plosone-phylo
Figure 1
MAG_5040 organization and position of homologs in the genome of phylogenetically related bacteria.(A) MAG_5040 schematic diagram. MAG_5040 is comprised of 390 amino acids and contains a hydrophobic N-terminal signal sequence and a prokaryotic lipoprotein cleavage site (indicated by the grey box). Amino acids 182 through 343 have significant identity and similarity with the TNASE_3 domain profile of the Staphylococcus aureus thermonuclease (SNc). Conserved amino acid residues involved in binding of divalent ions are indicated by arrowed vertical lines. Position of amino acids comprising the active catalytic site are shown as vertical lines with round tips. (B) Physical map of mycoplasma homologs of the putative MAG_5030-MAG_5040-MAG_5050-MAG_5060-MAG_5070 ABC transport system. Homologous proteins are shaded in the same pattern, and their amino acid identities to the corresponding M. agalactiae PG2T proteins are indicated above each row. Phylogeny based on the amino acid alignment of the SNc homologs is shown on the left.
Figure 1
MAG_5040 organization and position of homologs in the genome of phylogenetically related bacteria.(A) MAG_5040 schematic diagram. MAG_5040 is comprised of 390 amino acids and contains a hydrophobic N-terminal signal sequence and a prokaryotic lipoprotein cleavage site (indicated by the grey box). Amino acids 182 through 343 have significant identity and similarity with the TNASE_3 domain profile of the Staphylococcus aureus thermonuclease (SNc). Conserved amino acid residues involved in binding of divalent ions are indicated by arrowed vertical lines. Position of amino acids comprising the active catalytic site are shown as vertical lines with round tips. (B) Physical map of mycoplasma homologs of the putative MAG_5030-MAG_5040-MAG_5050-MAG_5060-MAG_5070 ABC transport system. Homologous proteins are shaded in the same pattern, and their amino acid identities to the corresponding M. agalactiae PG2T proteins are indicated above each row. Phylogeny based on the amino acid alignment of the SNc homologs is shown on the left.