| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | azo2703 | azo2780 | azo2703 | 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 to magn028431 of M. magnetotacticum of 33% (ZP 00053827). Domain structur: 76 aa - 144 aa TPR; 201 aa - 316 aa TPR; 408 aa - 761 aa COG3914. InterPro: TPR repeat (IPR001440). no signal peptide no TMH. | 0.754 |
| 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 |
| alaS | azo3761 | azo2780 | azo3761 | 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 to ebD78 of Azoarcus sp. EbN1 of 40% (gnl|keqq|eba:ebD78(KEGG)). no domains predicted. no signal peptide. no TMHs. | 0.829 |
| alaS | azo3763 | azo2780 | azo3763 | 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. | Hypothetical protein predicted by Glimmer/Critica; Hypothetical protein. no homology to the data bank no domains no signal peptide no TMHs. | 0.829 |
| alaS | dnaJ1 | azo2780 | azo1062 | 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. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.559 |
| azo0358 | azo3617 | azo0358 | azo3617 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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 [...] | 0.694 |
| azo0358 | azo3761 | azo0358 | azo3761 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical protein. Homology to ebD78 of Azoarcus sp. EbN1 of 40% (gnl|keqq|eba:ebD78(KEGG)). no domains predicted. no signal peptide. no TMHs. | 0.882 |
| azo0358 | azo3763 | azo0358 | azo3763 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Hypothetical protein predicted by Glimmer/Critica; Hypothetical protein. no homology to the data bank no domains no signal peptide no TMHs. | 0.882 |
| azo0358 | dnaJ1 | azo0358 | azo1062 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.961 |
| azo0358 | fkbP | azo0358 | azo3319 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.866 |
| 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 |
| azo1211 | azo2703 | azo1211 | azo2703 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Conserved hypothetical protein. Homology to magn028431 of M. magnetotacticum of 33% (ZP 00053827). Domain structur: 76 aa - 144 aa TPR; 201 aa - 316 aa TPR; 408 aa - 761 aa COG3914. InterPro: TPR repeat (IPR001440). no signal peptide no TMH. | 0.743 |
| azo1211 | azo3617 | azo1211 | azo3617 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 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 [...] | 0.945 |
| azo1211 | azo3761 | azo1211 | azo3761 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Conserved hypothetical protein. Homology to ebD78 of Azoarcus sp. EbN1 of 40% (gnl|keqq|eba:ebD78(KEGG)). no domains predicted. no signal peptide. no TMHs. | 0.849 |
| azo1211 | azo3763 | azo1211 | azo3763 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Hypothetical protein predicted by Glimmer/Critica; Hypothetical protein. no homology to the data bank no domains no signal peptide no TMHs. | 0.849 |
| azo1211 | dnaJ1 | azo1211 | azo1062 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.857 |
| azo1211 | fkbP | azo1211 | azo3319 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.480 |
| azo2703 | alaS | azo2703 | azo2780 | Conserved hypothetical protein. Homology to magn028431 of M. magnetotacticum of 33% (ZP 00053827). Domain structur: 76 aa - 144 aa TPR; 201 aa - 316 aa TPR; 408 aa - 761 aa COG3914. InterPro: TPR repeat (IPR001440). no signal peptide no TMH. | 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. | 0.754 |
| azo2703 | azo1211 | azo2703 | azo1211 | Conserved hypothetical protein. Homology to magn028431 of M. magnetotacticum of 33% (ZP 00053827). Domain structur: 76 aa - 144 aa TPR; 201 aa - 316 aa TPR; 408 aa - 761 aa COG3914. InterPro: TPR repeat (IPR001440). no signal peptide no TMH. | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.743 |