| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| def1 | fmt | VC_0046 | VC_0045 | 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. | 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. | 0.969 |
| def1 | rplD | VC_0046 | VC_2595 | 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. | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | 0.877 |
| def1 | rplI | VC_0046 | VC_0369 | 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. | Ribosomal protein L9; Binds to the 23S rRNA. | 0.893 |
| def1 | rplT | VC_0046 | VC_A0290 | 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. | 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 (By similarity). | 0.894 |
| def1 | rplU | VC_0046 | VC_0435 | 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. | Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.893 |
| def1 | rplV | VC_0046 | VC_2591 | 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. | Ribosomal protein L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). | 0.877 |
| def1 | rpmA | VC_0046 | VC_0436 | 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. | Ribosomal protein L27; Similar to GB:D13267 SP:P02427 PID:216637 PID:606123 GB:U00096; identified by sequence similarity; putative; Belongs to the bacterial ribosomal protein bL27 family. | 0.866 |
| def1 | rpsJ | VC_0046 | VC_2597 | 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. | Ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | 0.893 |
| def1 | rpsP | VC_0046 | VC_0561 | 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. | Ribosomal protein S16; Similar to SP:P02372 PID:43143 GB:U00096 PID:1788961; identified by sequence similarity; putative; Belongs to the bacterial ribosomal protein bS16 family. | 0.881 |
| def1 | tig | VC_0046 | VC_1923 | 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. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.871 |
| fmt | def1 | VC_0045 | VC_0046 | 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. | 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. | 0.969 |
| fmt | rplI | VC_0045 | VC_0369 | 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. | Ribosomal protein L9; Binds to the 23S rRNA. | 0.456 |
| fmt | rplU | VC_0045 | VC_0435 | 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. | Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.469 |
| fmt | rpsJ | VC_0045 | VC_2597 | 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. | Ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | 0.534 |
| rplD | def1 | VC_2595 | VC_0046 | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | 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. | 0.877 |
| rplD | rplI | VC_2595 | VC_0369 | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | Ribosomal protein L9; Binds to the 23S rRNA. | 0.993 |
| rplD | rplT | VC_2595 | VC_A0290 | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | 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 (By similarity). | 0.994 |
| rplD | rplU | VC_2595 | VC_0435 | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.993 |
| rplD | rplV | VC_2595 | VC_2591 | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | Ribosomal protein L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). | 0.999 |
| rplD | rpmA | VC_2595 | VC_0436 | Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion. | Ribosomal protein L27; Similar to GB:D13267 SP:P02427 PID:216637 PID:606123 GB:U00096; identified by sequence similarity; putative; Belongs to the bacterial ribosomal protein bL27 family. | 0.993 |