    [J]. BIOINFORMATICS, 1998, 14 (10) : 846 - 856
  • [7] The crystal structure of DNA mismatch repair protein MutS binding to a G•T mismatch
    Lamers, MH
    Perrakis, A
    Enzlin, JH
    Winterwerp, HHK
    de Wind, N
    Sixma, TK
    [J]. NATURE, 2000, 407 (6805) : 711 - 717
  • [8] Panchenko A, 1999, PROTEINS, P133
  • [9] Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods
    Park, J
    Karplus, K
    Barrett, C
    Hughey, R
    Haussler, D
    Hubbard, T
    Chothia, C
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1998, 284 (04) : 1201 - 1210
  • [10] SMART: a web-based tool for the study of genetically mobile domains
    Schultz, J
    Copley, RR
    Doerks, T
    Ponting, CP
    Bork, P
    [J]. NUCLEIC ACIDS RESEARCH, 2000, 28 (01) : 231 - 234