| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EHA62023.1 | EHA62024.1 | Syn8016DRAFT_2095 | Syn8016DRAFT_2096 | PFAM: Domain of unknown function DUF404; Domain of unknown function DUF407; KEGG: pme:NATL1_15711 hypothetical protein. | PFAM: Domain of unknown function DUF403; KEGG: pmn:PMN2A_0732 hypothetical protein. | 0.997 |
| EHA62023.1 | EHA62025.1 | Syn8016DRAFT_2095 | Syn8016DRAFT_2097 | PFAM: Domain of unknown function DUF404; Domain of unknown function DUF407; KEGG: pme:NATL1_15711 hypothetical protein. | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | 0.965 |
| EHA62024.1 | EHA62023.1 | Syn8016DRAFT_2096 | Syn8016DRAFT_2095 | PFAM: Domain of unknown function DUF403; KEGG: pmn:PMN2A_0732 hypothetical protein. | PFAM: Domain of unknown function DUF404; Domain of unknown function DUF407; KEGG: pme:NATL1_15711 hypothetical protein. | 0.997 |
| EHA62024.1 | EHA62025.1 | Syn8016DRAFT_2096 | Syn8016DRAFT_2097 | PFAM: Domain of unknown function DUF403; KEGG: pmn:PMN2A_0732 hypothetical protein. | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | 0.965 |
| EHA62025.1 | EHA62023.1 | Syn8016DRAFT_2097 | Syn8016DRAFT_2095 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | PFAM: Domain of unknown function DUF404; Domain of unknown function DUF407; KEGG: pme:NATL1_15711 hypothetical protein. | 0.965 |
| EHA62025.1 | EHA62024.1 | Syn8016DRAFT_2097 | Syn8016DRAFT_2096 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | PFAM: Domain of unknown function DUF403; KEGG: pmn:PMN2A_0732 hypothetical protein. | 0.965 |
| EHA62025.1 | EHA64296.1 | Syn8016DRAFT_2097 | Syn8016DRAFT_1339 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.710 |
| EHA62025.1 | guaA | Syn8016DRAFT_2097 | Syn8016DRAFT_2868 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.898 |
| EHA62025.1 | ruvA | Syn8016DRAFT_2097 | Syn8016DRAFT_0741 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | Holliday junction ATP-dependent DNA helicase ruvA; 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. | 0.710 |
| EHA62025.1 | ruvB | Syn8016DRAFT_2097 | Syn8016DRAFT_1734 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | Holliday junction ATP-dependent DNA helicase ruvB; 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. | 0.710 |
| EHA62025.1 | surE | Syn8016DRAFT_2097 | Syn8016DRAFT_2929 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | Multifunctional protein surE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.663 |
| EHA62025.1 | uvrA | Syn8016DRAFT_2097 | Syn8016DRAFT_2818 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | UvrABC system protein A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.718 |
| EHA62025.1 | uvrB | Syn8016DRAFT_2097 | Syn8016DRAFT_2894 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | 0.724 |
| EHA62025.1 | uvrC | Syn8016DRAFT_2097 | Syn8016DRAFT_0438 | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | UvrABC system protein C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.739 |
| EHA64296.1 | EHA62025.1 | Syn8016DRAFT_1339 | Syn8016DRAFT_2097 | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | KEGG: pmm:PMM1040 transglutaminase-like superfamily protein; PFAM: Bacterial transglutaminase-like, N-terminal; Transglutaminase-like; SMART: Transglutaminase-like. | 0.710 |
| EHA64296.1 | ruvA | Syn8016DRAFT_1339 | Syn8016DRAFT_0741 | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | Holliday junction ATP-dependent DNA helicase ruvA; 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. | 0.929 |
| EHA64296.1 | ruvB | Syn8016DRAFT_1339 | Syn8016DRAFT_1734 | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | Holliday junction ATP-dependent DNA helicase ruvB; 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. | 0.929 |
| EHA64296.1 | uvrA | Syn8016DRAFT_1339 | Syn8016DRAFT_2818 | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | UvrABC system protein A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.929 |
| EHA64296.1 | uvrB | Syn8016DRAFT_1339 | Syn8016DRAFT_2894 | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] | 0.929 |
| EHA64296.1 | uvrC | Syn8016DRAFT_1339 | Syn8016DRAFT_0438 | Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | UvrABC system protein C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.933 |