node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MJ_0443 | MJ_0719 | MJ_0443 | MJ_0719 | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | RNase L inhibitor; Similar to PIR:S63672 percent identity: 48.74; identified by sequence similarity; putative; Belongs to the ABC transporter superfamily. | 0.422 |
MJ_0443 | MJ_0882 | MJ_0443 | MJ_0882 | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | Conserved hypothetical protein; Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro. | 0.501 |
MJ_0443 | MJ_1136 | MJ_0443 | MJ_1136 | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | 0.534 |
MJ_0443 | dphB | MJ_0443 | MJ_1274 | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.480 |
MJ_0443 | rfcL | MJ_0443 | MJ_0884 | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | Activator 1 (replication factor C), 53 KD subunit; Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA; Belongs to the activator 1 small subunits family. RfcL subfamily. | 0.479 |
MJ_0443 | trm5b | MJ_0443 | MJ_0883 | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | Conserved hypothetical protein; Specifically methylates the N1 position of guanosine-37 in various tRNAs. | 0.659 |
MJ_0719 | MJ_0443 | MJ_0719 | MJ_0443 | RNase L inhibitor; Similar to PIR:S63672 percent identity: 48.74; identified by sequence similarity; putative; Belongs to the ABC transporter superfamily. | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | 0.422 |
MJ_0719 | MJ_0882 | MJ_0719 | MJ_0882 | RNase L inhibitor; Similar to PIR:S63672 percent identity: 48.74; identified by sequence similarity; putative; Belongs to the ABC transporter superfamily. | Conserved hypothetical protein; Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro. | 0.475 |
MJ_0719 | trm5b | MJ_0719 | MJ_0883 | RNase L inhibitor; Similar to PIR:S63672 percent identity: 48.74; identified by sequence similarity; putative; Belongs to the ABC transporter superfamily. | Conserved hypothetical protein; Specifically methylates the N1 position of guanosine-37 in various tRNAs. | 0.541 |
MJ_0882 | MJ_0443 | MJ_0882 | MJ_0443 | Conserved hypothetical protein; Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro. | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | 0.501 |
MJ_0882 | MJ_0719 | MJ_0882 | MJ_0719 | Conserved hypothetical protein; Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro. | RNase L inhibitor; Similar to PIR:S63672 percent identity: 48.74; identified by sequence similarity; putative; Belongs to the ABC transporter superfamily. | 0.475 |
MJ_0882 | rfcL | MJ_0882 | MJ_0884 | Conserved hypothetical protein; Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro. | Activator 1 (replication factor C), 53 KD subunit; Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA; Belongs to the activator 1 small subunits family. RfcL subfamily. | 0.762 |
MJ_0882 | trm5b | MJ_0882 | MJ_0883 | Conserved hypothetical protein; Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro. | Conserved hypothetical protein; Specifically methylates the N1 position of guanosine-37 in various tRNAs. | 0.988 |
MJ_1136 | MJ_0443 | MJ_1136 | MJ_0443 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | 0.534 |
MJ_1136 | dphB | MJ_1136 | MJ_1274 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.597 |
MJ_1136 | taw1 | MJ_1136 | MJ_0257 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Conserved hypothetical protein; Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe). | 0.417 |
MJ_1136 | trm5b | MJ_1136 | MJ_0883 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Conserved hypothetical protein; Specifically methylates the N1 position of guanosine-37 in various tRNAs. | 0.507 |
dphB | MJ_0443 | MJ_1274 | MJ_0443 | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative. | 0.480 |
dphB | MJ_1136 | MJ_1274 | MJ_1136 | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | 0.597 |
dphB | trm5b | MJ_1274 | MJ_0883 | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | Conserved hypothetical protein; Specifically methylates the N1 position of guanosine-37 in various tRNAs. | 0.691 |