| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS1 | alaS2 | Cphy_2617 | Cphy_0956 | 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. | 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 (By similarity). | 0.905 |
| alaS1 | hisI | Cphy_2617 | Cphy_2782 | 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. | TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: cth:Cthe_2889 phosphoribosyl-AMP cyclohydrolase; In the C-terminal section; belongs to the PRA-PH family. | 0.515 |
| alaS1 | leuS | Cphy_2617 | Cphy_0938 | 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. | TIGRFAM: leucyl-tRNA synthetase; KEGG: gka:GK2842 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.681 |
| alaS1 | metG | Cphy_2617 | Cphy_0025 | 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. | 0.831 |
| alaS1 | pheT | Cphy_2617 | Cphy_3476 | 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. | KEGG: cth:Cthe_0215 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.832 |
| alaS1 | thrS | Cphy_2617 | Cphy_0748 | 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. | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); TGS domain protein; Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: cbe:Cbei_0293 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.618 |
| alaS1 | thrS-2 | Cphy_2617 | Cphy_2665 | 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. | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: ctc:CTC02286 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.729 |
| alaS1 | valS | Cphy_2617 | Cphy_0472 | 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. | 0.737 |
| alaS2 | alaS1 | Cphy_0956 | Cphy_2617 | 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 (By similarity). | 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. | 0.905 |
| alaS2 | hisI | Cphy_0956 | Cphy_2782 | 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 (By similarity). | TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: cth:Cthe_2889 phosphoribosyl-AMP cyclohydrolase; In the C-terminal section; belongs to the PRA-PH family. | 0.515 |
| alaS2 | leuS | Cphy_0956 | Cphy_0938 | 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 (By similarity). | TIGRFAM: leucyl-tRNA synthetase; KEGG: gka:GK2842 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.733 |
| alaS2 | metG | Cphy_0956 | Cphy_0025 | 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 (By similarity). | 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. | 0.808 |
| alaS2 | pheT | Cphy_0956 | Cphy_3476 | 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 (By similarity). | KEGG: cth:Cthe_0215 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.800 |
| alaS2 | thrS | Cphy_0956 | Cphy_0748 | 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 (By similarity). | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); TGS domain protein; Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: cbe:Cbei_0293 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.757 |
| alaS2 | thrS-2 | Cphy_0956 | Cphy_2665 | 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 (By similarity). | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: ctc:CTC02286 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.794 |
| alaS2 | valS | Cphy_0956 | Cphy_0472 | 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 (By similarity). | 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. | 0.764 |
| hisI | alaS1 | Cphy_2782 | Cphy_2617 | TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: cth:Cthe_2889 phosphoribosyl-AMP cyclohydrolase; In the C-terminal section; belongs to the PRA-PH family. | 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. | 0.515 |
| hisI | alaS2 | Cphy_2782 | Cphy_0956 | TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: cth:Cthe_2889 phosphoribosyl-AMP cyclohydrolase; In the C-terminal section; belongs to the PRA-PH family. | 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 (By similarity). | 0.515 |
| hisI | leuS | Cphy_2782 | Cphy_0938 | TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: cth:Cthe_2889 phosphoribosyl-AMP cyclohydrolase; In the C-terminal section; belongs to the PRA-PH family. | TIGRFAM: leucyl-tRNA synthetase; KEGG: gka:GK2842 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.546 |
| hisI | metG | Cphy_2782 | Cphy_0025 | TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: cth:Cthe_2889 phosphoribosyl-AMP cyclohydrolase; In the C-terminal section; belongs to the PRA-PH family. | 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. | 0.742 |