node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SKB59850.1 | SKB80258.1 | SAMN05660477_00125 | SAMN05660477_01193 | DnaJ domain-containing protein. | Molecular chaperone HtpG. | 0.907 |
SKB59850.1 | clpP | SAMN05660477_00125 | SAMN05660477_00329 | DnaJ domain-containing protein. | ATP-dependent Clp protease, protease subunit; 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. | 0.460 |
SKB59850.1 | dnaK | SAMN05660477_00125 | SAMN05660477_02206 | DnaJ domain-containing protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
SKB59850.1 | groL | SAMN05660477_00125 | SAMN05660477_00922 | DnaJ domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.701 |
SKB59850.1 | groS | SAMN05660477_00125 | SAMN05660477_00923 | DnaJ domain-containing protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.553 |
SKB59850.1 | grpE | SAMN05660477_00125 | SAMN05660477_00315 | 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 [...] | 0.798 |
SKB59850.1 | lon | SAMN05660477_00125 | SAMN05660477_01196 | DnaJ domain-containing protein. | ATP-dependent Lon protease; 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. | 0.424 |
SKB80258.1 | SKB59850.1 | SAMN05660477_01193 | SAMN05660477_00125 | Molecular chaperone HtpG. | DnaJ domain-containing protein. | 0.907 |
SKB80258.1 | clpP | SAMN05660477_01193 | SAMN05660477_00329 | Molecular chaperone HtpG. | ATP-dependent Clp protease, protease subunit; 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. | 0.532 |
SKB80258.1 | dnaJ | SAMN05660477_01193 | SAMN05660477_00316 | Molecular chaperone HtpG. | Molecular chaperone 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, [...] | 0.907 |
SKB80258.1 | dnaK | SAMN05660477_01193 | SAMN05660477_02206 | Molecular chaperone HtpG. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
SKB80258.1 | groL | SAMN05660477_01193 | SAMN05660477_00922 | Molecular chaperone HtpG. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.885 |
SKB80258.1 | groS | SAMN05660477_01193 | SAMN05660477_00923 | Molecular chaperone HtpG. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.818 |
SKB80258.1 | grpE | SAMN05660477_01193 | SAMN05660477_00315 | Molecular chaperone HtpG. | 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 [...] | 0.770 |
SKB80258.1 | lon | SAMN05660477_01193 | SAMN05660477_01196 | Molecular chaperone HtpG. | ATP-dependent Lon protease; 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. | 0.824 |
SKB92204.1 | groL | SAMN05660477_01886 | SAMN05660477_00922 | Diacylglycerol kinase family enzyme. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.970 |
clpP | SKB59850.1 | SAMN05660477_00329 | SAMN05660477_00125 | ATP-dependent Clp protease, protease subunit; 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. | DnaJ domain-containing protein. | 0.460 |
clpP | SKB80258.1 | SAMN05660477_00329 | SAMN05660477_01193 | ATP-dependent Clp protease, protease subunit; 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. | Molecular chaperone HtpG. | 0.532 |
clpP | dnaJ | SAMN05660477_00329 | SAMN05660477_00316 | ATP-dependent Clp protease, protease subunit; 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. | Molecular chaperone 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, [...] | 0.593 |
clpP | dnaK | SAMN05660477_00329 | SAMN05660477_02206 | ATP-dependent Clp protease, protease subunit; 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. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.753 |