| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD30016.1 | ABD30293.1 | SAOUHSC_00891 | SAOUHSC_01186 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, putative; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | Conserved hypothetical protein. | 0.816 |
| ABD30016.1 | ABD30376.1 | SAOUHSC_00891 | SAOUHSC_01275 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, putative; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | Conserved hypothetical protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.792 |
| ABD30016.1 | ABD30915.1 | SAOUHSC_00891 | SAOUHSC_01849 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, putative; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | Conserved hypothetical protein. | 0.830 |
| ABD30016.1 | dnaJ | SAOUHSC_00891 | SAOUHSC_01682 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, putative; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | DnaJ protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and Gr [...] | 0.845 |
| ABD30016.1 | pcp | SAOUHSC_00891 | SAOUHSC_03025 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, putative; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | Pyrrolidone-carboxylate peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.790 |
| ABD30291.1 | ABD30293.1 | SAOUHSC_01184 | SAOUHSC_01186 | Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | Conserved hypothetical protein. | 0.978 |
| ABD30291.1 | ABD30294.1 | SAOUHSC_01184 | SAOUHSC_01187 | Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | Conserved hypothetical protein. | 0.908 |
| ABD30291.1 | def-2 | SAOUHSC_01184 | SAOUHSC_01182 | Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | Polypeptide deformylase, putative; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.875 |
| ABD30291.1 | fmt | SAOUHSC_01184 | SAOUHSC_01183 | Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.998 |
| ABD30291.1 | rlmN | SAOUHSC_01184 | SAOUHSC_01185 | Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. Confers resistance to some classes of antibiotics; Belongs to the radical SAM superfamily. RlmN family. | 0.991 |
| ABD30293.1 | ABD30016.1 | SAOUHSC_01186 | SAOUHSC_00891 | Conserved hypothetical protein. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, putative; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | 0.816 |
| ABD30293.1 | ABD30291.1 | SAOUHSC_01186 | SAOUHSC_01184 | Conserved hypothetical protein. | Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.978 |
| ABD30293.1 | ABD30294.1 | SAOUHSC_01186 | SAOUHSC_01187 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.998 |
| ABD30293.1 | ABD30376.1 | SAOUHSC_01186 | SAOUHSC_01275 | Conserved hypothetical protein. | Conserved hypothetical protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.810 |
| ABD30293.1 | ABD30915.1 | SAOUHSC_01186 | SAOUHSC_01849 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.837 |
| ABD30293.1 | def-2 | SAOUHSC_01186 | SAOUHSC_01182 | Conserved hypothetical protein. | Polypeptide deformylase, putative; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.857 |
| ABD30293.1 | dnaJ | SAOUHSC_01186 | SAOUHSC_01682 | Conserved hypothetical protein. | DnaJ protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and Gr [...] | 0.820 |
| ABD30293.1 | fmt | SAOUHSC_01186 | SAOUHSC_01183 | Conserved hypothetical protein. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.986 |
| ABD30293.1 | pcp | SAOUHSC_01186 | SAOUHSC_03025 | Conserved hypothetical protein. | Pyrrolidone-carboxylate peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.808 |
| ABD30293.1 | rlmN | SAOUHSC_01186 | SAOUHSC_01185 | Conserved hypothetical protein. | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. Confers resistance to some classes of antibiotics; Belongs to the radical SAM superfamily. RlmN family. | 0.891 |