| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDR47433.1 | EDR47435.1 | DORFOR_01399 | DORFOR_01401 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Arylsulfatase; KEGG: aha:AHA_2572 8.8e-07 sulfatase; COG: COG1368 Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily; Psort location: CytoplasmicMembrane, score: 9.26. | 0.857 |
| EDR47433.1 | folC | DORFOR_01399 | DORFOR_01400 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Bifunctional protein FolC; KEGG: bcz:BCZK4201 1.1e-59 folC; folylpolyglutamate synthase K01930; COG: COG0285 Folylpolyglutamate synthase; Psort location: Cytoplasmic, score: 8.87. | 0.812 |
| EDR47433.1 | valS | DORFOR_01399 | DORFOR_01402 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | valine--tRNA ligase; 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. | 0.756 |
| EDR47435.1 | EDR47433.1 | DORFOR_01401 | DORFOR_01399 | Arylsulfatase; KEGG: aha:AHA_2572 8.8e-07 sulfatase; COG: COG1368 Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily; Psort location: CytoplasmicMembrane, score: 9.26. | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 0.857 |
| EDR47435.1 | folC | DORFOR_01401 | DORFOR_01400 | Arylsulfatase; KEGG: aha:AHA_2572 8.8e-07 sulfatase; COG: COG1368 Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily; Psort location: CytoplasmicMembrane, score: 9.26. | Bifunctional protein FolC; KEGG: bcz:BCZK4201 1.1e-59 folC; folylpolyglutamate synthase K01930; COG: COG0285 Folylpolyglutamate synthase; Psort location: Cytoplasmic, score: 8.87. | 0.779 |
| EDR47435.1 | valS | DORFOR_01401 | DORFOR_01402 | Arylsulfatase; KEGG: aha:AHA_2572 8.8e-07 sulfatase; COG: COG1368 Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily; Psort location: CytoplasmicMembrane, score: 9.26. | valine--tRNA ligase; 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. | 0.754 |
| alaS | aspS-2 | DORFOR_00092 | DORFOR_00844 | 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. | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.586 |
| alaS | guaA | DORFOR_00092 | DORFOR_01859 | 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) domain protein; Catalyzes the synthesis of GMP from XMP. | 0.518 |
| alaS | ileS | DORFOR_00092 | DORFOR_02764 | 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 2 subfamily. | 0.700 |
| alaS | leuS | DORFOR_00092 | DORFOR_02266 | 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. | leucine--tRNA ligase; KEGG: bld:BLi03175 1.4e-237 leuS; leucyl-tRNA synthetase; RBL03411 K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score: 9.98; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.715 |
| alaS | pheT | DORFOR_00092 | DORFOR_02847 | 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. | KEGG: tte:TTE1688 1.9e-107 pheT; phenylalanyl-tRNA synthetase beta subunit K01890; COG: COG0073 EMAP domain; Psort location: Cytoplasmic, score: 9.98. | 0.767 |
| alaS | thrS | DORFOR_00092 | DORFOR_01734 | 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. | threonine--tRNA ligase; 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). | 0.734 |
| alaS | valS | DORFOR_00092 | DORFOR_01402 | 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. | valine--tRNA ligase; 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. | 0.727 |
| aspS-2 | alaS | DORFOR_00844 | DORFOR_00092 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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. | 0.586 |
| aspS-2 | guaA | DORFOR_00844 | DORFOR_01859 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GMP synthase (glutamine-hydrolyzing) domain protein; Catalyzes the synthesis of GMP from XMP. | 0.866 |
| aspS-2 | ileS | DORFOR_00844 | DORFOR_02764 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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 2 subfamily. | 0.615 |
| aspS-2 | leuS | DORFOR_00844 | DORFOR_02266 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | leucine--tRNA ligase; KEGG: bld:BLi03175 1.4e-237 leuS; leucyl-tRNA synthetase; RBL03411 K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score: 9.98; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.675 |
| aspS-2 | pheT | DORFOR_00844 | DORFOR_02847 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | KEGG: tte:TTE1688 1.9e-107 pheT; phenylalanyl-tRNA synthetase beta subunit K01890; COG: COG0073 EMAP domain; Psort location: Cytoplasmic, score: 9.98. | 0.709 |
| aspS-2 | thrS | DORFOR_00844 | DORFOR_01734 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | threonine--tRNA ligase; 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). | 0.511 |
| aspS-2 | valS | DORFOR_00844 | DORFOR_01402 | aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | valine--tRNA ligase; 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. | 0.843 |