| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Daci_3503 | clpP-2 | Daci_3503 | Daci_2645 | KEGG: ajs:Ajs_1832 ATP-dependent Clp protease, ATP-binding subunit ClpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 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. | 0.671 |
| Daci_3503 | groL | Daci_3503 | Daci_5661 | KEGG: ajs:Ajs_1832 ATP-dependent Clp protease, ATP-binding subunit ClpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.643 |
| Daci_3503 | groS | Daci_3503 | Daci_5660 | KEGG: ajs:Ajs_1832 ATP-dependent Clp protease, ATP-binding subunit ClpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.664 |
| Daci_3503 | lon | Daci_3503 | Daci_2647 | KEGG: ajs:Ajs_1832 ATP-dependent Clp protease, ATP-binding subunit ClpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.626 |
| Daci_3503 | tig | Daci_3503 | Daci_2644 | KEGG: ajs:Ajs_1832 ATP-dependent Clp protease, ATP-binding subunit ClpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.464 |
| Daci_3864 | clpP-2 | Daci_3864 | Daci_2645 | KEGG: aav:Aave_1482 ATPase AAA-2 domain protein; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 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. | 0.642 |
| Daci_3864 | groL | Daci_3864 | Daci_5661 | KEGG: aav:Aave_1482 ATPase AAA-2 domain protein; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.618 |
| Daci_3864 | groS | Daci_3864 | Daci_5660 | KEGG: aav:Aave_1482 ATPase AAA-2 domain protein; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.651 |
| Daci_3864 | lon | Daci_3864 | Daci_2647 | KEGG: aav:Aave_1482 ATPase AAA-2 domain protein; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.626 |
| clpB | clpP-2 | Daci_5207 | Daci_2645 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 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. | 0.698 |
| clpB | groL | Daci_5207 | Daci_5661 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.618 |
| clpB | groS | Daci_5207 | Daci_5660 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.651 |
| clpB | lon | Daci_5207 | Daci_2647 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.626 |
| clpP-2 | Daci_3503 | Daci_2645 | Daci_3503 | 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: ajs:Ajs_1832 ATP-dependent Clp protease, ATP-binding subunit ClpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 0.671 |
| clpP-2 | Daci_3864 | Daci_2645 | Daci_3864 | 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: aav:Aave_1482 ATPase AAA-2 domain protein; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 0.642 |
| clpP-2 | clpB | Daci_2645 | Daci_5207 | 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. | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.698 |
| clpP-2 | clpX | Daci_2645 | Daci_2646 | 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. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.986 |
| clpP-2 | def-2 | Daci_2645 | Daci_4855 | 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. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.562 |
| clpP-2 | groL | Daci_2645 | Daci_5661 | 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. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.696 |
| clpP-2 | groS | Daci_2645 | Daci_5660 | 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. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.717 |