We propose, therefore, that the double-proline motif is conserved for the purpose of domain swapping, which suggests that this phenomenon plays a role in the function of cks proteins.
This motif is conserved in all the species.
The γ-core motif is conserved in all antifungal plant defensins including MsDef1 and MtDef4.
The ATF motif is conserved and present in HAdV-D (Fig. 6).
The DQHA(X 2E(X)4E motif is conserved throughout known hPMS2 homologues.
This motif is conserved in the HN proteins of all APMVS sequenced to date (Table 4).
The STP motif is conserved in all sequences with the exception of the D. mojavensis duplicated copy.
This motif is conserved in all species except the sea urchin, which has an Alanine instead of the first Glycine.
Notably, in these cases the C-terminal hydrophobic region of the DRY/RVYVVV motif is conserved but the DRY motif is not found.
Concerning the interaction topology, we show that the position of the motif is conserved in the structure, while more flexibility is allowed for the placement of the context.
In silico analyses have suggested that the HT motif is conserved throughout the Plasmodium species but experimental evidence only exists for P. falciparum.
