| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rta_36870 | azlC-2 | Rta_36870 | Rta_36880 | Conserved hypothetical protein. | Candidate branched chain amino acid permease, azaleucine resistance. | 0.947 |
| Rta_36870 | def-2 | Rta_36870 | Rta_36910 | Conserved hypothetical protein. | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.786 |
| Rta_36870 | fmt | Rta_36870 | Rta_36890 | Conserved hypothetical protein. | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.804 |
| azlC-2 | Rta_36870 | Rta_36880 | Rta_36870 | Candidate branched chain amino acid permease, azaleucine resistance. | Conserved hypothetical protein. | 0.947 |
| azlC-2 | def-2 | Rta_36880 | Rta_36910 | Candidate branched chain amino acid permease, azaleucine resistance. | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.786 |
| azlC-2 | fmt | Rta_36880 | Rta_36890 | Candidate branched chain amino acid permease, azaleucine resistance. | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.804 |
| def-2 | Rta_36870 | Rta_36910 | Rta_36870 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Conserved hypothetical protein. | 0.786 |
| def-2 | azlC-2 | Rta_36910 | Rta_36880 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate branched chain amino acid permease, azaleucine resistance. | 0.786 |
| def-2 | fmt | Rta_36910 | Rta_36890 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.981 |
| def-2 | rplI | Rta_36910 | Rta_24100 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 50S ribosomal protein L9; Binds to the 23S rRNA. | 0.813 |
| def-2 | rplM | Rta_36910 | Rta_07010 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate 50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.782 |
| def-2 | rplR | Rta_36910 | Rta_36150 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate 50S ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | 0.783 |
| def-2 | rplT | Rta_36910 | Rta_17800 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate 50S ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | 0.835 |
| def-2 | rplU | Rta_36910 | Rta_29120 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate 50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.798 |
| def-2 | rplV | Rta_36910 | Rta_03310 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate 50S ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | 0.802 |
| def-2 | rpsJ | Rta_36910 | Rta_03250 | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Candidate 30S ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | 0.777 |
| fmt | Rta_36870 | Rta_36890 | Rta_36870 | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Conserved hypothetical protein. | 0.804 |
| fmt | azlC-2 | Rta_36890 | Rta_36880 | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Candidate branched chain amino acid permease, azaleucine resistance. | 0.804 |
| fmt | def-2 | Rta_36890 | Rta_36910 | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Candidate peptide deformylase (Polypeptide deformylase); Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.981 |
| fmt | rplU | Rta_36890 | Rta_29120 | Candidate methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Candidate 50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.501 |