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OJBTM

Online Journal of Bioinformatics

Volume 14 (1): 56-65, 2013


Sequence informatics of carbonic anhydrase from different source organisms

 

Vivek Dhar Dwivedi, Shikha Arora, Jyoti Sharma, and Amit Pandey*

 

Forest Pathology Division, Forest Research Institute, Dehradun, India

 

ABSTRACT

 

Dwivedi VD, Arora S, Sharma J, Pandey A Sequence Informatics of Carbonic anhydrase Enzyme from Different Source organisms, Online J Bioinform., 14 (1): 56-65, 2013. Carbonic anhydrases are widely distributed among bacteria, fungi, plants and animals. Forty full length amino acid sequences of the enzyme were subjected to multiple sequence alignment (MSA), motif identification, domain identification, individual amino acid composition and phylogenetic analysis. MSA revealed that 1 alanine and glutamic acid residues were semi-conserved in all sequences while 1 proline and glycine residues were identically conserved in all sequences of fungi. Two major sequence clusters were obtained by phylogenetic analysis. One cluster contains 10 species of animals, 9 fungi, 2 bacteria and 1 plant, whereas another cluster contains 9 species of plants, 8 bacteria, and 1 fungus but no animal species were found in this cluster. Amino acid composition results revealed that the average frequency of alanine residue was 8.99% which was very high compared with the average frequency of other amino acids in all analyzed sequences. Fifteen amino acids Motif (QSPKAMVLACSDSRV) were found in all bacterial and plant sources. In addition, some motifs belonging to Pro_CA and Carb_anhydrase domain family unique to their groups, were also identified.

Keywords: Carbonic anhydrase, MSA, Phylogenetic analysis, Conserved regions, Motifs, Domains.


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