| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LVIS_1989 | LVIS_1990 | LVIS_1989 | LVIS_1990 | Transcriptional regulator, LysR family; Belongs to the LysR transcriptional regulatory family. | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | 0.595 |
| LVIS_1990 | LVIS_1989 | LVIS_1990 | LVIS_1989 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | Transcriptional regulator, LysR family; Belongs to the LysR transcriptional regulatory family. | 0.595 |
| LVIS_1990 | fmt | LVIS_1990 | LVIS_0965 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | 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. | 0.630 |
| LVIS_1990 | map | LVIS_1990 | LVIS_1919 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.555 |
| LVIS_1990 | map-2 | LVIS_1990 | LVIS_2007 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.555 |
| LVIS_1990 | rplQ | LVIS_1990 | LVIS_1663 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | LSU ribosomal protein L17P. | 0.696 |
| LVIS_1990 | rplV | LVIS_1990 | LVIS_1685 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | LSU ribosomal protein L22P; 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). | 0.699 |
| LVIS_1990 | rpsP | LVIS_1990 | LVIS_0943 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | SSU ribosomal protein S16P; Belongs to the bacterial ribosomal protein bS16 family. | 0.617 |
| LVIS_1990 | rpsT | LVIS_1990 | LVIS_1393 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | SSU ribosomal protein S20P; Binds directly to 16S ribosomal RNA. | 0.569 |
| LVIS_1990 | rpsU | LVIS_1990 | LVIS_0744 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | SSU ribosomal protein S21P; Belongs to the bacterial ribosomal protein bS21 family. | 0.542 |
| LVIS_1990 | tig | LVIS_1990 | LVIS_1388 | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | FKBP-type peptidyl-prolyl cis-trans isomerase (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; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.576 |
| fmt | LVIS_1990 | LVIS_0965 | LVIS_1990 | 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. | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | 0.630 |
| map | LVIS_1990 | LVIS_1919 | LVIS_1990 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | 0.555 |
| map | rplQ | LVIS_1919 | LVIS_1663 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | LSU ribosomal protein L17P. | 0.671 |
| map | rplV | LVIS_1919 | LVIS_1685 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | LSU ribosomal protein L22P; 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). | 0.771 |
| map | rpsP | LVIS_1919 | LVIS_0943 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | SSU ribosomal protein S16P; Belongs to the bacterial ribosomal protein bS16 family. | 0.448 |
| map | rpsT | LVIS_1919 | LVIS_1393 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | SSU ribosomal protein S20P; Binds directly to 16S ribosomal RNA. | 0.464 |
| map-2 | LVIS_1990 | LVIS_2007 | LVIS_1990 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | N-formylmethionyl-tRNA deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family. | 0.555 |
| map-2 | rplQ | LVIS_2007 | LVIS_1663 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | LSU ribosomal protein L17P. | 0.628 |
| map-2 | rplV | LVIS_2007 | LVIS_1685 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | LSU ribosomal protein L22P; 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). | 0.771 |