| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | azo3626 | azo0358 | azo3626 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | 0.973 |
| azo0358 | azo3907 | azo0358 | azo3907 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical protein. Homology to xac4125 of X. axonopodis of 42% (trembl|Q8PF60). Domain structure: 5 x TRP, 50 aa - 83 aa; 84 aa - 117 aa; 118 aa - 151 aa; 152 aa - 182 aa; 186 aa - 219 aa. InterPro: TPR repeat (IPR001440); SAM (and some other nucleotide) binding motif (IPR000051). Pfam: TPR daomian. no signal peptide. no TMHs. | 0.883 |
| azo0358 | dnaK | azo0358 | azo1063 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.973 |
| 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 |
| azo0358 | hscA | azo0358 | azo2012 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.973 |
| azo0358 | oma | azo0358 | azo1901 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Outer membrane protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.731 |
| azo3617 | azo0358 | azo3617 | azo0358 | 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 [...] | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.694 |
| azo3617 | azo3626 | azo3617 | azo3626 | 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 [...] | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | 0.888 |
| azo3617 | azo3907 | azo3617 | azo3907 | 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 [...] | Conserved hypothetical protein. Homology to xac4125 of X. axonopodis of 42% (trembl|Q8PF60). Domain structure: 5 x TRP, 50 aa - 83 aa; 84 aa - 117 aa; 118 aa - 151 aa; 152 aa - 182 aa; 186 aa - 219 aa. InterPro: TPR repeat (IPR001440); SAM (and some other nucleotide) binding motif (IPR000051). Pfam: TPR daomian. no signal peptide. no TMHs. | 0.835 |
| azo3617 | dnaK | azo3617 | azo1063 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.837 |
| azo3617 | fkbP | azo3617 | azo3319 | 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 [...] | 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. | 0.914 |
| azo3617 | hscA | azo3617 | azo2012 | 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 [...] | Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.837 |
| azo3617 | htpG | azo3617 | azo1425 | 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 [...] | Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity. | 0.520 |
| azo3626 | azo0358 | azo3626 | azo0358 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.973 |
| azo3626 | azo3617 | azo3626 | azo3617 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; 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 [...] | 0.888 |
| azo3626 | azo3907 | azo3626 | azo3907 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Conserved hypothetical protein. Homology to xac4125 of X. axonopodis of 42% (trembl|Q8PF60). Domain structure: 5 x TRP, 50 aa - 83 aa; 84 aa - 117 aa; 118 aa - 151 aa; 152 aa - 182 aa; 186 aa - 219 aa. InterPro: TPR repeat (IPR001440); SAM (and some other nucleotide) binding motif (IPR000051). Pfam: TPR daomian. no signal peptide. no TMHs. | 0.779 |
| azo3626 | fkbP | azo3626 | azo3319 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | 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. | 0.812 |
| azo3626 | htpG | azo3626 | azo1425 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity. | 0.964 |
| azo3626 | oma | azo3626 | azo1901 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Outer membrane protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.687 |