Analysis of DNA sequences coding for the C-terminus of spider silk proteins from a range of spiders suggests that many silk C-termini share a common origin, and that their physical properties have been highly conserved over several hundred million years. These physical properties are compatible with roles in protein synthesis, silk function and in recruiting accessory proteins. Phylogenetic relationships among different silk genes suggest that any recombination has been insufficient to homogenize the different types of silk gene, which appear to have evolved independently of one another. The types of nucleotide substitutions that have occurred suggest that selection may have operated differently in the various silk lineages. Amino acid sequences of flagelliform silk C-termini differ substantially from the other types of spider silk studied, but they are expected to have very similar physical properties and may perform a similar function.