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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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