| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ARB04094.1 | glyQ | B2G52_03620 | B2G52_03615 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.559 |
| ARB04094.1 | glyS | B2G52_03620 | B2G52_03625 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | glycine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.709 |
| alaS | glyQ | B2G52_10260 | B2G52_03615 | alanine--tRNA ligase; 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. | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.628 |
| alaS | glyS | B2G52_10260 | B2G52_03625 | alanine--tRNA ligase; 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. | glycine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.574 |
| alaS | guaA | B2G52_10260 | B2G52_03685 | alanine--tRNA ligase; 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. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.681 |
| alaS | hisS | B2G52_10260 | B2G52_06300 | alanine--tRNA ligase; 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. | histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.660 |
| alaS | ileS | B2G52_10260 | B2G52_04160 | alanine--tRNA ligase; 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. | isoleucine--tRNA ligase; 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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.763 |
| alaS | metG | B2G52_10260 | B2G52_02450 | alanine--tRNA ligase; 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. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.892 |
| alaS | pheT | B2G52_10260 | B2G52_05620 | alanine--tRNA ligase; 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. | phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.896 |
| atpH | glyQ | B2G52_03585 | B2G52_03615 | F0F1 ATP synthase subunit delta; 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. | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.668 |
| atpH | glyS | B2G52_03585 | B2G52_03625 | F0F1 ATP synthase subunit delta; 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 ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.482 |
| atpH | pheT | B2G52_03585 | B2G52_05620 | F0F1 ATP synthase subunit delta; 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. | phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.520 |
| glyQ | ARB04094.1 | B2G52_03615 | B2G52_03620 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.559 |
| glyQ | alaS | B2G52_03615 | B2G52_10260 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | alanine--tRNA ligase; 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. | 0.628 |
| glyQ | atpH | B2G52_03615 | B2G52_03585 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit delta; 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. | 0.668 |
| glyQ | glyS | B2G52_03615 | B2G52_03625 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | glycine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| glyQ | guaA | B2G52_03615 | B2G52_03685 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.616 |
| glyQ | hisS | B2G52_03615 | B2G52_06300 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.718 |
| glyQ | ileS | B2G52_03615 | B2G52_04160 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | isoleucine--tRNA ligase; 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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.510 |
| glyQ | metG | B2G52_03615 | B2G52_02450 | Glycosyl transferase family 1; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.648 |