node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
WL94_17930 | carB | DM42_427 | DM42_429 | Uncharacterized protein | CPSaseII_lrg- carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family | 0.598 |
WL94_17930 | greA | DM42_427 | DM42_428 | Uncharacterized protein | 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 | 0.846 |
carB | WL94_17930 | DM42_429 | DM42_427 | CPSaseII_lrg- carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family | Uncharacterized protein | 0.598 |
carB | greA | DM42_429 | DM42_428 | CPSaseII_lrg- carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family | 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 | 0.766 |
carB | polA | DM42_429 | DM42_4183 | CPSaseII_lrg- carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.634 |
carB | rpoB | DM42_429 | DM42_1481 | CPSaseII_lrg- carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates | 0.538 |
greA | WL94_17930 | DM42_428 | DM42_427 | 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 | Uncharacterized protein | 0.846 |
greA | carB | DM42_428 | DM42_429 | 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 | CPSaseII_lrg- carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family | 0.766 |
greA | nusG | DM42_428 | DM42_1486 | 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 | Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination | 0.823 |
greA | polA | DM42_428 | DM42_4183 | 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 polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.681 |
greA | rpoA | DM42_428 | DM42_1447 | 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 | 0.900 |
greA | rpoB | DM42_428 | DM42_1481 | 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 | 0.842 |
greA | rpoC | DM42_428 | DM42_1480 | 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 | 0.857 |
greA | rpoZ | DM42_428 | DM42_836 | 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 omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta’ subunit thereby facilitating its interaction with the beta and alpha subunits | 0.860 |
greA | rpsG | DM42_428 | DM42_1477 | 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 | 30S ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA | 0.665 |
greA | rpsP | DM42_428 | DM42_758 | 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 | S16- ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family | 0.670 |
nusG | greA | DM42_1486 | DM42_428 | Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination | 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 | 0.823 |
nusG | polA | DM42_1486 | DM42_4183 | Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.721 |
nusG | rpoA | DM42_1486 | DM42_1447 | Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination | DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates | 0.967 |
nusG | rpoB | DM42_1486 | DM42_1481 | Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates | 0.972 |