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Figure 1 | Malaria Journal

Figure 1

From: The dimerization domain of Pf CENP-C is required for its functions as a centromere protein in human malaria parasite Plasmodium falciparum

Figure 1

Identification of Pf CENP-C and mapping of Pf CENP-C conserved domains, the CENP-C motif and dimerization domain. (A) (i) The schematic representation of the regions of homology (black bars) between the full-length Pf CENP-C, MIF2p (S. cerevisiae CENP-C) and human CENP-C using BLASTp analysis. The regions of maximum homology are confined to the centre and the C-terminus region. Percent pair-wise similarity of full-length Pf CENP-C with full-length yeast MIF2p and human CENP-C were acquired by Needleman-Wunsch alignment. The full-length Pf CENP-C shares 10.8 and 17.5% amino acid sequence similarities with MIF2p and CENP-C, respectively. (ii) The schematic representation of the Pf CENP-C motif (green) and Pf CENP-C dimerization domain (orange) based on the sequence comparisons and in silico analyses. The region before the Pf CENP-C motif is represented as the N-terminal region (grey). The numbers indicate the amino acid positions. (B) Sequence comparison between the conserved CENP-C motifs. The CENP-C motif of P. falciparum shares 30 and 63% homology with Sc CENP-C and Hs CENP-C motifs, respectively. The red-shaded boxes represent the identical amino acids. (C) Sequence comparison of the dimerization domains (DD). The Pf CENP-C-DD shows 50 and 46% homology with the yeast and human CENP-C dimerization domains, respectively. The conserved amino acid residues in the dimerization domains of Pf CENP-C and MIF2p are indicated by arrows. (Pf- Plasmodium falciparum; Sc- Saccharomyces cerevisiae; Hs- Homo sapiens).

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