| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | glyQ | SBG_2447 | SBG_3250 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | glycine-tRNA synthetase, alpha subunit. | 0.644 |
| alaS | glyS | SBG_2447 | SBG_3249 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | glycine-tRNA synthetase, beta subunit. | 0.618 |
| alaS | guaA | SBG_2447 | SBG_2288 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.582 |
| alaS | hisS | SBG_2447 | SBG_2298 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | histidyl-tRNA synthetase. | 0.704 |
| alaS | ileS | SBG_2447 | SBG_0044 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | isoleucyl-tRNA synthetase. | 0.743 |
| alaS | metG | SBG_2447 | SBG_1968 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.860 |
| alaS | pheS | SBG_2447 | SBG_1189 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | phenylalanyl-tRNA synthetase alpha chain. | 0.544 |
| alaS | pheT | SBG_2447 | SBG_1190 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | phenylalanyl-tRNA synthetase beta chain. | 0.878 |
| alaS | trmD | SBG_2447 | SBG_2390 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | tRNA(guanine-N1)methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. | 0.418 |
| atpH | glyQ | SBG_3420 | SBG_3250 | ATP synthase delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | glycine-tRNA synthetase, alpha subunit. | 0.576 |
| atpH | pheT | SBG_3420 | SBG_1190 | ATP synthase delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | phenylalanyl-tRNA synthetase beta chain. | 0.450 |
| atpH | trmD | SBG_3420 | SBG_2390 | ATP synthase delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | tRNA(guanine-N1)methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. | 0.891 |
| glyQ | alaS | SBG_3250 | SBG_2447 | glycine-tRNA synthetase, alpha subunit. | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.644 |
| glyQ | atpH | SBG_3250 | SBG_3420 | glycine-tRNA synthetase, alpha subunit. | ATP synthase delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.576 |
| glyQ | glyS | SBG_3250 | SBG_3249 | glycine-tRNA synthetase, alpha subunit. | glycine-tRNA synthetase, beta subunit. | 0.999 |
| glyQ | guaA | SBG_3250 | SBG_2288 | glycine-tRNA synthetase, alpha subunit. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.618 |
| glyQ | hisS | SBG_3250 | SBG_2298 | glycine-tRNA synthetase, alpha subunit. | histidyl-tRNA synthetase. | 0.754 |
| glyQ | ileS | SBG_3250 | SBG_0044 | glycine-tRNA synthetase, alpha subunit. | isoleucyl-tRNA synthetase. | 0.595 |
| glyQ | metG | SBG_3250 | SBG_1968 | glycine-tRNA synthetase, alpha subunit. | methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.659 |
| glyQ | pheS | SBG_3250 | SBG_1189 | glycine-tRNA synthetase, alpha subunit. | phenylalanyl-tRNA synthetase alpha chain. | 0.652 |