| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO69525.1 | miaB | STAUR_1721 | STAUR_4328 | Oxygen-independent coproporphyrinogen III oxidase; 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. | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | 0.654 |
| ADO69525.1 | rimO | STAUR_1721 | STAUR_2278 | Oxygen-independent coproporphyrinogen III oxidase; 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. | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.518 |
| ADO69525.1 | rlmN | STAUR_1721 | STAUR_1908 | Oxygen-independent coproporphyrinogen III oxidase; 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; 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. | 0.703 |
| ADO69711.1 | rlmN | STAUR_1907 | STAUR_1908 | Uncharacterized protein. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.775 |
| ADO70478.1 | rlmN | STAUR_2675 | STAUR_1908 | Methyltransferase, RsmB/NOP family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.551 |
| ADO71104.1 | rlmN | STAUR_3312 | STAUR_1908 | Methyltransferase, RsmB/NOP family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.551 |
| ADO72020.1 | rlmN | STAUR_4239 | STAUR_1908 | Methyltransferase, RsmB/NOP family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.551 |
| ADO75782.1 | miaB | STAUR_8027 | STAUR_4328 | Coproporphyrinogen III oxidase. | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | 0.513 |
| ADO75782.1 | rimO | STAUR_8027 | STAUR_2278 | Coproporphyrinogen III oxidase. | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.428 |
| ADO75782.1 | rlmN | STAUR_8027 | STAUR_1908 | Coproporphyrinogen III oxidase. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.674 |
| efp | rlmN | STAUR_6438 | STAUR_1908 | Translation elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.554 |
| efp | rsmB | STAUR_6438 | STAUR_2169 | Translation elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.458 |
| miaB | ADO69525.1 | STAUR_4328 | STAUR_1721 | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.654 |
| miaB | ADO75782.1 | STAUR_4328 | STAUR_8027 | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | Coproporphyrinogen III oxidase. | 0.513 |
| miaB | rimO | STAUR_4328 | STAUR_2278 | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.418 |
| miaB | rlmN | STAUR_4328 | STAUR_1908 | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | Ribosomal RNA large subunit methyltransferase N; 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. | 0.770 |
| miaB | rsmB | STAUR_4328 | STAUR_2169 | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.675 |
| rimO | ADO69525.1 | STAUR_2278 | STAUR_1721 | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.518 |
| rimO | ADO75782.1 | STAUR_2278 | STAUR_8027 | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | Coproporphyrinogen III oxidase. | 0.428 |
| rimO | miaB | STAUR_2278 | STAUR_4328 | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. | 0.418 |