| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | azo1113 | azo2780 | azo1113 | 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 Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 0.829 |
| 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 | azo2279 | azo2780 | azo2279 | 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 Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.843 |
| 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 | 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 | azo1113 | azo0358 | azo1113 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 0.882 |
| azo0358 | azo2279 | azo0358 | azo2279 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.823 |
| 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 | azo3791 | azo0358 | azo3791 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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. | 0.818 |
| 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 |
| azo1113 | alaS | azo1113 | azo2780 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 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. | 0.829 |
| azo1113 | azo0358 | azo1113 | azo0358 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.882 |
| azo1113 | azo1211 | azo1113 | azo1211 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.849 |
| azo1113 | azo2279 | azo1113 | azo2279 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.907 |
| azo1113 | azo2703 | azo1113 | azo2703 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 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. | 0.808 |
| azo1113 | azo3617 | azo1113 | azo3617 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 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 [...] | 0.835 |
| azo1113 | azo3791 | azo1113 | azo3791 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 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. | 0.892 |
| azo1113 | dnaJ1 | azo1113 | azo1062 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 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 [...] | 0.782 |
