| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BF49_0170 | BF49_0205 | BF49_0170 | BF49_0205 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.524 |
| BF49_0170 | BF49_0223 | BF49_0170 | BF49_0223 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 0.534 |
| BF49_0170 | BF49_0380 | BF49_0170 | BF49_0380 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | tRNAt6A37 methylthiotransferase. | 0.476 |
| BF49_0170 | BF49_7356 | BF49_0170 | BF49_7356 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | tRNAi6A37 methylthiotransferase. | 0.602 |
| BF49_0170 | miaB | BF49_0170 | BF49_0031 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | tRNAi6A37 methylthiotransferase; 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. | 0.602 |
| BF49_0170 | rlmN | BF49_0170 | BF49_0320 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ribosomal RNA large subunit methyltransferase N EC 211; 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. | 0.724 |
| BF49_0205 | BF49_0170 | BF49_0205 | BF49_0170 | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.524 |
| BF49_0205 | BF49_0223 | BF49_0205 | BF49_0223 | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 0.660 |
| BF49_0205 | BF49_0380 | BF49_0205 | BF49_0380 | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | tRNAt6A37 methylthiotransferase. | 0.586 |
| BF49_0205 | BF49_7356 | BF49_0205 | BF49_7356 | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | tRNAi6A37 methylthiotransferase. | 0.549 |
| BF49_0205 | miaB | BF49_0205 | BF49_0031 | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | tRNAi6A37 methylthiotransferase; 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. | 0.549 |
| BF49_0205 | rlmN | BF49_0205 | BF49_0320 | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Ribosomal RNA large subunit methyltransferase N EC 211; 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. | 0.606 |
| BF49_0223 | BF49_0170 | BF49_0223 | BF49_0170 | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.534 |
| BF49_0223 | BF49_0205 | BF49_0223 | BF49_0205 | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Septum formation protein Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.660 |
| BF49_0223 | BF49_7356 | BF49_0223 | BF49_7356 | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | tRNAi6A37 methylthiotransferase. | 0.415 |
| BF49_0223 | miaB | BF49_0223 | BF49_0031 | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | tRNAi6A37 methylthiotransferase; 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. | 0.415 |
| BF49_0223 | rlmN | BF49_0223 | BF49_0320 | Hypothetical protein YggS proline synthase cotranscribed bacterial homolog PROSC; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Ribosomal RNA large subunit methyltransferase N EC 211; 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. | 0.605 |
| BF49_0263 | rlmN | BF49_0263 | BF49_0320 | 16S rRNA m5C 967 methyltransferase EC 211; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Ribosomal RNA large subunit methyltransferase N EC 211; 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. | 0.731 |
| BF49_0321 | rlmN | BF49_0321 | BF49_0320 | FIG00444358 hypothetical protein. | Ribosomal RNA large subunit methyltransferase N EC 211; 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. | 0.662 |
| BF49_0380 | BF49_0170 | BF49_0380 | BF49_0170 | tRNAt6A37 methylthiotransferase. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.476 |