| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ank1 | azo0358 | azo1599 | azo0358 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.761 |
| ank1 | azo1211 | azo1599 | azo1211 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.896 |
| ank1 | azo3573 | azo1599 | azo3573 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Conserved hypothetical protein, 43% identity(65% similarity) to TrEMBL|Q9HUG7,Hypothetical protein PA4998 [PA4998] [Pseudomonas aeruginosa]. Has PF06293:IPR010440:Lipopolysaccharide kinase (Kdo/WaaP) family;These lipopolysaccharide kinases are related to protein kinases Pkinase. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it [...] | 0.795 |
| ank1 | azo3617 | azo1599 | azo3617 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 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 [...] | 0.898 |
| ank1 | azo3626 | azo1599 | azo3626 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 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. | 0.598 |
| ank1 | dnaK | azo1599 | azo1063 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.598 |
| ank1 | hscA | azo1599 | azo2012 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 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. | 0.598 |
| azo0358 | ank1 | azo0358 | azo1599 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.761 |
| 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 | azo3573 | azo0358 | azo3573 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical protein, 43% identity(65% similarity) to TrEMBL|Q9HUG7,Hypothetical protein PA4998 [PA4998] [Pseudomonas aeruginosa]. Has PF06293:IPR010440:Lipopolysaccharide kinase (Kdo/WaaP) family;These lipopolysaccharide kinases are related to protein kinases Pkinase. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it [...] | 0.869 |
| 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 | azo3776 | azo0358 | azo3776 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Conserved hypothetical membrane protein. Homology to ebA2790 of Azoarcus sp. EbN1 of 31% (gnl|keqq|eba:ebA2790(KEGG)). No domains predicted. no signal peptide. 2 TMHS; Conserved hypothetical protein. | 0.761 |
| 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 | 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 | tnkS | azo0358 | azo2985 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Putative tankyrase type protein; Tankyrase 2 (EC 2.4.2.30) (TANK2) (Tankyrase II) (TNKS-2) (TRF1- interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase-like protein) (Tankyrase-related protein). May regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Has PARP activity and can modify TRF1 and thereby contribute to the regulation of telomere length. TREMBL:Q800E0:34%; Q8YTG9:36% identity. InterPro: Ankyrin-repeat Mop: molybdenum-pterin binding domain Presence of signal peptide (SignalP) but absence of transmembrane helices; Function [...] | 0.761 |
| azo1211 | ank1 | azo1211 | azo1599 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.896 |
| azo1211 | azo2279 | azo1211 | azo2279 | 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 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 [...] | 0.899 |
| azo1211 | azo3573 | azo1211 | azo3573 | 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, 43% identity(65% similarity) to TrEMBL|Q9HUG7,Hypothetical protein PA4998 [PA4998] [Pseudomonas aeruginosa]. Has PF06293:IPR010440:Lipopolysaccharide kinase (Kdo/WaaP) family;These lipopolysaccharide kinases are related to protein kinases Pkinase. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it [...] | 0.897 |
| 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 |