node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DR97_1775 | DR97_266 | DR97_1775 | DR97_266 | Hypothetical protein; Pathogenesis-related protein | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | 0.673 |
DR97_265 | DR97_266 | DR97_265 | DR97_266 | Hypothetical protein; Uncharacterized protein | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | 0.854 |
DR97_266 | DR97_1775 | DR97_266 | DR97_1775 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Hypothetical protein; Pathogenesis-related protein | 0.673 |
DR97_266 | DR97_265 | DR97_266 | DR97_265 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Hypothetical protein; Uncharacterized protein | 0.854 |
DR97_266 | Gpo | DR97_266 | DR97_5115 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Glutathione peroxidase family protein; Belongs to the glutathione peroxidase family | 0.677 |
DR97_266 | argS | DR97_266 | DR97_2406 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Arginyl-trna synthetase; argS: arginine--tRNA ligase | 0.659 |
DR97_266 | gor | DR97_266 | DR97_5822 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Pyridine nucleotide-disulfide oxidoreductase family protein; Maintains high levels of reduced glutathione in the cytosol | 0.836 |
DR97_266 | ileS | DR97_266 | DR97_1864 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Isoleucyl-trna synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) | 0.637 |
DR97_266 | katE | DR97_266 | DR97_6280 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Hydroperoxidase ii; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide | 0.710 |
DR97_266 | lysS | DR97_266 | DR97_4177 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Lysyl-trna synthetase, class ii; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.726 |
DR97_266 | metG | DR97_266 | DR97_4439 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Methionyl-trna synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation | 0.680 |
DR97_266 | proS | DR97_266 | DR97_981 | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | Prolyl-trna synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.701 |
Gpo | DR97_266 | DR97_5115 | DR97_266 | Glutathione peroxidase family protein; Belongs to the glutathione peroxidase family | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | 0.677 |
Gpo | gor | DR97_5115 | DR97_5822 | Glutathione peroxidase family protein; Belongs to the glutathione peroxidase family | Pyridine nucleotide-disulfide oxidoreductase family protein; Maintains high levels of reduced glutathione in the cytosol | 0.986 |
Gpo | katE | DR97_5115 | DR97_6280 | Glutathione peroxidase family protein; Belongs to the glutathione peroxidase family | Hydroperoxidase ii; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide | 0.933 |
argS | DR97_266 | DR97_2406 | DR97_266 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Gsh-dependent disulfide-bond oxidoreductase; Belongs to the GST superfamily | 0.659 |
argS | ileS | DR97_2406 | DR97_1864 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Isoleucyl-trna synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) | 0.997 |
argS | lysS | DR97_2406 | DR97_4177 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Lysyl-trna synthetase, class ii; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.994 |
argS | metG | DR97_2406 | DR97_4439 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Methionyl-trna synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation | 0.996 |
argS | proS | DR97_2406 | DR97_981 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Prolyl-trna synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.994 |