node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SB4_00340 | rlmN | SB4_00340 | SB4_07350 | RNA methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | RNA methyltransferase RlmN; 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. | 0.644 |
SB4_07345 | SB4_07355 | SB4_07345 | SB4_07355 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.454 |
SB4_07345 | SB4_07360 | SB4_07345 | SB4_07360 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.471 |
SB4_07345 | rlmN | SB4_07345 | SB4_07350 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA methyltransferase RlmN; 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. | 0.738 |
SB4_07355 | SB4_07345 | SB4_07355 | SB4_07345 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.454 |
SB4_07355 | SB4_07360 | SB4_07355 | SB4_07360 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.494 |
SB4_07355 | rlmN | SB4_07355 | SB4_07350 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA methyltransferase RlmN; 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. | 0.784 |
SB4_07360 | SB4_07345 | SB4_07360 | SB4_07345 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.471 |
SB4_07360 | SB4_07355 | SB4_07360 | SB4_07355 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.494 |
SB4_07360 | rlmN | SB4_07360 | SB4_07350 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA methyltransferase RlmN; 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. | 0.757 |
SB4_07845 | miaB | SB4_07845 | SB4_04145 | 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. | (dimethylallyl)adenosine tRNA 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. | 0.539 |
SB4_07845 | rlmN | SB4_07845 | SB4_07350 | 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. | RNA methyltransferase RlmN; 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. | 0.714 |
SB4_15665 | rlmN | SB4_15665 | SB4_07350 | 2-methylthioadenine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA methyltransferase RlmN; 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. | 0.679 |
SB4_18615 | rlmN | SB4_18615 | SB4_07350 | SAM-dependent methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | RNA methyltransferase RlmN; 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. | 0.644 |
amn | metK | SB4_03075 | SB4_04195 | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.484 |
amn | rlmN | SB4_03075 | SB4_07350 | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | RNA methyltransferase RlmN; 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. | 0.706 |
metK | amn | SB4_04195 | SB4_03075 | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | 0.484 |
metK | rlmN | SB4_04195 | SB4_07350 | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | RNA methyltransferase RlmN; 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. | 0.678 |
miaB | SB4_07845 | SB4_04145 | SB4_07845 | (dimethylallyl)adenosine tRNA 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. | 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. | 0.539 |
miaB | rlmN | SB4_04145 | SB4_07350 | (dimethylallyl)adenosine tRNA 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. | RNA methyltransferase RlmN; 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. | 0.783 |