| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | aspS | HI_0814 | HI_0317 | alanyl-tRNA synthetase (alaS); 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. | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.535 |
| alaS | glyQ | HI_0814 | HI_0927 | alanyl-tRNA synthetase (alaS); 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. | glycyl-tRNA synthetase, alpha chain (glyQ); Similar to SP:P00960 GB:J01622 PID:146222 PID:146225 PID:466698 percent identity: 90.64; identified by sequence similarity; putative. | 0.620 |
| alaS | glyS | HI_0814 | HI_0924 | alanyl-tRNA synthetase (alaS); 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. | glycyl-tRNA synthetase, beta chain (glyS); Similar to SP:P00961 GB:J01622 PID:146223 PID:466697 GB:U00096 percent identity: 69.67; identified by sequence similarity; putative. | 0.607 |
| alaS | leuS | HI_0814 | HI_0921 | alanyl-tRNA synthetase (alaS); 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. | leucyl-tRNA synthetase (leuS); Similar to SP:P07813 GB:X06331 PID:41916 GB:U00096 PID:1651269 percent identity: 72.64; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.811 |
| alaS | pheT | HI_0814 | HI_1312 | alanyl-tRNA synthetase (alaS); 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 (pheT); Similar to GB:K02844 SP:P07395 PID:146346 PID:43071 GB:U00096 percent identity: 65.28; identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.804 |
| alaS | valS | HI_0814 | HI_1391 | alanyl-tRNA synthetase (alaS); 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 (valS); 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. | 0.847 |
| aspS | alaS | HI_0317 | HI_0814 | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | alanyl-tRNA synthetase (alaS); 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. | 0.535 |
| aspS | glyQ | HI_0317 | HI_0927 | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glycyl-tRNA synthetase, alpha chain (glyQ); Similar to SP:P00960 GB:J01622 PID:146222 PID:146225 PID:466698 percent identity: 90.64; identified by sequence similarity; putative. | 0.479 |
| aspS | glyS | HI_0317 | HI_0924 | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glycyl-tRNA synthetase, beta chain (glyS); Similar to SP:P00961 GB:J01622 PID:146223 PID:466697 GB:U00096 percent identity: 69.67; identified by sequence similarity; putative. | 0.551 |
| aspS | leuS | HI_0317 | HI_0921 | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | leucyl-tRNA synthetase (leuS); Similar to SP:P07813 GB:X06331 PID:41916 GB:U00096 PID:1651269 percent identity: 72.64; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.634 |
| aspS | pheT | HI_0317 | HI_1312 | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | phenylalanyl-tRNA synthetase, beta subunit (pheT); Similar to GB:K02844 SP:P07395 PID:146346 PID:43071 GB:U00096 percent identity: 65.28; identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.734 |
| aspS | valS | HI_0317 | HI_1391 | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | valyl-tRNA synthetase (valS); 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. | 0.767 |
| dnaB | glyS | HI_1574 | HI_0924 | Replicative DNA helicase (dnaB); Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. | glycyl-tRNA synthetase, beta chain (glyS); Similar to SP:P00961 GB:J01622 PID:146223 PID:466697 GB:U00096 percent identity: 69.67; identified by sequence similarity; putative. | 0.519 |
| dnaB | pheT | HI_1574 | HI_1312 | Replicative DNA helicase (dnaB); Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. | phenylalanyl-tRNA synthetase, beta subunit (pheT); Similar to GB:K02844 SP:P07395 PID:146346 PID:43071 GB:U00096 percent identity: 65.28; identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.473 |
| efp | glyS | HI_0328 | HI_0924 | Elongation factor P (efp); Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | glycyl-tRNA synthetase, beta chain (glyS); Similar to SP:P00961 GB:J01622 PID:146223 PID:466697 GB:U00096 percent identity: 69.67; identified by sequence similarity; putative. | 0.555 |
| efp | mutY | HI_0328 | HI_0759 | Elongation factor P (efp); Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | A/G-specific adenine glycosylase (mutY); Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo- dGTP); Belongs to the Nth/MutY family. | 0.531 |
| efp | pheT | HI_0328 | HI_1312 | Elongation factor P (efp); Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | phenylalanyl-tRNA synthetase, beta subunit (pheT); Similar to GB:K02844 SP:P07395 PID:146346 PID:43071 GB:U00096 percent identity: 65.28; identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.635 |
| efp | ppa | HI_0328 | HI_0124 | Elongation factor P (efp); Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | Inorganic pyrophosphatase (ppa); Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. | 0.865 |
| glyQ | alaS | HI_0927 | HI_0814 | glycyl-tRNA synthetase, alpha chain (glyQ); Similar to SP:P00960 GB:J01622 PID:146222 PID:146225 PID:466698 percent identity: 90.64; identified by sequence similarity; putative. | alanyl-tRNA synthetase (alaS); 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. | 0.620 |
| glyQ | aspS | HI_0927 | HI_0317 | glycyl-tRNA synthetase, alpha chain (glyQ); Similar to SP:P00960 GB:J01622 PID:146222 PID:146225 PID:466698 percent identity: 90.64; identified by sequence similarity; putative. | aspartyl-tRNA synthetase (aspS); Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.479 |