| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rmag_0034 | Rmag_0682 | Rmag_0034 | Rmag_0682 | Cytochrome-c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 0.701 |
| Rmag_0034 | Rmag_0744 | Rmag_0034 | Rmag_0744 | Cytochrome-c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | PFAM: electron transport protein SCO1/SenC; KEGG: rbe:RBE_0699 Sco2 protein precursor. | 0.903 |
| Rmag_0044 | Rmag_0098 | Rmag_0044 | Rmag_0098 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: tcx:Tcr_0763 thioredoxin reductase. | PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein; KEGG: tcx:Tcr_1387 alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen. | 0.907 |
| Rmag_0044 | Rmag_0682 | Rmag_0044 | Rmag_0682 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: tcx:Tcr_0763 thioredoxin reductase. | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 0.640 |
| Rmag_0098 | Rmag_0044 | Rmag_0098 | Rmag_0044 | PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein; KEGG: tcx:Tcr_1387 alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen. | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: tcx:Tcr_0763 thioredoxin reductase. | 0.907 |
| Rmag_0098 | Rmag_0682 | Rmag_0098 | Rmag_0682 | PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein; KEGG: tcx:Tcr_1387 alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen. | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 0.803 |
| Rmag_0310 | Rmag_0682 | Rmag_0310 | Rmag_0682 | PFAM: peptidylprolyl isomerase, FKBP-type; peptidyl-prolyl cis-trans isomerase, cyclophilin type; KEGG: tde:TDE2391 peptidyl-prolyl cis-trans isomerase. | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 0.869 |
| Rmag_0310 | dnaJ | Rmag_0310 | Rmag_0352 | PFAM: peptidylprolyl isomerase, FKBP-type; peptidyl-prolyl cis-trans isomerase, cyclophilin type; KEGG: tde:TDE2391 peptidyl-prolyl cis-trans isomerase. | 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 [...] | 0.897 |
| Rmag_0682 | Rmag_0034 | Rmag_0682 | Rmag_0034 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | Cytochrome-c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.701 |
| Rmag_0682 | Rmag_0044 | Rmag_0682 | Rmag_0044 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: tcx:Tcr_0763 thioredoxin reductase. | 0.640 |
| Rmag_0682 | Rmag_0098 | Rmag_0682 | Rmag_0098 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein; KEGG: tcx:Tcr_1387 alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen. | 0.803 |
| Rmag_0682 | Rmag_0310 | Rmag_0682 | Rmag_0310 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | PFAM: peptidylprolyl isomerase, FKBP-type; peptidyl-prolyl cis-trans isomerase, cyclophilin type; KEGG: tde:TDE2391 peptidyl-prolyl cis-trans isomerase. | 0.869 |
| Rmag_0682 | Rmag_0744 | Rmag_0682 | Rmag_0744 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | PFAM: electron transport protein SCO1/SenC; KEGG: rbe:RBE_0699 Sco2 protein precursor. | 0.599 |
| Rmag_0682 | dnaJ | Rmag_0682 | Rmag_0352 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 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 [...] | 0.673 |
| Rmag_0682 | dsbD | Rmag_0682 | Rmag_1057 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | Protein-disulfide reductase; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.860 |
| Rmag_0682 | msrA | Rmag_0682 | Rmag_0636 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | Peptide methionine 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. | 0.726 |
| Rmag_0682 | pdxB | Rmag_0682 | Rmag_0684 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 4-phosphoerythronate dehydrogenase; Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate. | 0.773 |
| Rmag_0682 | ung | Rmag_0682 | Rmag_0683 | KEGG: tcx:Tcr_1759 thioredoxin, putative. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.773 |
| Rmag_0744 | Rmag_0034 | Rmag_0744 | Rmag_0034 | PFAM: electron transport protein SCO1/SenC; KEGG: rbe:RBE_0699 Sco2 protein precursor. | Cytochrome-c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.903 |
| Rmag_0744 | Rmag_0682 | Rmag_0744 | Rmag_0682 | PFAM: electron transport protein SCO1/SenC; KEGG: rbe:RBE_0699 Sco2 protein precursor. | KEGG: tcx:Tcr_1759 thioredoxin, putative. | 0.599 |