CD-Search: protein domain annotations on the fly - PubMed
- ️Thu Jan 01 2004
. 2004 Jul 1;32(Web Server issue):W327-31.
doi: 10.1093/nar/gkh454.
Affiliations
- PMID: 15215404
- PMCID: PMC441592
- DOI: 10.1093/nar/gkh454
CD-Search: protein domain annotations on the fly
Aron Marchler-Bauer et al. Nucleic Acids Res. 2004.
Abstract
We describe the Conserved Domain Search service (CD-Search), a web-based tool for the detection of structural and functional domains in protein sequences. CD-Search uses BLAST(R) heuristics to provide a fast, interactive service, and searches a comprehensive collection of domain models. Search results are displayed as domain architecture cartoons and pairwise alignments between the query and domain-model consensus sequences. Search results may be visualized in further detail by embedding the query sequence into multiple alignment displays and by mapping onto three-dimensional molecular graphic displays of known structures within the domain family. CD-Search can be accessed at http://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi.
Figures

Graphical summary of results and hit list. The query sequence used in this search was gi|116863 (9).

A fragment of the query sequence embedded in the domain alignment for hemopexin-like repeats. Conserved features (metal binding sites) are indicated with hash marks on top of aligned columns.

Alignment visualization in the context of 3D structure. The query sequence has been added to the domain-alignment model. In this particular view the user visualizes evidence for the metal binding site (a conserved feature of this family), which is provided by the solved 3D structure of a protein–metal complex.
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