node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ARE82580.1 | ARE84111.1 | ROSMUCSMR3_01085 | ROSMUCSMR3_02642 | Hemin uptake protein HemP; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.552 |
ARE82657.1 | ARE84111.1 | ROSMUCSMR3_01163 | ROSMUCSMR3_02642 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.429 |
ARE84110.1 | ARE84111.1 | ROSMUCSMR3_02641 | ROSMUCSMR3_02642 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.899 |
ARE84110.1 | acsA-2 | ROSMUCSMR3_02641 | ROSMUCSMR3_02643 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.401 |
ARE84110.1 | uvrB | ROSMUCSMR3_02641 | ROSMUCSMR3_02639 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | 0.533 |
ARE84110.1 | yciC-2 | ROSMUCSMR3_02641 | ROSMUCSMR3_02640 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | Putative metal chaperone YciC; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.948 |
ARE84111.1 | ARE82580.1 | ROSMUCSMR3_02642 | ROSMUCSMR3_01085 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hemin uptake protein HemP; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.552 |
ARE84111.1 | ARE82657.1 | ROSMUCSMR3_02642 | ROSMUCSMR3_01163 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.429 |
ARE84111.1 | ARE84110.1 | ROSMUCSMR3_02642 | ROSMUCSMR3_02641 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | 0.899 |
ARE84111.1 | acsA-2 | ROSMUCSMR3_02642 | ROSMUCSMR3_02643 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.401 |
ARE84111.1 | uvrB | ROSMUCSMR3_02642 | ROSMUCSMR3_02639 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | 0.533 |
ARE84111.1 | yciC-2 | ROSMUCSMR3_02642 | ROSMUCSMR3_02640 | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Putative metal chaperone YciC; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.906 |
acsA-2 | ARE84110.1 | ROSMUCSMR3_02643 | ROSMUCSMR3_02641 | Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | 0.401 |
acsA-2 | ARE84111.1 | ROSMUCSMR3_02643 | ROSMUCSMR3_02642 | Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.401 |
acsA-2 | yciC-2 | ROSMUCSMR3_02643 | ROSMUCSMR3_02640 | Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family. | Putative metal chaperone YciC; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.401 |
uvrB | ARE84110.1 | ROSMUCSMR3_02639 | ROSMUCSMR3_02641 | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | 0.533 |
uvrB | ARE84111.1 | ROSMUCSMR3_02639 | ROSMUCSMR3_02642 | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.533 |
uvrB | yciC-2 | ROSMUCSMR3_02639 | ROSMUCSMR3_02640 | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | Putative metal chaperone YciC; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.541 |
yciC-2 | ARE84110.1 | ROSMUCSMR3_02640 | ROSMUCSMR3_02641 | Putative metal chaperone YciC; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg; protein of unknown function (DUF1826). | 0.948 |
yciC-2 | ARE84111.1 | ROSMUCSMR3_02640 | ROSMUCSMR3_02642 | Putative metal chaperone YciC; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hypothetical protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.906 |