| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB83089.1 | AEB83308.1 | Alide2_0673 | Alide2_0897 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | 0.628 |
| AEB83089.1 | clpP | Alide2_0673 | Alide2_1459 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.562 |
| AEB83089.1 | ftsH-3 | Alide2_0673 | Alide2_4290 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.468 |
| AEB83089.1 | groL | Alide2_0673 | Alide2_0774 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.870 |
| AEB83089.1 | grpE | Alide2_0673 | Alide2_1322 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 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 [...] | 0.936 |
| AEB83089.1 | hslU | Alide2_0673 | Alide2_4069 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 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. | 0.778 |
| AEB83089.1 | hslV | Alide2_0673 | Alide2_4070 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.611 |
| AEB83089.1 | htpG | Alide2_0673 | Alide2_0508 | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.962 |
| AEB83307.1 | AEB83308.1 | Alide2_0896 | Alide2_0897 | PFAM: Domain of unknown function DUF21; Cystathionine beta-synthase, core; Transporter-associated domain; KEGG: dia:Dtpsy_0777 protein of unknown function DUF21. | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | 0.649 |
| AEB83308.1 | AEB83089.1 | Alide2_0897 | Alide2_0673 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 0.628 |
| AEB83308.1 | AEB83307.1 | Alide2_0897 | Alide2_0896 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | PFAM: Domain of unknown function DUF21; Cystathionine beta-synthase, core; Transporter-associated domain; KEGG: dia:Dtpsy_0777 protein of unknown function DUF21. | 0.649 |
| AEB83308.1 | clpP | Alide2_0897 | Alide2_1459 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.631 |
| AEB83308.1 | dnaJ | Alide2_0897 | Alide2_1320 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | 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 [...] | 0.796 |
| AEB83308.1 | ftsH-3 | Alide2_0897 | Alide2_4290 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.620 |
| AEB83308.1 | groL | Alide2_0897 | Alide2_0774 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.837 |
| AEB83308.1 | grpE | Alide2_0897 | Alide2_1322 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | 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 [...] | 0.788 |
| AEB83308.1 | hslU | Alide2_0897 | Alide2_4069 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | 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. | 0.801 |
| AEB83308.1 | hslV | Alide2_0897 | Alide2_4070 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.781 |
| AEB83308.1 | htpG | Alide2_0897 | Alide2_0508 | KEGG: aav:Aave_3667 ATPase central domain-containing protein; PFAM: ATPase, AAA-type, core; SMART: ATPase, AAA+ type, core. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.807 |
| clpP | AEB83089.1 | Alide2_1459 | Alide2_0673 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 0.562 |