Signature pattern analysis of various pectinases using in silico tools

Author: 
Suman Kumari

Protein sequence of pectin lyases as available in NCBI was subjected for multiple sequence alignment, conserved domain analysis, topology and phylogenetic tree construction. Acetyl xylan esterase showed the maximum similarity indexed (99%) isolated from A. flavus having length of protein 307 with XP_002378019 accession number in hydrolytic depolymerase where as Polyhydroxybutyrate depolymerase showed the maximum similarity indexed raised from Burkholderia pseudomallei having length of protien 364 with YP_001077537 accession number. In depolymerase trans-membrane protein from Burkholderia pseudomallei showed presence of three helics located on 47-66, 97-120 and 178-201. Other proteins showed zero and one number of helics. Hydrolytic depolymerase showed four conserved motifs as Ferttrrygkpewgldxtel, Smtlggtidrrnptxayn, Rvamtvgndisgigqteaxh And Gvghgvfngsrfrseivpri as per sequence alignment where as estrase also showed four conserved motifs Sgltceqnfixksg, Vdpxxsfgshmgghgal, Sfghsmgghgal And Kipvvfrqegydhsy as per sequence alignment but depolymerase was not showed any conserved motifs.

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DOI: http://dx.doi.org/10.24327/ijcar.2017.5441.0724
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