| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AQQ67400.1 | AQQ69113.1 | Mag101_06940 | Mag101_16865 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.407 |
| AQQ69109.1 | AQQ69110.1 | Mag101_16845 | Mag101_16850 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.773 |
| AQQ69109.1 | AQQ69111.1 | Mag101_16845 | Mag101_16855 | Hypothetical 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. | 0.773 |
| AQQ69109.1 | AQQ69112.1 | Mag101_16845 | Mag101_16860 | Hypothetical 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. | 0.817 |
| AQQ69109.1 | AQQ69113.1 | Mag101_16845 | Mag101_16865 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.437 |
| AQQ69110.1 | AQQ69109.1 | Mag101_16850 | Mag101_16845 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.773 |
| AQQ69110.1 | AQQ69111.1 | Mag101_16850 | Mag101_16855 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.773 |
| AQQ69110.1 | AQQ69112.1 | Mag101_16850 | Mag101_16860 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.773 |
| AQQ69110.1 | AQQ69113.1 | Mag101_16850 | Mag101_16865 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.437 |
| AQQ69111.1 | AQQ69109.1 | Mag101_16855 | Mag101_16845 | Hypothetical 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. | 0.773 |
| AQQ69111.1 | AQQ69110.1 | Mag101_16855 | Mag101_16850 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.773 |
| AQQ69111.1 | AQQ69112.1 | Mag101_16855 | Mag101_16860 | Hypothetical 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. | 0.956 |
| AQQ69111.1 | AQQ69113.1 | Mag101_16855 | Mag101_16865 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.437 |
| AQQ69112.1 | AQQ69109.1 | Mag101_16860 | Mag101_16845 | Hypothetical 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. | 0.817 |
| AQQ69112.1 | AQQ69110.1 | Mag101_16860 | Mag101_16850 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.773 |
| AQQ69112.1 | AQQ69111.1 | Mag101_16860 | Mag101_16855 | Hypothetical 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. | 0.956 |
| AQQ69112.1 | AQQ69113.1 | Mag101_16860 | Mag101_16865 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.437 |
| AQQ69113.1 | AQQ67400.1 | Mag101_16865 | Mag101_06940 | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.407 |
| AQQ69113.1 | AQQ69109.1 | Mag101_16865 | Mag101_16845 | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.437 |
| AQQ69113.1 | AQQ69110.1 | Mag101_16865 | Mag101_16850 | Transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.437 |
