node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADZ89323.1 | ADZ91544.1 | Marme_0017 | Marme_2303 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 0.477 |
ADZ89323.1 | ADZ92683.1 | Marme_0017 | Marme_3467 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | Hsp33 protein; 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. | 0.893 |
ADZ89323.1 | dnaJ | Marme_0017 | Marme_0569 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 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 [...] | 0.553 |
ADZ89323.1 | grpE | Marme_0017 | Marme_0567 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | 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-dependent i [...] | 0.590 |
ADZ89323.1 | hslU | Marme_0017 | Marme_3736 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | ATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.626 |
ADZ89323.1 | hslV | Marme_0017 | Marme_3735 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.741 |
ADZ89323.1 | htpG | Marme_0017 | Marme_1929 | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.483 |
ADZ91544.1 | ADZ89323.1 | Marme_2303 | Marme_0017 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | 0.477 |
ADZ91544.1 | ADZ92683.1 | Marme_2303 | Marme_3467 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Hsp33 protein; 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. | 0.499 |
ADZ91544.1 | ftsH | Marme_2303 | Marme_0972 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 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. | 0.421 |
ADZ91544.1 | groL | Marme_2303 | Marme_2068 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.796 |
ADZ91544.1 | grpE | Marme_2303 | Marme_0567 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 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-dependent i [...] | 0.862 |
ADZ91544.1 | hslU | Marme_2303 | Marme_3736 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.806 |
ADZ91544.1 | hslV | Marme_2303 | Marme_3735 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.766 |
ADZ91544.1 | htpG | Marme_2303 | Marme_1929 | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.895 |
ADZ92683.1 | ADZ89323.1 | Marme_3467 | Marme_0017 | Hsp33 protein; 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. | KEGG: mmw:Mmwyl1_0019 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4; Belongs to the HSP15 family. | 0.893 |
ADZ92683.1 | ADZ91544.1 | Marme_3467 | Marme_2303 | Hsp33 protein; 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. | KEGG: mmw:Mmwyl1_2077 heat shock protein DnaJ domain-containing protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 0.499 |
ADZ92683.1 | dnaJ | Marme_3467 | Marme_0569 | Hsp33 protein; 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 [...] | 0.577 |
ADZ92683.1 | ftsH | Marme_3467 | Marme_0972 | Hsp33 protein; 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. | 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. | 0.576 |
ADZ92683.1 | groL | Marme_3467 | Marme_2068 | Hsp33 protein; 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. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.590 |