When CsTegu20.6 was compared with six other tegumental proteins of C. sinensis, multiple sequences alignment of the amino acids revealed that CsTegu20.6 shares 39% identity with CsTegu21.1 (NCBI Accession No. ADZ13689.1) , 38% with CsTegu20.8 (ABC47326.1) , 29% with CsTegu21.6 (JF911532) , 38% with CsTegu_Ca_EF (ABZ82044), 32% with CsTegu22.3 (ABK60085.1)  and 35% with CsTegu31.8 (ABK60086.1)  (Figure 1). Both the consensus sequences (Asp46, Gly51, Ile53, Leu55, Cys59, Leu62 and Gly63, shaded in red) and the conserved helix-loop-helix (HLH) motif were observed in the calcium-binding EF-hand domain. The HLH structure is an important characteristic of EF-hand domains, of which residue mutation in the loop region can cause an inability of calcium-binding activity . The length of the EF-hand of CsTegu20.6 was almost similar to that of CsTegu21.6, which was conspicuously shorter than those of other C. sinensis tegumental proteins . The DLC domain was less conserved than the EF-hand domain. Although the functions of the DLC domain remain unclear, DLC appears to act as part of a large complex and to contribute to maintenance of the tegument .