node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
def | fmt | DR_2434 | DR_2435 | 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. | 0.963 |
def | rplI | DR_2434 | DR_0102 | 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 and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | 0.907 |
def | rplQ | DR_2434 | DR_2129 | 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 L17; Binds to the 23S rRNA; Belongs to the bacterial ribosomal protein bL17 family. | 0.941 |
def | rplT | DR_2434 | DR_2004 | 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 rRNA, probably serving to organize its structure; Belongs to the bacterial ribosomal protein bL20 family. | 0.936 |
def | rplV | DR_2434 | DR_0316 | 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). | 0.935 |
def | rpmA | DR_2434 | DR_0085 | 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; Binds the 5S and 23S rRNAs and also the tRNA in the P site; Belongs to the bacterial ribosomal protein bL27 family. | 0.909 |
def | rpsO | DR_2434 | DR_0341 | 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 S15; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. | 0.922 |
def | rpsP | DR_2434 | DR_1294 | 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 PID:2149138 percent identity: 86.57; identified by sequence similarity; putative; Belongs to the bacterial ribosomal protein bS16 family. | 0.924 |
def | rpsT | DR_2434 | DR_1309 | 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 S20; Binds directly to 16S ribosomal RNA. | 0.923 |
def | tig | DR_2434 | DR_1948 | 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). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, , exposing a hydrophobic crevice that is probably important for its chaperone activity. | 0.914 |
fmt | def | DR_2435 | DR_2434 | 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. | 0.963 |
fmt | rplI | DR_2435 | DR_0102 | 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 and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | 0.535 |
fmt | tig | DR_2435 | DR_1948 | 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. | 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). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, , exposing a hydrophobic crevice that is probably important for its chaperone activity. | 0.451 |
rplI | def | DR_0102 | DR_2434 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 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. | 0.907 |
rplI | fmt | DR_0102 | DR_2435 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 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. | 0.535 |
rplI | rplQ | DR_0102 | DR_2129 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | Ribosomal protein L17; Binds to the 23S rRNA; Belongs to the bacterial ribosomal protein bL17 family. | 0.999 |
rplI | rplT | DR_0102 | DR_2004 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | Ribosomal protein L20; Binds directly to 23S rRNA, probably serving to organize its structure; Belongs to the bacterial ribosomal protein bL20 family. | 0.999 |
rplI | rplV | DR_0102 | DR_0316 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | 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 |
rplI | rpmA | DR_0102 | DR_0085 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | Ribosomal protein L27; Binds the 5S and 23S rRNAs and also the tRNA in the P site; Belongs to the bacterial ribosomal protein bL27 family. | 0.998 |
rplI | rpsO | DR_0102 | DR_0341 | Ribosomal protein L9; Binds to the 23S rRNA and protein L31; Belongs to the bacterial ribosomal protein bL9 family. | Ribosomal protein S15; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. | 0.986 |