node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
WDC_0250 | WDC_0256 | WDC_0250 | WDC_0256 | RNA-binding S4. | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.677 |
WDC_0250 | WDC_0257 | WDC_0250 | WDC_0257 | RNA-binding S4. | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | 0.677 |
WDC_0250 | grpE | WDC_0250 | WDC_1728 | RNA-binding S4. | Heat shock protein 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- [...] | 0.462 |
WDC_0250 | hpt | WDC_0250 | WDC_0254 | RNA-binding S4. | Protein involved in hypoxanthine phosphoribosyltransferase activity; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | 0.414 |
WDC_0250 | tilS | WDC_0250 | WDC_0253 | RNA-binding S4. | tRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | 0.468 |
WDC_0256 | WDC_0250 | WDC_0256 | WDC_0250 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | RNA-binding S4. | 0.677 |
WDC_0256 | WDC_0257 | WDC_0256 | WDC_0257 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | 0.994 |
WDC_0256 | WDC_1328 | WDC_0256 | WDC_1328 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Hypothetical protein. | 0.484 |
WDC_0256 | dnaJ | WDC_0256 | WDC_1730 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 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 [...] | 0.500 |
WDC_0256 | dusB | WDC_0256 | WDC_0258 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | tRNA dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.647 |
WDC_0256 | ftsH | WDC_0256 | WDC_0255 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Cell division protein; 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. | 0.683 |
WDC_0256 | groEL | WDC_0256 | WDC_1745 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.505 |
WDC_0256 | grpE | WDC_0256 | WDC_1728 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Heat shock protein 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 |
WDC_0256 | hpt | WDC_0256 | WDC_0254 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Protein involved in hypoxanthine phosphoribosyltransferase activity; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | 0.468 |
WDC_0256 | tilS | WDC_0256 | WDC_0253 | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | tRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | 0.470 |
WDC_0257 | WDC_0250 | WDC_0257 | WDC_0250 | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | RNA-binding S4. | 0.677 |
WDC_0257 | WDC_0256 | WDC_0257 | WDC_0256 | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | Chaperonin hsp 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.994 |
WDC_0257 | dnaJ | WDC_0257 | WDC_1730 | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | 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 [...] | 0.500 |
WDC_0257 | dusB | WDC_0257 | WDC_0258 | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | tRNA dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.647 |
WDC_0257 | ftsH | WDC_0257 | WDC_0255 | Chaperonin hsp 33; Protein involved in unfolded protein binding and protein folding. | Cell division protein; 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. | 0.683 |