| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADV43255.1 | ADV43256.1 | Bache_1245 | Bache_1246 | Peptidase M23; COGs: COG0739 Membrane protein related to metalloendopeptidase; InterPro IPR016047; KEGG: bfs:BF0690 putative transmembrane peptidase; PFAM: Peptidase M23; SPTR: Putative uncharacterized protein; PFAM: Peptidase family M23. | Transcriptional regulator; InterPro IPR000551; KEGG: bfs:BF0691 putative transcriptional regulator protein; PFAM: regulatory protein MerR; SMART: regulatory protein MerR; SPTR: Putative uncharacterized protein. | 0.861 |
| ADV43255.1 | alaS | Bache_1245 | Bache_1244 | Peptidase M23; COGs: COG0739 Membrane protein related to metalloendopeptidase; InterPro IPR016047; KEGG: bfs:BF0690 putative transmembrane peptidase; PFAM: Peptidase M23; SPTR: Putative uncharacterized protein; PFAM: Peptidase family M23. | 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. | 0.700 |
| ADV43256.1 | ADV43255.1 | Bache_1246 | Bache_1245 | Transcriptional regulator; InterPro IPR000551; KEGG: bfs:BF0691 putative transcriptional regulator protein; PFAM: regulatory protein MerR; SMART: regulatory protein MerR; SPTR: Putative uncharacterized protein. | Peptidase M23; COGs: COG0739 Membrane protein related to metalloendopeptidase; InterPro IPR016047; KEGG: bfs:BF0690 putative transmembrane peptidase; PFAM: Peptidase M23; SPTR: Putative uncharacterized protein; PFAM: Peptidase family M23. | 0.861 |
| ADV43256.1 | alaS | Bache_1246 | Bache_1244 | Transcriptional regulator; InterPro IPR000551; KEGG: bfs:BF0691 putative transcriptional regulator protein; PFAM: regulatory protein MerR; SMART: regulatory protein MerR; SPTR: Putative uncharacterized protein. | 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. | 0.676 |
| alaS | ADV43255.1 | Bache_1244 | Bache_1245 | 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. | Peptidase M23; COGs: COG0739 Membrane protein related to metalloendopeptidase; InterPro IPR016047; KEGG: bfs:BF0690 putative transmembrane peptidase; PFAM: Peptidase M23; SPTR: Putative uncharacterized protein; PFAM: Peptidase family M23. | 0.700 |
| alaS | ADV43256.1 | Bache_1244 | Bache_1246 | 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. | Transcriptional regulator; InterPro IPR000551; KEGG: bfs:BF0691 putative transcriptional regulator protein; PFAM: regulatory protein MerR; SMART: regulatory protein MerR; SPTR: Putative uncharacterized protein. | 0.676 |
| alaS | gltX | Bache_1244 | Bache_1034 | 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. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.687 |
| alaS | ileS | Bache_1244 | Bache_2349 | 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. | Isoleucyl-tRNA synthetase; 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. | 0.701 |
| alaS | metG | Bache_1244 | Bache_0864 | 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. | 0.748 |
| alaS | pheT | Bache_1244 | Bache_2580 | 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. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: bfr:BF2565 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Putative uncharacterized protein; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial. | 0.758 |
| alaS | purL | Bache_1244 | Bache_3097 | 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. | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.702 |
| alaS | secD | Bache_1244 | Bache_0924 | 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. | Protein translocase subunit secF;protein translocase subunit secD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.730 |
| alaS | thrS | Bache_1244 | Bache_2836 | 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. | Ser-tRNA(Thr) hydrolase; 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). | 0.784 |
| alaS | valS | Bache_1244 | Bache_1526 | 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. | 0.691 |
| gltX | alaS | Bache_1034 | Bache_1244 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 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. | 0.687 |
| gltX | ileS | Bache_1034 | Bache_2349 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Isoleucyl-tRNA synthetase; 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. | 0.892 |
| gltX | metG | Bache_1034 | Bache_0864 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 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. | 0.886 |
| gltX | pheT | Bache_1034 | Bache_2580 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: bfr:BF2565 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Putative uncharacterized protein; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial. | 0.678 |
| gltX | thrS | Bache_1034 | Bache_2836 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Ser-tRNA(Thr) hydrolase; 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). | 0.685 |
| gltX | valS | Bache_1034 | Bache_1526 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 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. | 0.507 |