| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| lepA | yggW | bbp_241 | bbp_498 | GTP-Binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.432 |
| lepA | yleA | bbp_241 | bbp_392 | GTP-Binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | Hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.502 |
| yfgB | yggW | bbp_265 | bbp_498 | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.547 |
| yfgB | yleA | bbp_265 | bbp_392 | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | Hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.498 |
| yggS | yggW | bbp_497 | bbp_498 | Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.659 |
| yggW | lepA | bbp_498 | bbp_241 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | GTP-Binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.432 |
| yggW | yfgB | bbp_498 | bbp_265 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.547 |
| yggW | yggS | bbp_498 | bbp_497 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 0.659 |
| yggW | yleA | bbp_498 | bbp_392 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.446 |
| yleA | lepA | bbp_392 | bbp_241 | Hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | GTP-Binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.502 |
| yleA | yfgB | bbp_392 | bbp_265 | Hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.498 |
| yleA | yggW | bbp_392 | bbp_498 | Hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.446 |
