Bhadra, Rana and Srinivasan, Narayanaswamy and Pandit, Shashi B (2005) A New Domain Family in the Superfamily of Alkaline Phosphatases. In: In Silico Biology, 5 (4). pp. 379-387.
Full text not available from this repository. (Request a copy)Abstract
During the course of our large-scale genome analysis a conserved domain, currently detectable only in the genomes of Drosophila melanogaster, Caenorhabditis elegans and Anopheles gambiae, has been identified. The function of this domain is currently unknown and no function annotation is provided for this domain in the publicly available genomic, protein family and sequence databases. The search for the homologues of this domain in the non-redundant sequence database using PSI-BLAST, resulted in identification of distant relationship between this family and the alkaline phosphatase-like superfamily, which includes families of aryl sulfatase, N-acetylgalactosomine-4-sulfatase, alkaline phosphatase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGM). The fold recognition procedures showed that this new domain could adopt a similar 3-D fold as for this supefamily. Most of the phosphatases and sulfatases of this superfamily are characterized by functional residues Ser and Cys respectively in the topologically equivalent positions. This functionally important site aligns with Ser/Thr in the members of the new family. Additionally, set of residues responsible for a metal binding site in phosphatases and sulphtases are conserved in the new family. The in-depth analysis suggests that the new family could possess phosphatase activity.
| Item Type: | Journal Article |
|---|---|
| Publication: | In Silico Biology |
| Publisher: | IOS Press |
| Additional Information: | The Copyright belongs to IOS Press. |
| Keywords: | Functional domains;phosphatases;protein domains;sequence analysis;sulfatases |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 20 Jan 2006 |
| Last Modified: | 27 Aug 2008 11:40 |
| URI: | http://eprints.iisc.ac.in/id/eprint/4889 |
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