Figure 1

Structural diversity of the TvBspA proteins. (A) Proteins with an inferred TMD (black boxes) are contrasted with those without them. In both case a fraction of entries are inferred to posses a SP (red boxes, brackets illustrate variability). A few TvBspA have more then one TMD but these are not depicted. In addition to the TpLRR (green boxes) some proteins also possessed other type of repeats (R) or low complexity segments (LC) of various lengths (pink box) typically located between the TpLRR and the TMD (additional file 10, Table S7). Notable structural variants are illustrated in panels B and C and variation in the length of the TpLRR in panels D and E. (B) The 12 TvBspA entries forming a subfamily that share a glycine-rich domain (blue box, GRD). Their TpLRR lengths range from 16 to 20 repeats. Four proteins have an inferred SP and one has a TMD. (C) A TvBspA entry with InterProScan hits indicating a partial peptidase S8/S53-like domain (purple box - Pfam domain PF00082) and a galactose-binding domain (red box - SUPERFAMILY domain SSF49785), both of which are typically found in extracellular proteins. One TvBspA proteins was also identified to possess ankirin-like repeats at its C-terminus end (data not shown). (D) Graph illustrating the relationship between the TvBspA TpLRR length and corresponding total length for proteins without TMD. The linear regression is shown (black line) and is contrasted with the y = x line (red dashed) and y = 1/2 x line (black dashed). (E) Corresponding graph (as shown in D) for the 193 TvBspA with TMD-CCT.