node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ANZ45871.1 | BED41_06005 | BED41_12710 | BED41_06005 | Single-stranded DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.533 |
ANZ45871.1 | dnaX | BED41_12710 | BED41_06580 | Single-stranded DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA polymerase III, subunit gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. | 0.884 |
ANZ45871.1 | metG | BED41_12710 | BED41_05985 | Single-stranded DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.595 |
ANZ46588.1 | BED41_06005 | BED41_06015 | BED41_06005 | threonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.724 |
ANZ46588.1 | tgt | BED41_06015 | BED41_06010 | threonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. | tRNA guanosine(34) transglycosylase Tgt; 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 t [...] | 0.678 |
BED41_06005 | ANZ45871.1 | BED41_06005 | BED41_12710 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | Single-stranded DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.533 |
BED41_06005 | ANZ46588.1 | BED41_06005 | BED41_06015 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | threonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. | 0.724 |
BED41_06005 | aspS | BED41_06005 | BED41_12135 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | aspartate--tRNA ligase; 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. | 0.417 |
BED41_06005 | dnaX | BED41_06005 | BED41_06580 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA polymerase III, subunit gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. | 0.557 |
BED41_06005 | ftsH | BED41_06005 | BED41_06940 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.436 |
BED41_06005 | metG | BED41_06005 | BED41_05985 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.893 |
BED41_06005 | obg | BED41_06005 | BED41_07690 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | GTP-binding protein CgtA; An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | 0.481 |
BED41_06005 | tgt | BED41_06005 | BED41_06010 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | tRNA guanosine(34) transglycosylase Tgt; 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 t [...] | 0.822 |
BED41_06005 | tpiA | BED41_06005 | BED41_07660 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | Triose-phosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. | 0.437 |
BED41_06005 | ychF | BED41_06005 | BED41_11645 | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | Redox-regulated ATPase YchF; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. | 0.603 |
aspS | BED41_06005 | BED41_12135 | BED41_06005 | aspartate--tRNA ligase; 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. | Phosphate starvation-inducible protein PhoH; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.417 |
aspS | dnaX | BED41_12135 | BED41_06580 | aspartate--tRNA ligase; 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. | DNA polymerase III, subunit gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. | 0.505 |
aspS | metG | BED41_12135 | BED41_05985 | aspartate--tRNA ligase; 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. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.700 |
aspS | obg | BED41_12135 | BED41_07690 | aspartate--tRNA ligase; 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. | GTP-binding protein CgtA; An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | 0.520 |
aspS | tgt | BED41_12135 | BED41_06010 | aspartate--tRNA ligase; 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. | tRNA guanosine(34) transglycosylase Tgt; 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 t [...] | 0.496 |