node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AEV28016.1 | AEV28254.1 | SpiGrapes_0152 | SpiGrapes_0396 | PFAM: Uroporphyrinogen decarboxylase (URO-D); Belongs to the uroporphyrinogen decarboxylase family. | Putative oxygen-independent 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. | 0.929 |
AEV28229.1 | AEV28254.1 | SpiGrapes_0371 | SpiGrapes_0396 | tRNA-N(6)-(isopentenyl)adenosine-37 thiotransferase enzyme MiaB; 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. | Putative oxygen-independent 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. | 0.693 |
AEV28229.1 | AEV30454.1 | SpiGrapes_0371 | SpiGrapes_2696 | tRNA-N(6)-(isopentenyl)adenosine-37 thiotransferase enzyme MiaB; 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. | 23S rRNA m2A2503 methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | 0.713 |
AEV28253.1 | AEV28254.1 | SpiGrapes_0395 | SpiGrapes_0396 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | Putative oxygen-independent 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. | 0.795 |
AEV28253.1 | AEV28255.1 | SpiGrapes_0395 | SpiGrapes_0397 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | 0.633 |
AEV28253.1 | queA | SpiGrapes_0395 | SpiGrapes_0401 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.597 |
AEV28253.1 | ruvA | SpiGrapes_0395 | SpiGrapes_0399 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | Holliday junction DNA helicase, RuvA subunit; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.582 |
AEV28253.1 | ruvB | SpiGrapes_0395 | SpiGrapes_0400 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | Holliday junction DNA helicase, RuvB subunit; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | 0.620 |
AEV28253.1 | ruvC | SpiGrapes_0395 | SpiGrapes_0398 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | Holliday junction resolvasome, endonuclease subunit; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.632 |
AEV28253.1 | smpB | SpiGrapes_0395 | SpiGrapes_0393 | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...] | 0.597 |
AEV28254.1 | AEV28016.1 | SpiGrapes_0396 | SpiGrapes_0152 | Putative oxygen-independent 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. | PFAM: Uroporphyrinogen decarboxylase (URO-D); Belongs to the uroporphyrinogen decarboxylase family. | 0.929 |
AEV28254.1 | AEV28229.1 | SpiGrapes_0396 | SpiGrapes_0371 | Putative oxygen-independent 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. | tRNA-N(6)-(isopentenyl)adenosine-37 thiotransferase enzyme MiaB; 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. | 0.693 |
AEV28254.1 | AEV28253.1 | SpiGrapes_0396 | SpiGrapes_0395 | Putative oxygen-independent 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. | PFAM: Peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family. | 0.795 |
AEV28254.1 | AEV28255.1 | SpiGrapes_0396 | SpiGrapes_0397 | Putative oxygen-independent 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. | PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | 0.607 |
AEV28254.1 | AEV30454.1 | SpiGrapes_0396 | SpiGrapes_2696 | Putative oxygen-independent 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. | 23S rRNA m2A2503 methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | 0.711 |
AEV28254.1 | queA | SpiGrapes_0396 | SpiGrapes_0401 | Putative oxygen-independent 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. | S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.683 |
AEV28254.1 | ruvA | SpiGrapes_0396 | SpiGrapes_0399 | Putative oxygen-independent 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. | Holliday junction DNA helicase, RuvA subunit; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.597 |
AEV28254.1 | ruvB | SpiGrapes_0396 | SpiGrapes_0400 | Putative oxygen-independent 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. | Holliday junction DNA helicase, RuvB subunit; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | 0.597 |
AEV28254.1 | ruvC | SpiGrapes_0396 | SpiGrapes_0398 | Putative oxygen-independent 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. | Holliday junction resolvasome, endonuclease subunit; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.597 |
AEV28254.1 | smpB | SpiGrapes_0396 | SpiGrapes_0393 | Putative oxygen-independent 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. | SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...] | 0.607 |