A Biallelic Mutation in CCDC103 Impairs Sperm Motility due to the Absence of Dynein Arms

Figure 3

Amino acid conservation analysis of CCDC103 and the 3D reconstruction of the CCDC103 protein. (a) Gene structure (top) and protein conserved domain analysis (bottom) in CCDC103. The red and gray rectangles represent exons and UTR structures, respectively, while the gray lines represent introns. Different protein-conserved domains are represented by rectangles of different colors. CC, coiled coils, IDR, coiled coils, RPAP3_C, N-terminal of the RPAP3_C domain. (b) Multiple sequence alignment of seven species indicating the conserved nature of amino acids 55 and 154 sites (above), and the seqlogo picture showed the amino acid frequency of each site near the 55 and 154 sites in these seven species (below). (c) c1: CCDC103 protein model: ALA-158 forms hydrogen bonds with HIS-154 with a length of 1.9. c2: CCDC103 p.His154Pro protein model. c3, c4: CCDC103 and CCDC103 p.His55Serfs9 protein models, respectively. c5: Image c3 is superimposed onto the image of c4. The RMSD (root mean square deviation) is 17.329, indicating that the base deletion (c.161_162del) has a great influence on the protein structure.

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