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Biol Direct. 2016 May 31;11:27. doi: 10.1186/s13062-016-0130-9.

Computational recognition and analysis of hitherto uncharacterized nucleotide cyclase-like proteins in bacteria.

Author information

1
Indian Institute of Science Mathematics Initiative, Indian Institute of Science, Bangalore, 560012, India.
2
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, India.
3
Undergraduate studies, Indian Institute of Science, Bangalore, 560012, India.
4
Department of Biochemistry, Indian Institute of Science, Bangalore, 560012, India.
5
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, India. ns@mbu.iisc.ernet.in.

Abstract

Evolutionary relationship between class III nucleotide cyclases and an uncharacterized set of bacterial proteins from Actinobacteria, Bacteroidetes and Proteobacteria has been recognized and analyzed. Detailed analyses of sequence and structural features resulted in the recognition of potential cyclase function conferring residues and presence of signature topological motif (βααββαβ) in the uncharacterized set of bacterial proteins. Lack of transmembrane domains and signal peptide cleavage sites is suggestive of their cytosolic subcellular localization. Furthermore, analysis on evolutionarily conserved gene clusters of the predicted nucleotide cyclase-like proteins and their evolutionary relationship with nucleotide cyclases suggest their participation in cellular signalling events. Our analyses suggest expansion of class III nucleotide cyclases.

REVIEWERS:

This article was reviewed by Eugene Koonin and Michael Gromiha.

KEYWORDS:

Distant relationship; Domain of unknown function; Mycobacteria; Nucleotide cyclase; Protein evolution; Sequence analysis

PMID:
27246835
PMCID:
PMC4886424
DOI:
10.1186/s13062-016-0130-9
[Indexed for MEDLINE]
Free PMC Article

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