| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa1981 | PSHAa1982 | PSHAa1981 | PSHAa1982 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Homologs of previously reported genes of unknown function. | 0.804 |
| PSHAa1981 | PSHAa1983 | PSHAa1981 | PSHAa1983 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Homologs of previously reported genes of unknown function. | 0.800 |
| PSHAa1981 | PSHAa1984 | PSHAa1981 | PSHAa1984 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Putative orphan protein; No homology to any previously reported sequences. | 0.731 |
| PSHAa1981 | PSHAb0347 | PSHAa1981 | PSHAb0347 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Putative Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.713 |
| PSHAa1981 | htpG | PSHAa1981 | PSHAa1207 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.750 |
| PSHAa1981 | kdkA | PSHAa1981 | PSHAa2319 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Putative lipopolysaccharide kinase family; Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D- manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position; Belongs to the protein kinase superfamily. KdkA/RfaP family. | 0.696 |
| PSHAa1981 | rplO | PSHAa1981 | PSHAa2811 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 50S ribosomal subunit protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.670 |
| PSHAa1981 | rplU | PSHAa1981 | PSHAa2656 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 50S ribosomal subunit protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.673 |
| PSHAa1981 | rpsQ | PSHAa1981 | PSHAa0153 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 30S ribosomal subunit protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.669 |
| PSHAa1981 | sodB | PSHAa1981 | PSHAa1215 | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Iron superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.678 |
| PSHAa1982 | PSHAa1981 | PSHAa1982 | PSHAa1981 | Homologs of previously reported genes of unknown function. | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.804 |
| PSHAa1982 | PSHAa1983 | PSHAa1982 | PSHAa1983 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.998 |
| PSHAa1982 | PSHAa1984 | PSHAa1982 | PSHAa1984 | Homologs of previously reported genes of unknown function. | Putative orphan protein; No homology to any previously reported sequences. | 0.551 |
| PSHAa1983 | PSHAa1981 | PSHAa1983 | PSHAa1981 | Homologs of previously reported genes of unknown function. | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.800 |
| PSHAa1983 | PSHAa1982 | PSHAa1983 | PSHAa1982 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.998 |
| PSHAa1983 | PSHAa1984 | PSHAa1983 | PSHAa1984 | Homologs of previously reported genes of unknown function. | Putative orphan protein; No homology to any previously reported sequences. | 0.551 |
| PSHAa1984 | PSHAa1981 | PSHAa1984 | PSHAa1981 | Putative orphan protein; No homology to any previously reported sequences. | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.731 |
| PSHAa1984 | PSHAa1982 | PSHAa1984 | PSHAa1982 | Putative orphan protein; No homology to any previously reported sequences. | Homologs of previously reported genes of unknown function. | 0.551 |
| PSHAa1984 | PSHAa1983 | PSHAa1984 | PSHAa1983 | Putative orphan protein; No homology to any previously reported sequences. | Homologs of previously reported genes of unknown function. | 0.551 |
| PSHAb0347 | PSHAa1981 | PSHAb0347 | PSHAa1981 | Putative Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Putative Peptidyl-prolyl cis-trans isomerase (PPIase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.713 |