The taxonomic affiliation (in the systematisation of viruses and biological domains) of known peptides and proteins of biomineralization (silicateins, silaffins, silacidins and silicase) and their primary structure homologues were analysed (methods in silico; using Uniprot database). The total number of known peptides and proteins of biosilicification was counted. The data of the quantitative distribution of the detected homologues found in nature are presented. The similarity of the primary structures of silaffins, silacidins, silicateins, silicase and their homologues was 21-94%, 45-98%, 39-50% and 28-40%, respectively. These homologues are found in many organisms, from the Protista to the higher plants and animals, including humans, as well as in bacteria and extracellular agents, and they perform a variety of biological functions, such as biologically controlled mineralisation. The provisional classification of these biomineralization proteins is presented. The interrelation of the origin of the first organic polymers and biomineralization is discussed.
BioMed Research International, vol. 2013, Article ID 397278, 7 pages, 2013. doi:10.1155/2013/397278

In this paper computer research data of silicateins (50), silicases (1), silaffins (5), silicon transporters and magnetosome proteins (97) are presented. The research was carried out with the use of biological processing servers UniProt (www.uniprot.org) and Blast (www.ncbi.nlm.nih.gov). It is shown that the proteins which have the biomineralization mechanism and homological to them are widely spread in the tree of life and could be met in different organisms starting with protozoa to humans.
Pacific science review, 2011. – Vol. 13, №1. – P. 39-46.