| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | azo0839 | azo2780 | azo0839 | AlaS protein; 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. | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.799 |
| alaS | azo1211 | azo2780 | azo1211 | AlaS protein; 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. | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.950 |
| alaS | azo3617 | azo2780 | azo3617 | AlaS protein; 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. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.624 |
| azo0839 | alaS | azo0839 | azo2780 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | AlaS protein; 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. | 0.799 |
| azo0839 | azo1095 | azo0839 | azo1095 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | 0.925 |
| azo0839 | azo1211 | azo0839 | azo1211 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.925 |
| azo0839 | azo1601 | azo0839 | azo1601 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Histone deacetylases catalyse the removal of the acetyl group from histones. Histone deacetylase, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient family, TREMBL:Q7NVL6 (58% identity); TREMBL:Q8XZ00 (57% identity). InterPro (IPR000286): Histone deacetylase superfamily Pfam (PF00850): Histone deacetylase domain; Family membership. | 0.925 |
| azo0839 | azo2638 | azo0839 | azo2638 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Conserved hypothetical ATPase. Homology to rsc1961 of R. solanacearum of 37% (trembl|Q8XY02). Pfam: Atpase familly associated with various cellular activities (domaine 1 from 300 aa to 499 aa, domaine 2 from 543 to 723 aa). no signal peptide. no TMHs; Conserved hypothetical protein. | 0.531 |
| azo0839 | azo3617 | azo0839 | azo3617 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.751 |
| azo0839 | azo3791 | azo0839 | azo3791 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Conserved hypothetical ATPase. Homology to MCA0262 of Methylococcus capsulatus of 68% (gi|53756248|gb|AAU90539.1|(NBCI ENTREZ)). InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959);AAA ATPase superfamily (IPR003593) Pfam: ATPase family associated with various cellular activities (domaine from 365 aa to 540 aa) no signal peptide. no TMHs; Function unclear. | 0.531 |
| azo0839 | ppiA | azo0839 | azo1057 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.562 |
| azo0839 | ppiB | azo0839 | azo1056 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.562 |
| azo1095 | azo0839 | azo1095 | azo0839 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.925 |
| azo1095 | azo1211 | azo1095 | azo1211 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.927 |
| azo1095 | azo2638 | azo1095 | azo2638 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | Conserved hypothetical ATPase. Homology to rsc1961 of R. solanacearum of 37% (trembl|Q8XY02). Pfam: Atpase familly associated with various cellular activities (domaine 1 from 300 aa to 499 aa, domaine 2 from 543 to 723 aa). no signal peptide. no TMHs; Conserved hypothetical protein. | 0.897 |
| azo1095 | azo3617 | azo1095 | azo3617 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.827 |
| azo1095 | azo3791 | azo1095 | azo3791 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | Conserved hypothetical ATPase. Homology to MCA0262 of Methylococcus capsulatus of 68% (gi|53756248|gb|AAU90539.1|(NBCI ENTREZ)). InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959);AAA ATPase superfamily (IPR003593) Pfam: ATPase family associated with various cellular activities (domaine from 365 aa to 540 aa) no signal peptide. no TMHs; Function unclear. | 0.897 |
| azo1095 | ppiA | azo1095 | azo1057 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.896 |
| azo1095 | ppiB | azo1095 | azo1056 | Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.896 |
| azo1211 | alaS | azo1211 | azo2780 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | AlaS protein; 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. | 0.950 |