| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| def1 | fmt | SH09_06935 | SH09_06930 | 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. | 0.982 |
| def1 | prkC_1 | SH09_06935 | SH09_06910 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.869 |
| def1 | ribBA_2 | SH09_06935 | SH09_04215 | 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. | GTP cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the DHBP synthase family. | 0.421 |
| def1 | rlmN | SH09_06935 | SH09_06920 | 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. | 0.900 |
| def1 | rsmB | SH09_06935 | SH09_06925 | 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. | 16S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.925 |
| def1 | stp_1 | SH09_06935 | SH09_06915 | 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 |
| fmt | def1 | SH09_06930 | SH09_06935 | 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. | 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. | 0.982 |
| fmt | prkC_1 | SH09_06930 | SH09_06910 | 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. | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.883 |
| fmt | rlmN | SH09_06930 | SH09_06920 | 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. | 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. | 0.938 |
| fmt | rsmB | SH09_06930 | SH09_06925 | 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. | 16S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.999 |
| fmt | stp_1 | SH09_06930 | SH09_06915 | 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. | Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.972 |
| pbpX_2 | prkC_1 | SH09_07110 | SH09_06910 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.892 |
| pbpX_2 | ribBA_2 | SH09_07110 | SH09_04215 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | GTP cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the DHBP synthase family. | 0.581 |
| pbpX_2 | rlmN | SH09_07110 | SH09_06920 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.467 |
| pbpX_2 | rsmB | SH09_07110 | SH09_06925 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 16S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.692 |
| pbpX_2 | sigS | SH09_07110 | SH09_04180 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.525 |
| pbpX_2 | stp_1 | SH09_07110 | SH09_06915 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.884 |
| pbpX_2 | ydgH | SH09_07110 | SH09_14820 | Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.523 |
| prkC_1 | def1 | SH09_06910 | SH09_06935 | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.869 |
| prkC_1 | fmt | SH09_06910 | SH09_06930 | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.883 |