DAP Evolutionary Analysis
'Blastp' results of the query sequence gi|119390187|pdb|2IJZ|A (Chain A, Crystal Structure Of Aminopeptidase) against non-redundant (-nr) database was selectively chosen for multiple sequence alignment using ClustalX 1.83.
“Sequence of aspartyl aminopeptidase is highly conserved. For example, the human enzyme has 51% identity to an “aspartyl-aminopeptidase-like protein” in Arabidopsis Thaliana (Accession Number BAA97497)” –Wilk .et, al. 2002. This is true to our protein sequence which originated from Pseudomonas Aeruginosa.
Aspartyl aminopeptidase belongs to the M18 family of clan MH cocatalytic metallopeptidases [reference no 14 wilk 2002 paper]. The M18 family is widely represented in both eukaryotes and prokaryotes. It is not known how many of the other members of the M18 family are also aspartyl aminopeptidases since most of the entries in the databases derive from genome sequencing and the enzymatic activities of the encoded proteins have not been determined. Many M18 family members are highly homologous to aspartyl aminopeptidase, and it is likely that they are also aspartyl aminopeptidases (Wilk .et, al. 2002).
Sequence of the query aminopeptidase protein is highly conserved throughout multiple sequence alignment from the many other organisms, suggesting a fundamental role for this enzyme in cellular functions.
Talk about histidine residues.
Talk about the vertical gene transfer not lateral thing
From the rectangular cladogram view of bootstrapped rooted tree, it could be observed using five-kingdom biological taxonomy that all five kingdoms are present in the tree, namely Archaea, Eubacteria, Fungi, Animalia, Plantae and Protista.