Affiliations: Molecular Biophysics Unit, Indian Institute of
Science, Bangalore 560 012, India | Present address: Center of Excellence in
Bioinformatics, University at Buffalo, NY, USA
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.
Keywords: Functional domains, phosphatases, protein domains, sequence analysis, sulfatases
