SMART: identification and annotation of domains from signalling and extracellular protein sequences
Open Access
- 1 January 1999
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 27 (1), 229-232
- https://doi.org/10.1093/nar/27.1.229
Abstract
SMART is a simple modular architecture research tool and database that provides domain identification and annotation on the WWW (http://coot.embl-heidelberg.de/SMART). The tool compares query sequences with its databases of domain sequences and multiple alignments whilst concurrently identifying compositionally biased regions such as signal peptide, transmembrane and coiled coil segments. Annotated and unannotated regions of the sequence can be used as queries in searches of sequence databases. The SMART alignment collection represents more than 250 signalling and extracellular domains. Each alignment is curated to assign appropriate domain boundaries and to ensure its quality. In addition, each domain is annotated extensively with respect to cellular localisation, species distribution, functional class, tertiary structure and functionally important residues.Keywords
This publication has 25 references indexed in Scilit:
- SMART, a simple modular architecture research tool: Identification of signaling domainsProceedings of the National Academy of Sciences, 1998
- Predicting functions from protein sequences—where are the bottlenecks?Nature Genetics, 1998
- Pfam: multiple sequence alignments and HMM-profiles of protein domainsNucleic Acids Research, 1998
- Superior performance in protein homology detection with the Blocks Database serversNucleic Acids Research, 1998
- Linking up with entrezTrends in Genetics, 1998
- PDBsum: a web-based database of summaries and analyses of all PDB structuresTrends in Biochemical Sciences, 1997
- Cytoplasmic signalling domains: the next generationTrends in Biochemical Sciences, 1997
- The PROSITE database, its status in 1997Nucleic Acids Research, 1997
- Structure and distribution of modules in extracellular proteinsQuarterly Reviews of Biophysics, 1996
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994