| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB84593.1 | AEB86783.1 | Alide2_2224 | Alide2_4480 | TIGRFAM: Glutathione reductase, eukaryote/bacterial; KEGG: dac:Daci_2356 glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation. | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 0.923 |
| AEB84593.1 | groL | Alide2_2224 | Alide2_0774 | TIGRFAM: Glutathione reductase, eukaryote/bacterial; KEGG: dac:Daci_2356 glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.425 |
| AEB85459.1 | AEB86783.1 | Alide2_3117 | Alide2_4480 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 0.766 |
| AEB85459.1 | groL | Alide2_3117 | Alide2_0774 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.407 |
| AEB86036.1 | AEB86783.1 | Alide2_3711 | Alide2_4480 | Thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; manually curated; KEGG: dia:Dtpsy_2721 thioredoxin reductase; TIGRFAM: Thioredoxin reductase. | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 0.680 |
| AEB86783.1 | AEB84593.1 | Alide2_4480 | Alide2_2224 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | TIGRFAM: Glutathione reductase, eukaryote/bacterial; KEGG: dac:Daci_2356 glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation. | 0.923 |
| AEB86783.1 | AEB85459.1 | Alide2_4480 | Alide2_3117 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.766 |
| AEB86783.1 | AEB86036.1 | Alide2_4480 | Alide2_3711 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | Thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; manually curated; KEGG: dia:Dtpsy_2721 thioredoxin reductase; TIGRFAM: Thioredoxin reductase. | 0.680 |
| AEB86783.1 | dnaJ | Alide2_4480 | Alide2_1320 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin 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 [...] | 0.802 |
| AEB86783.1 | groL | Alide2_4480 | Alide2_0774 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.679 |
| AEB86783.1 | grpE | Alide2_4480 | Alide2_1322 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] | 0.829 |
| AEB86783.1 | hslU | Alide2_4480 | Alide2_4069 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.820 |
| AEB86783.1 | hslV | Alide2_4480 | Alide2_4070 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.813 |
| AEB86783.1 | htpG | Alide2_4480 | Alide2_0508 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.814 |
| AEB86783.1 | purK | Alide2_4480 | Alide2_4482 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | Phosphoribosylaminoimidazole carboxylase, ATPase subunit; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). | 0.672 |
| dnaJ | AEB86783.1 | Alide2_1320 | Alide2_4480 | 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 [...] | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 0.802 |
| dnaJ | groL | Alide2_1320 | Alide2_0774 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.926 |
| dnaJ | grpE | Alide2_1320 | Alide2_1322 | 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 [...] | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] | 0.979 |
| dnaJ | hslU | Alide2_1320 | Alide2_4069 | 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 [...] | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.913 |
| dnaJ | hslV | Alide2_1320 | Alide2_4070 | 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 [...] | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.840 |