node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EIC29258.1 | EIC29552.1 | Metal_1473 | Metal_1785 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | 0.528 |
EIC29258.1 | EIC29771.1 | Metal_1473 | Metal_2008 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | 0.439 |
EIC29258.1 | grpE | Metal_1473 | Metal_2047 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. | Molecular chaperone GrpE (heat shock 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. [...] | 0.966 |
EIC29258.1 | msrA | Metal_1473 | Metal_1214 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. | methionine-S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.469 |
EIC29505.1 | EIC29552.1 | Metal_1736 | Metal_1785 | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | 0.988 |
EIC29505.1 | EIC29771.1 | Metal_1736 | Metal_2008 | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | 0.644 |
EIC29552.1 | EIC29258.1 | Metal_1785 | Metal_1473 | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. | 0.528 |
EIC29552.1 | EIC29505.1 | Metal_1785 | Metal_1736 | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.988 |
EIC29552.1 | EIC29771.1 | Metal_1785 | Metal_2008 | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | 0.470 |
EIC29552.1 | dnaJ | Metal_1785 | Metal_2045 | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | 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 [...] | 0.528 |
EIC29771.1 | EIC29258.1 | Metal_2008 | Metal_1473 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. | 0.439 |
EIC29771.1 | EIC29505.1 | Metal_2008 | Metal_1736 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.644 |
EIC29771.1 | EIC29552.1 | Metal_2008 | Metal_1785 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | 0.470 |
EIC29771.1 | EIC31449.1 | Metal_2008 | Metal_3807 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | Hypothetical protein. | 0.846 |
EIC29771.1 | dnaJ | Metal_2008 | Metal_2045 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | 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 [...] | 0.439 |
EIC29771.1 | grpE | Metal_2008 | Metal_2047 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | Molecular chaperone GrpE (heat shock 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. [...] | 0.552 |
EIC29771.1 | msrA | Metal_2008 | Metal_1214 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | methionine-S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.473 |
EIC29771.1 | orn | Metal_2008 | Metal_2009 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | Oligoribonuclease (3'->5' exoribonuclease); 3'-to-5' exoribonuclease specific for small oligoribonucleotides; Belongs to the oligoribonuclease family. | 0.620 |
EIC29771.1 | rsgA | Metal_2008 | Metal_2007 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | Ribosome small subunit-dependent GTPase A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit; Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily. | 0.813 |
EIC29771.1 | serS | Metal_2008 | Metal_2010 | Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.450 |