| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BDP_0057 | tgt | BDP_0057 | BDP_0056 | Serine protease. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.594 |
| aspS | der | BDP_0785 | BDP_1165 | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.495 |
| aspS | gltX | BDP_0785 | BDP_2005 | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.484 |
| aspS | hisS | BDP_0785 | BDP_0784 | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | HisS Histidyl-tRNA synthetase. | 0.932 |
| aspS | tgt | BDP_0785 | BDP_0056 | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.512 |
| der | aspS | BDP_1165 | BDP_0785 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.495 |
| der | gltX | BDP_1165 | BDP_2005 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.407 |
| der | tgt | BDP_1165 | BDP_0056 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.434 |
| der | tig | BDP_1165 | BDP_1372 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | Tig Trigger factor, PPIase; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.564 |
| der | trmD | BDP_1165 | BDP_0307 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | trmD tRNA (Guanine-N1) -methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. | 0.577 |
| der | truB | BDP_1165 | BDP_0467 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | truB tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. | 0.660 |
| gltX | aspS | BDP_2005 | BDP_0785 | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.484 |
| gltX | der | BDP_2005 | BDP_1165 | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.407 |
| gltX | tgt | BDP_2005 | BDP_0056 | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.540 |
| hisS | aspS | BDP_0784 | BDP_0785 | HisS Histidyl-tRNA synthetase. | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.932 |
| hisS | tgt | BDP_0784 | BDP_0056 | HisS Histidyl-tRNA synthetase. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.465 |
| hisS | truB | BDP_0784 | BDP_0467 | HisS Histidyl-tRNA synthetase. | truB tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. | 0.437 |
| tgt | BDP_0057 | BDP_0056 | BDP_0057 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | Serine protease. | 0.594 |
| tgt | aspS | BDP_0056 | BDP_0785 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | aspS Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.512 |
| tgt | der | BDP_0056 | BDP_1165 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.434 |