| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADH59863.1 | ADH60730.1 | Tmath_0077 | Tmath_1008 | KEGG: tpd:Teth39_0051 hypothetical protein. | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | 0.725 |
| ADH59863.1 | dnaJ | Tmath_0077 | Tmath_0937 | KEGG: tpd:Teth39_0051 hypothetical 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 [...] | 0.702 |
| ADH59952.1 | ADH60730.1 | Tmath_0168 | Tmath_1008 | PFAM: AAA ATPase central domain protein; peptidase M41; KEGG: tpd:Teth39_2125 microtubule-severing ATPase; SMART: AAA ATPase; Belongs to the AAA ATPase family. | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | 0.573 |
| ADH59952.1 | dnaJ | Tmath_0168 | Tmath_0937 | PFAM: AAA ATPase central domain protein; peptidase M41; KEGG: tpd:Teth39_2125 microtubule-severing ATPase; SMART: AAA ATPase; Belongs to the AAA ATPase 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 [...] | 0.516 |
| ADH60730.1 | ADH59863.1 | Tmath_1008 | Tmath_0077 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | KEGG: tpd:Teth39_0051 hypothetical protein. | 0.725 |
| ADH60730.1 | ADH59952.1 | Tmath_1008 | Tmath_0168 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | PFAM: AAA ATPase central domain protein; peptidase M41; KEGG: tpd:Teth39_2125 microtubule-severing ATPase; SMART: AAA ATPase; Belongs to the AAA ATPase family. | 0.573 |
| ADH60730.1 | ADH60731.1 | Tmath_1008 | Tmath_1009 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | KEGG: tpd:Teth39_0963 radical SAM domain-containing protein; PFAM: Radical SAM domain protein; cobalamin B12-binding domain protein; SMART: Elongator protein 3/MiaB/NifB. | 0.537 |
| ADH60730.1 | ADH61644.1 | Tmath_1008 | Tmath_1957 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | KEGG: tpd:Teth39_0342 ATPase; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp domain protein; Clp ATPase-like; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 0.586 |
| ADH60730.1 | dnaJ | Tmath_1008 | Tmath_0937 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | 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 [...] | 0.543 |
| ADH60730.1 | ftsH | Tmath_1008 | Tmath_1771 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | ATP-dependent metalloprotease FtsH; 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. | 0.573 |
| ADH60730.1 | ftsH-2 | Tmath_1008 | Tmath_2014 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | ATP-dependent metalloprotease FtsH; 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. | 0.573 |
| ADH60730.1 | grpE | Tmath_1008 | Tmath_0935 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | GrpE 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 ATP-dependent i [...] | 0.650 |
| ADH60730.1 | ribBA | Tmath_1008 | Tmath_0040 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family. | 0.546 |
| ADH60730.1 | secY | Tmath_1008 | Tmath_1914 | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.615 |
| ADH60731.1 | ADH60730.1 | Tmath_1009 | Tmath_1008 | KEGG: tpd:Teth39_0963 radical SAM domain-containing protein; PFAM: Radical SAM domain protein; cobalamin B12-binding domain protein; SMART: Elongator protein 3/MiaB/NifB. | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | 0.537 |
| ADH61644.1 | ADH60730.1 | Tmath_1957 | Tmath_1008 | KEGG: tpd:Teth39_0342 ATPase; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp domain protein; Clp ATPase-like; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | KEGG: tex:Teth514_1403 STE24 endopeptidase; PFAM: peptidase M48 Ste24p. | 0.586 |
| ADH61644.1 | dnaJ | Tmath_1957 | Tmath_0937 | KEGG: tpd:Teth39_0342 ATPase; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp domain protein; Clp ATPase-like; SMART: AAA ATPase; Belongs to the ClpA/ClpB 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 [...] | 0.979 |
| ADH61644.1 | grpE | Tmath_1957 | Tmath_0935 | KEGG: tpd:Teth39_0342 ATPase; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp domain protein; Clp ATPase-like; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | GrpE 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 ATP-dependent i [...] | 0.923 |
| dnaJ | ADH59863.1 | Tmath_0937 | Tmath_0077 | 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 [...] | KEGG: tpd:Teth39_0051 hypothetical protein. | 0.702 |
| dnaJ | ADH59952.1 | Tmath_0937 | Tmath_0168 | 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 [...] | PFAM: AAA ATPase central domain protein; peptidase M41; KEGG: tpd:Teth39_2125 microtubule-severing ATPase; SMART: AAA ATPase; Belongs to the AAA ATPase family. | 0.516 |