node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KRM26448.1 | KRM26452.1 | FD32_GL000417 | FD32_GL000421 | S4 domain protein. | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | 0.481 |
KRM26448.1 | dnaJ | FD32_GL000417 | FD32_GL000599 | S4 domain protein. | 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 [...] | 0.483 |
KRM26448.1 | ftsH | FD32_GL000417 | FD32_GL000422 | S4 domain protein. | ATP-dependent metallopeptidase HflB; 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. | 0.437 |
KRM26448.1 | grpE | FD32_GL000417 | FD32_GL000597 | S4 domain protein. | Co-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-depend [...] | 0.545 |
KRM26448.1 | hslO | FD32_GL000417 | FD32_GL000423 | S4 domain protein. | Chaperonin HslO; 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. | 0.833 |
KRM26448.1 | tilS | FD32_GL000417 | FD32_GL000420 | S4 domain protein. | tRNA(Ile)-lysidine synthase (tRNA(Ile)-lysidinesynthetase); 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. | 0.609 |
KRM26452.1 | KRM26448.1 | FD32_GL000421 | FD32_GL000417 | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | S4 domain protein. | 0.481 |
KRM26452.1 | KRM26455.1 | FD32_GL000421 | FD32_GL000424 | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | Transcription regulator; 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. | 0.436 |
KRM26452.1 | ftsH | FD32_GL000421 | FD32_GL000422 | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | ATP-dependent metallopeptidase HflB; 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. | 0.919 |
KRM26452.1 | hslO | FD32_GL000421 | FD32_GL000423 | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | Chaperonin HslO; 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. | 0.525 |
KRM26452.1 | tilS | FD32_GL000421 | FD32_GL000420 | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | tRNA(Ile)-lysidine synthase (tRNA(Ile)-lysidinesynthetase); 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. | 0.998 |
KRM26455.1 | KRM26452.1 | FD32_GL000424 | FD32_GL000421 | Transcription regulator; 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. | Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | 0.436 |
KRM26455.1 | ftsH | FD32_GL000424 | FD32_GL000422 | Transcription regulator; 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. | ATP-dependent metallopeptidase HflB; 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. | 0.630 |
KRM26455.1 | hslO | FD32_GL000424 | FD32_GL000423 | Transcription regulator; 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. | Chaperonin HslO; 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. | 0.743 |
KRM26455.1 | lysS | FD32_GL000424 | FD32_GL000425 | Transcription regulator; 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. | lysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.837 |
KRM26455.1 | tilS | FD32_GL000424 | FD32_GL000420 | Transcription regulator; 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. | tRNA(Ile)-lysidine synthase (tRNA(Ile)-lysidinesynthetase); 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. | 0.577 |
dnaJ | KRM26448.1 | FD32_GL000599 | FD32_GL000417 | 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 [...] | S4 domain protein. | 0.483 |
dnaJ | dnaK | FD32_GL000599 | FD32_GL000598 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | ftsH | FD32_GL000599 | FD32_GL000422 | 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 [...] | ATP-dependent metallopeptidase HflB; 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. | 0.680 |
dnaJ | groL | FD32_GL000599 | FD32_GL001328 | 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 [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.957 |