| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ06968.1 | leuS | SKA53_01191 | SKA53_12508 | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | COG0495 Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.528 |
| EAQ06968.1 | pheT-2 | SKA53_01191 | SKA53_10114 | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | phenylalanyl-tRNA synthetase, beta subunit; COG0073 EMAP domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.675 |
| EAQ06968.1 | rplT | SKA53_01191 | SKA53_10219 | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 50S ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | 0.946 |
| EAQ06968.1 | rpoC | SKA53_01191 | SKA53_13278 | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | DNA-directed RNA polymerase beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.998 |
| EAQ06968.1 | thrS | SKA53_01191 | SKA53_07606 | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). | 0.807 |
| EAQ06968.1 | valS | SKA53_01191 | SKA53_15306 | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.684 |
| alaS | hisS | SKA53_03344 | SKA53_08889 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COG0124 Histidyl-tRNA synthetase. | 0.730 |
| alaS | leuS | SKA53_03344 | SKA53_12508 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COG0495 Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.884 |
| alaS | metG | SKA53_03344 | SKA53_01331 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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. | 0.747 |
| alaS | pheT-2 | SKA53_03344 | SKA53_10114 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | phenylalanyl-tRNA synthetase, beta subunit; COG0073 EMAP domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.908 |
| alaS | rpoC | SKA53_03344 | SKA53_13278 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | DNA-directed RNA polymerase beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.665 |
| alaS | thrS | SKA53_03344 | SKA53_07606 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). | 0.852 |
| alaS | valS | SKA53_03344 | SKA53_15306 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.931 |
| hisS | alaS | SKA53_08889 | SKA53_03344 | COG0124 Histidyl-tRNA synthetase. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.730 |
| hisS | leuS | SKA53_08889 | SKA53_12508 | COG0124 Histidyl-tRNA synthetase. | COG0495 Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.737 |
| hisS | metG | SKA53_08889 | SKA53_01331 | COG0124 Histidyl-tRNA synthetase. | 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. | 0.817 |
| hisS | pheT-2 | SKA53_08889 | SKA53_10114 | COG0124 Histidyl-tRNA synthetase. | phenylalanyl-tRNA synthetase, beta subunit; COG0073 EMAP domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.682 |
| hisS | rpoC | SKA53_08889 | SKA53_13278 | COG0124 Histidyl-tRNA synthetase. | DNA-directed RNA polymerase beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.512 |
| hisS | thrS | SKA53_08889 | SKA53_07606 | COG0124 Histidyl-tRNA synthetase. | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). | 0.826 |
| hisS | valS | SKA53_08889 | SKA53_15306 | COG0124 Histidyl-tRNA synthetase. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.761 |