| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Meso_0301 | queA | Meso_0301 | Meso_1405 | PFAM: flagellar basal body rod protein protein of unknown function DUF1078-like; KEGG: mlo:mlr2907 flagellar basal-body rod protein flgF. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.531 |
| Meso_0301 | tgt | Meso_0301 | Meso_1406 | PFAM: flagellar basal body rod protein protein of unknown function DUF1078-like; KEGG: mlo:mlr2907 flagellar basal-body rod protein flgF. | tRNA-guanine transglycosylase; 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 the [...] | 0.531 |
| Meso_1403 | Meso_1404 | Meso_1403 | Meso_1404 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.793 |
| Meso_1403 | coaD | Meso_1403 | Meso_1402 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.813 |
| Meso_1403 | queA | Meso_1403 | Meso_1405 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.571 |
| Meso_1403 | tgt | Meso_1403 | Meso_1406 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | tRNA-guanine transglycosylase; 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 the [...] | 0.573 |
| Meso_1404 | Meso_1403 | Meso_1404 | Meso_1403 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.793 |
| Meso_1404 | coaD | Meso_1404 | Meso_1402 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.762 |
| Meso_1404 | queA | Meso_1404 | Meso_1405 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.679 |
| Meso_1404 | tgt | Meso_1404 | Meso_1406 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | tRNA-guanine transglycosylase; 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 the [...] | 0.681 |
| Meso_3418 | queA | Meso_3418 | Meso_1405 | PFAM: Fmu (Sun) NusB/RsmB/TIM44; KEGG: mlo:mlr4098 hypothetical protein, similarity to RNA-binding Sun protein, putative Fmu protein; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.547 |
| Meso_3418 | rlmN | Meso_3418 | Meso_2859 | PFAM: Fmu (Sun) NusB/RsmB/TIM44; KEGG: mlo:mlr4098 hypothetical protein, similarity to RNA-binding Sun protein, putative Fmu protein; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 23S rRNA m(2)A-2503 methyltransferase; 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. | 0.921 |
| Meso_3418 | tgt | Meso_3418 | Meso_1406 | PFAM: Fmu (Sun) NusB/RsmB/TIM44; KEGG: mlo:mlr4098 hypothetical protein, similarity to RNA-binding Sun protein, putative Fmu protein; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | tRNA-guanine transglycosylase; 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 the [...] | 0.524 |
| Meso_3418 | truB | Meso_3418 | Meso_3932 | PFAM: Fmu (Sun) NusB/RsmB/TIM44; KEGG: mlo:mlr4098 hypothetical protein, similarity to RNA-binding Sun protein, putative Fmu protein; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 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. | 0.886 |
| coaD | Meso_1403 | Meso_1402 | Meso_1403 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.813 |
| coaD | Meso_1404 | Meso_1402 | Meso_1404 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.762 |
| coaD | queA | Meso_1402 | Meso_1405 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.648 |
| coaD | secF | Meso_1402 | Meso_1796 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Protein translocase subunit secD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.419 |
| coaD | tgt | Meso_1402 | Meso_1406 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | tRNA-guanine transglycosylase; 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 the [...] | 0.572 |
| queA | Meso_0301 | Meso_1405 | Meso_0301 | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | PFAM: flagellar basal body rod protein protein of unknown function DUF1078-like; KEGG: mlo:mlr2907 flagellar basal-body rod protein flgF. | 0.531 |
