| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | azo2643 | azo1599 | azo2643 | 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 dual specificity protein phosphatase,; Function unclear. | 0.827 |
| 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 | npd1 | azo1599 | azo0237 | 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 NAD-dependent deacetylase (EC 3.5.1.-) (Regulatory protein SIR2 homolog). Modulates the activities of several enzymes which are inactive in their acetylated form. Similar to SWISSPROT: sprot|NPD_AERPE (27% Aeropyrum pernix, NpdA or aq_2170) Pfam: PF02146 Sir2 family; High confidence in function and specificity. | 0.613 |
| ank1 | npd2 | azo1599 | azo3660 | 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 [...] | NAD-dependent deacetylase 2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2). Modulates the activities of several enzymes which are inactive in their acetylated form. Similar to SWISSPROT: sprot|NPD2_PSEAE (50% Pseudomonas aeruginosa, Npd2) / sprot|NPD1_ARCFU (33% Archaeoglobus fulgidus, NpdA) InterPro: IPR003000 SIR2. Pfam: PF02146 Sir2 family; High confidence in function and specificity. | 0.613 |
| azo1032 | azo2279 | azo1032 | azo2279 | Conserved hypothetical protein; TREMBL:Q8XZ43; 52% identity, 70% similarity. TREMBL:Q8F5Y8; 30% identity, 56% similarity. Protein At5g10860 mitochondrial precursor. IPR000644: CBS domain Pfam:PF00571 - GARS_N TIGRFAM: rrf2 family, KpsF/GutQ family (by similarity) kpsF: KpsF/GutQ family protein; 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 [...] | 0.679 |
| azo1032 | azo2643 | azo1032 | azo2643 | Conserved hypothetical protein; TREMBL:Q8XZ43; 52% identity, 70% similarity. TREMBL:Q8F5Y8; 30% identity, 56% similarity. Protein At5g10860 mitochondrial precursor. IPR000644: CBS domain Pfam:PF00571 - GARS_N TIGRFAM: rrf2 family, KpsF/GutQ family (by similarity) kpsF: KpsF/GutQ family protein; Specificity unclear. | Putative dual specificity protein phosphatase,; Function unclear. | 0.692 |
| 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 | azo2643 | azo1211 | azo2643 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Putative dual specificity protein phosphatase,; Function unclear. | 0.840 |
| 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 | azo3776 | azo1211 | azo3776 | 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 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. | 0.896 |
| azo1211 | npd1 | azo1211 | azo0237 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Putative NAD-dependent deacetylase (EC 3.5.1.-) (Regulatory protein SIR2 homolog). Modulates the activities of several enzymes which are inactive in their acetylated form. Similar to SWISSPROT: sprot|NPD_AERPE (27% Aeropyrum pernix, NpdA or aq_2170) Pfam: PF02146 Sir2 family; High confidence in function and specificity. | 0.865 |
| azo1211 | npd2 | azo1211 | azo3660 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | NAD-dependent deacetylase 2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2). Modulates the activities of several enzymes which are inactive in their acetylated form. Similar to SWISSPROT: sprot|NPD2_PSEAE (50% Pseudomonas aeruginosa, Npd2) / sprot|NPD1_ARCFU (33% Archaeoglobus fulgidus, NpdA) InterPro: IPR003000 SIR2. Pfam: PF02146 Sir2 family; High confidence in function and specificity. | 0.865 |
| azo1211 | tnkS | azo1211 | azo2985 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 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 [...] | 0.896 |
| azo2279 | azo1032 | azo2279 | azo1032 | 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 protein; TREMBL:Q8XZ43; 52% identity, 70% similarity. TREMBL:Q8F5Y8; 30% identity, 56% similarity. Protein At5g10860 mitochondrial precursor. IPR000644: CBS domain Pfam:PF00571 - GARS_N TIGRFAM: rrf2 family, KpsF/GutQ family (by similarity) kpsF: KpsF/GutQ family protein; Specificity unclear. | 0.679 |
| azo2279 | azo1211 | azo2279 | azo1211 | 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 protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.899 |
| azo2279 | azo2643 | azo2279 | azo2643 | 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 dual specificity protein phosphatase,; Function unclear. | 0.845 |
| 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 [...] | 0.898 |
| azo2279 | npd1 | azo2279 | azo0237 | 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 NAD-dependent deacetylase (EC 3.5.1.-) (Regulatory protein SIR2 homolog). Modulates the activities of several enzymes which are inactive in their acetylated form. Similar to SWISSPROT: sprot|NPD_AERPE (27% Aeropyrum pernix, NpdA or aq_2170) Pfam: PF02146 Sir2 family; High confidence in function and specificity. | 0.662 |