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. 2020 Jun 4;133(11):jcs240838. doi: 10.1242/jcs.240838

Fig. 1.

Fig. 1.

TtPoc5 contains evolutionarily conserved Poc5 domains. (A) Schematics showing conserved organization of centrin-binding repeats (CBRs; gray boxes), predicted coiled-coil domains (green regions) and the Poc5 box (yellow box) in hPOC5 and TtPoc5. (B) Sequence alignment within the region containing an isolated CBR (CBR1), tandem CBRs (CBR2,3), and the Poc5 box. Identical residues are shaded in black and similar residues are shaded in gray. Asterisks denote conserved centrin-binding sequence motif (Ax7LLx3F/Lx2WK/R) residues. (C) Sequence logos showing the amino acid composition within 18-amino-acid sequence motifs (positions 6–23) of hPOC5 and TtPoc5 CBRs plus five upstream amino acids. Black residues indicate the high proportion of hydrophobic AAs at conserved positions (marked with asterisks). Hydrophilic residues are indicated in blue and neutral residues are indicated in green. (D) Multiple sequence alignment of the highly conserved 21-amino-acid Poc5 box across selected Poc5 orthologs.