| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ97023.1 | clpC | ZOBELLIA_2876 | ZOBELLIA_469 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.638 |
| CAZ97023.1 | dnaK | ZOBELLIA_2876 | ZOBELLIA_4708 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.576 |
| CAZ97023.1 | grpE | ZOBELLIA_2876 | ZOBELLIA_2823 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Co-chaperone HSP-70 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 [...] | 0.494 |
| CAZ97023.1 | htpG | ZOBELLIA_2876 | ZOBELLIA_607 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.575 |
| CAZ97207.1 | clpC | ZOBELLIA_3068 | ZOBELLIA_469 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.718 |
| CAZ97207.1 | clpP1 | ZOBELLIA_3068 | ZOBELLIA_2449 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | Endopeptidase Clp, peptidase subunit, family S14; 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. | 0.476 |
| CAZ97207.1 | clpP2 | ZOBELLIA_3068 | ZOBELLIA_718 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | Endopeptidase Clp, peptidase subunit, family S14; 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. | 0.480 |
| CAZ97207.1 | dnaK | ZOBELLIA_3068 | ZOBELLIA_4708 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.901 |
| CAZ97207.1 | groL | ZOBELLIA_3068 | ZOBELLIA_1162 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.704 |
| CAZ97207.1 | grpE | ZOBELLIA_3068 | ZOBELLIA_2823 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | Co-chaperone HSP-70 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 [...] | 0.753 |
| CAZ97207.1 | htpG | ZOBELLIA_3068 | ZOBELLIA_607 | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.847 |
| CAZ97977.1 | clpC | ZOBELLIA_3839 | ZOBELLIA_469 | Heat shock protein acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation; Belongs to the HSP20 family. Hsp20 proteins seem to form large heterooligomeric aggregates; Localized in the cytoplasm; Family membership. | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.638 |
| CAZ97977.1 | dnaK | ZOBELLIA_3839 | ZOBELLIA_4708 | Heat shock protein acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation; Belongs to the HSP20 family. Hsp20 proteins seem to form large heterooligomeric aggregates; Localized in the cytoplasm; Family membership. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.576 |
| CAZ97977.1 | grpE | ZOBELLIA_3839 | ZOBELLIA_2823 | Heat shock protein acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation; Belongs to the HSP20 family. Hsp20 proteins seem to form large heterooligomeric aggregates; Localized in the cytoplasm; Family membership. | Co-chaperone HSP-70 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 [...] | 0.494 |
| CAZ97977.1 | htpG | ZOBELLIA_3839 | ZOBELLIA_607 | Heat shock protein acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation; Belongs to the HSP20 family. Hsp20 proteins seem to form large heterooligomeric aggregates; Localized in the cytoplasm; Family membership. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.575 |
| clpC | CAZ97023.1 | ZOBELLIA_469 | ZOBELLIA_2876 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 0.638 |
| clpC | CAZ97207.1 | ZOBELLIA_469 | ZOBELLIA_3068 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm. | 0.718 |
| clpC | CAZ97977.1 | ZOBELLIA_469 | ZOBELLIA_3839 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Heat shock protein acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation; Belongs to the HSP20 family. Hsp20 proteins seem to form large heterooligomeric aggregates; Localized in the cytoplasm; Family membership. | 0.638 |
| clpC | clpP1 | ZOBELLIA_469 | ZOBELLIA_2449 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, peptidase subunit, family S14; 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. | 0.816 |
| clpC | clpP2 | ZOBELLIA_469 | ZOBELLIA_718 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, peptidase subunit, family S14; 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. | 0.819 |