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Figure 2 | BMC Biochemistry

Figure 2

From: The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases

Figure 2

Sequence comparison and phylogenetic relationship of LAPTc to other members of the M17 family of metallopeptidases. (A), Multiple C-portion amino acid sequence alignments of different LAPs. Amino acid sequences from the conserved C-terminal region of LAPs were aligned by the ClustalX program. Amino acids marked in black show 50% identity and those in gray show 50% similarity. Putative metal binding sites (*), catalytic site (#), and M17 signature (underlined) are indicated. Sequences were obtained from the protein database of the National Center for Biotechnology Information (NCBI) under the following accession numbers: EAN87580.1 (T. cruzi 1) and EAN97960.1 (T. cruzi 2), EAN79621.1 (T. brucei 1) and AAX70152.1(T. brucei 2), CAJ02694.1 (L. major 1) and AAL16097.1(L. major 2), CAM36610.1 (L. braziliensis), YP_672349.1 (E. coli), NP_194821.1 (A. thaliana), AAD17527.1 (H. sapiens). (B), Phylogenetic relationship of LAPTc to other LAPs of different organisms. 29 full-length sequences, derived from the nonreduntant (NR) protein database of the NCBI (listed in Experimental Procedures), were aligned by the ClustalX program, and the phylogram was generated with the Mega package after 10,000 bootstraps with the neighbor joining (NJ) algorithm. The bar scale at the bottom represents 10% amino acid substitution per site. LAPTc is indicated by a closed square.

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