| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ank1 | azo0839 | azo1599 | azo0839 | 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 [...] | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.723 |
| 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 [...] | 0.918 |
| ank1 | gmk | azo1599 | azo3953 | 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 [...] | Guanylate kinase; Essential for recycling GMP and indirectly, cGMP. | 0.800 |
| ank1 | inaA | azo1599 | azo3161 | 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 InaA protein. Homology to inaA of P. putida of 39% (gnl|keqq|ppu:PP0904(KEGG)). Pfam: 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 is required for virulence in invasive strains of S. e [...] | 0.765 |
| ank1 | ndk | azo1599 | azo0923 | 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 [...] | Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.674 |
| azo0346 | azo2279 | azo0346 | azo2279 | Putative Na+/H+ antiporter; Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. | 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 [...] | 0.417 |
| azo0346 | azo3617 | azo0346 | azo3617 | Putative Na+/H+ antiporter; Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. | 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 [...] | 0.866 |
| azo0839 | ank1 | azo0839 | azo1599 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 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 [...] | 0.723 |
| azo0839 | azo2279 | azo0839 | azo2279 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 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 [...] | 0.737 |
| 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 [...] | 0.855 |
| azo0839 | azo3776 | azo0839 | azo3776 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 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. | 0.723 |
| azo0839 | gmk | azo0839 | azo3953 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Guanylate kinase; Essential for recycling GMP and indirectly, cGMP. | 0.819 |
| azo0839 | tnkS | azo0839 | azo2985 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 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 [...] | 0.723 |
| azo2279 | azo0346 | azo2279 | azo0346 | 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 [...] | Putative Na+/H+ antiporter; Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. | 0.417 |
| azo2279 | azo0839 | azo2279 | azo0839 | 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 [...] | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.737 |
| azo2279 | azo3617 | azo2279 | azo3617 | 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 [...] | 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 [...] | 0.919 |
| azo2279 | fkbP | azo2279 | azo3319 | 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 [...] | 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. | 0.468 |
| azo2279 | gmk | azo2279 | azo3953 | 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 [...] | Guanylate kinase; Essential for recycling GMP and indirectly, cGMP. | 0.835 |
| azo2279 | inaA | azo2279 | azo3161 | 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 [...] | Conserved hypothetical InaA protein. Homology to inaA of P. putida of 39% (gnl|keqq|ppu:PP0904(KEGG)). Pfam: 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 is required for virulence in invasive strains of S. e [...] | 0.765 |
| azo2279 | ndk | azo2279 | azo0923 | 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 [...] | Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.645 |