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Assigning genomic sequences to CATH
Open accessAbstract
We report the latest release (version 1.6) of the CATH protein domains database (http://www.biochem.ucl. ac.uk/bsm/cath ). This is a hierarchical classification of 18 577 domains into evolutionary families and structural groupings. We have identified 1028 homo-logous superfamilies in which the proteins have both structural, and sequence or functional similarity. These can be further clustered into 672 fold groups and 35 distinct architectures. Recent developments of the database include the generation of 3D templates for recognising structural relatives in each fold group, which has led to significant improvements in the speed and accuracy of updating the database and also means that less manual validation is required. We also report the establishment of the CATH-PFDB (Protein Family Database), which associates 1D sequences with the 3D homologous superfamilies. Sequences showing identifiable homology to entries in CATH have been extracted from GenBank using PSI-BLAST. A CATH-PSIBLAST server has been established, which allows you to scan a new sequence against the database. The CATH Dictionary of Homologous Superfamilies (DHS), which contains validated multiple structural alignments annotated with consensus functional information for evolutionary protein superfamilies, has been updated to include annotations associated with sequence relatives identified in GenBank. The DHS is a powerful tool for considering the variation of functional properties within a given CATH superfamily and in deciding what functional properties may be reliably inherited by a newly identified relative.
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Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288
Cited by
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Cheng, J., Randall, A. Z., Sweredoski, M. J., & Baldi, P. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki396 · Cited by 1,044
PDBsum: summaries and analyses of PDB structures
Laskowski, R. A. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.1.221 · Cited by 849
Multi-class protein fold recognition using support vector machines and neural networks
Ding, C. H. Q., & Dubchak, I. (2001) · Bioinformatics · doi:10.1093/bioinformatics/17.4.349 · Cited by 834
Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491
Fold Change in Evolution of Protein Structures
Grishin, N. V. (2001) · Journal of Structural Biology · doi:10.1006/jsbi.2001.4335 · Cited by 444
Metadata
- Authors
- Pearl, F. M. G.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2000-01-01
- Volume
- 28
- Issue
- 1
- Pages
- 277-282
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2167197805
- Cited by
- 191
- References
- 1
- FWCI
- 8.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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