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Fig. 1 | BMC Cell Biology

Fig. 1

From: Myc-binding protein orthologue interacts with AKAP240 in the central pair apparatus of the Chlamydomonas flagella

Fig. 1

FAP174 harbours a RII-like fold (a) A BLAST of FAP174 was carried out and representative MYCBP-1-like sequences from species of plants, animals, algae and protozoans were selected and a phylogenetic tree was generated using MEGA6. Organisms and their Accession numbers used for this exercise are C. reinhardtii ACR55627, V. carterii XP_002950671.1, B. rapa NP_001288931.1, A. thaliana NP_671849.1, C. arabica ADY38785.1, C. sativus XP_004172365.1, O. sativa EEC81635.1, S. bicolor XP_002459454.1, S. lycopersicon XP_004236796.1, P. sitchensis ABR18049.1, A. mellifera XP_624300.1, S. kowaleskii XP_002733639.1, X. tropicalis NP_001017035.1, M. Domestica XP_001364995.1, P. troglodytes XP_003949426.1, M. mulatta XP_001113156.2, H. sapiens BAA09338.1, P. tetraaurelia XP_001442915.1, T. cruzi XP_805155.1, P. sojae XP_009522570.1, A. anophagefferens XP_009033259.1, E. siliculosus CBN77061.1 and T. gondii XP_002370315.1. (b) Alignment of representative sequences from those used for the Phylogenetic analysis. The sequence homology is the highest at the N-terminal region that is predicted to fold into a helix-loop-helix structure as expected of dimerization and docking domains. The C-terminus of FAP174 shows a propensity to form coiled-coils. Identical residues are shaded, arrows represent the helix-forming residues and the lines represent coiled-coil forming residues. (c) Multiple alignment of FAP174 with proteins contianing the D/D domain using the best matches from HHpred. (http://toolkit.tuebingen.mpg.de/hhpred). The sequences with the RIIa D/D domain and DPY-30 domains that showed significant match were aligned using Multiple Sequence Alignment software (Clustal Omega). Identical regions are shaded

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