| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJC96632.1 | acuC | SHYC_09505 | SHYC_05960 | Peptidylprolyl 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. | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.787 |
| AJC96632.1 | dnaJ | SHYC_09505 | SHYC_06650 | Peptidylprolyl 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. | Molecular chaperone DnaJ; 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, [...] | 0.801 |
| AJC96632.1 | glpF | SHYC_09505 | SHYC_07880 | Peptidylprolyl 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. | Glycerol uptake facilitator protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.729 |
| AJC96632.1 | pcp | SHYC_09505 | SHYC_02880 | Peptidylprolyl 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. | Pyrrolidone-carboxylate peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.728 |
| AJC96632.1 | prpC | SHYC_09505 | SHYC_08335 | Peptidylprolyl 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. | Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.742 |
| acuC | AJC96632.1 | SHYC_05960 | SHYC_09505 | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidylprolyl 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. | 0.787 |
| acuC | dnaJ | SHYC_05960 | SHYC_06650 | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; 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, [...] | 0.758 |
| acuC | glpF | SHYC_05960 | SHYC_07880 | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycerol uptake facilitator protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.738 |
| acuC | pcp | SHYC_05960 | SHYC_02880 | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrrolidone-carboxylate peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.742 |
| acuC | prpC | SHYC_05960 | SHYC_08335 | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.747 |
| def-1 | fmt | SHYC_08355 | SHYC_08350 | Peptide deformylase; 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. | 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. | 0.981 |
| def-1 | prkC | SHYC_08355 | SHYC_08330 | Peptide deformylase; 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. | Serine/threonine-protein kinase PrkC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.868 |
| def-1 | prpC | SHYC_08355 | SHYC_08335 | Peptide deformylase; 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. | Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.871 |
| def-1 | rlmN | SHYC_08355 | SHYC_08340 | Peptide deformylase; 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. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.899 |
| def-1 | rsmB | SHYC_08355 | SHYC_08345 | Peptide deformylase; 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. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.889 |
| dnaJ | AJC96632.1 | SHYC_06650 | SHYC_09505 | Molecular chaperone DnaJ; 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, [...] | Peptidylprolyl 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. | 0.801 |
| dnaJ | acuC | SHYC_06650 | SHYC_05960 | Molecular chaperone DnaJ; 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, [...] | Acetoin utilization protein AcuC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.758 |
| dnaJ | glpF | SHYC_06650 | SHYC_07880 | Molecular chaperone DnaJ; 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, [...] | Glycerol uptake facilitator protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.812 |
| dnaJ | pcp | SHYC_06650 | SHYC_02880 | Molecular chaperone DnaJ; 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, [...] | Pyrrolidone-carboxylate peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.743 |
| dnaJ | prpC | SHYC_06650 | SHYC_08335 | Molecular chaperone DnaJ; 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, [...] | Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.759 |
