node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDA42529.1 | SDA59173.1 | SAMN02927914_00436 | SAMN02927914_01465 | DnaJ domain-containing protein. | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | 0.481 |
SDA42529.1 | dnaK | SAMN02927914_00436 | SAMN02927914_00856 | DnaJ domain-containing protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
SDA42529.1 | ftsH-2 | SAMN02927914_00436 | SAMN02927914_03008 | DnaJ domain-containing protein. | Membrane protease FtsH catalytic subunit; 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. | 0.671 |
SDA42529.1 | grpE | SAMN02927914_00436 | SAMN02927914_04855 | DnaJ domain-containing protein. | Molecular chaperone GrpE; 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 [...] | 0.938 |
SDA42529.1 | hslU | SAMN02927914_00436 | SAMN02927914_05201 | DnaJ domain-containing protein. | ATP-dependent HslUV protease ATP-binding 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. | 0.816 |
SDA42529.1 | hslV | SAMN02927914_00436 | SAMN02927914_05204 | DnaJ domain-containing protein. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.788 |
SDA42529.1 | htpG | SAMN02927914_00436 | SAMN02927914_02492 | DnaJ domain-containing protein. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.968 |
SDA42529.1 | lon | SAMN02927914_00436 | SAMN02927914_02616 | DnaJ domain-containing protein. | ATP-dependent proteinase. Serine peptidase. MEROPS family S16; 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. | 0.795 |
SDA59173.1 | SDA42529.1 | SAMN02927914_01465 | SAMN02927914_00436 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | DnaJ domain-containing protein. | 0.481 |
SDA59173.1 | dnaK | SAMN02927914_01465 | SAMN02927914_00856 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
SDA59173.1 | ftsH-2 | SAMN02927914_01465 | SAMN02927914_03008 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Membrane protease FtsH catalytic subunit; 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. | 0.658 |
SDA59173.1 | grpE | SAMN02927914_01465 | SAMN02927914_04855 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone GrpE; 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 [...] | 0.954 |
SDA59173.1 | hslU | SAMN02927914_01465 | SAMN02927914_05201 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent HslUV protease ATP-binding 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. | 0.816 |
SDA59173.1 | hslV | SAMN02927914_01465 | SAMN02927914_05204 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.788 |
SDA59173.1 | htpG | SAMN02927914_01465 | SAMN02927914_02492 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.975 |
SDA59173.1 | lon | SAMN02927914_01465 | SAMN02927914_02616 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent proteinase. Serine peptidase. MEROPS family S16; 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. | 0.821 |
clpX | dnaK | SAMN02927914_02615 | SAMN02927914_00856 | 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. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.412 |
clpX | ftsH-2 | SAMN02927914_02615 | SAMN02927914_03008 | 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. | Membrane protease FtsH catalytic subunit; 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. | 0.802 |
clpX | grpE | SAMN02927914_02615 | SAMN02927914_04855 | 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. | Molecular chaperone GrpE; 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 [...] | 0.531 |
clpX | hslU | SAMN02927914_02615 | SAMN02927914_05201 | 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. | ATP-dependent HslUV protease ATP-binding 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. | 0.534 |