node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KPL88521.1 | cbpA | SE16_06970 | SE16_06965 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.473 |
KPL88521.1 | greA | SE16_06970 | SE16_02100 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.440 |
KPL88521.1 | rluD | SE16_06970 | SE16_06975 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.705 |
KPL88521.1 | rpoA | SE16_06970 | SE16_00245 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.814 |
KPL88521.1 | rpoB | SE16_06970 | SE16_10945 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.852 |
cbpA | KPL88521.1 | SE16_06965 | SE16_06970 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.473 |
cbpA | rluD | SE16_06965 | SE16_06975 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.902 |
greA | KPL88521.1 | SE16_02100 | SE16_06970 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.440 |
greA | rpoA | SE16_02100 | SE16_00245 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.929 |
greA | rpoB | SE16_02100 | SE16_10945 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.949 |
rluD | KPL88521.1 | SE16_06975 | SE16_06970 | Hypothetical protein; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.705 |
rluD | cbpA | SE16_06975 | SE16_06965 | Hypothetical protein; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.902 |
rpoA | KPL88521.1 | SE16_00245 | SE16_06970 | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.814 |
rpoA | greA | SE16_00245 | SE16_02100 | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.929 |
rpoA | rpoB | SE16_00245 | SE16_10945 | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.999 |
rpoB | KPL88521.1 | SE16_10945 | SE16_06970 | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
rpoB | greA | SE16_10945 | SE16_02100 | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.949 |
rpoB | rpoA | SE16_10945 | SE16_00245 | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.999 |