| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Krad_0002 | Krad_0490 | Krad_0002 | Krad_0490 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | 0.980 |
| Krad_0002 | Krad_1769 | Krad_0002 | Krad_1769 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | 0.922 |
| Krad_0002 | Krad_3215 | Krad_0002 | Krad_3215 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | KEGG: sco:SCO1739 putative DNA polymerase III, alpha chain; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein; Belongs to the DNA polymerase type-C family. DnaE2 subfamily. | 0.704 |
| Krad_0002 | Krad_3422 | Krad_0002 | Krad_3422 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III delta; KEGG: lxx:Lxx14720 DNA polymerase III, delta subunit. | 0.983 |
| Krad_0002 | Krad_4338 | Krad_0002 | Krad_4338 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: aau:AAur_4164 single-strand binding protein. | 0.454 |
| Krad_0002 | dinB | Krad_0002 | Krad_3213 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.812 |
| Krad_0002 | dnaX | Krad_0002 | Krad_0466 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | DNA polymerase III, subunits 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. | 0.980 |
| Krad_0002 | recA | Krad_0002 | Krad_1492 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.737 |
| Krad_0490 | Krad_0002 | Krad_0490 | Krad_0002 | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | 0.980 |
| Krad_0490 | Krad_1769 | Krad_0490 | Krad_1769 | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | 0.969 |
| Krad_0490 | Krad_3215 | Krad_0490 | Krad_3215 | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | KEGG: sco:SCO1739 putative DNA polymerase III, alpha chain; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein; Belongs to the DNA polymerase type-C family. DnaE2 subfamily. | 0.712 |
| Krad_0490 | Krad_3422 | Krad_0490 | Krad_3422 | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III delta; KEGG: lxx:Lxx14720 DNA polymerase III, delta subunit. | 0.991 |
| Krad_0490 | Krad_4338 | Krad_0490 | Krad_4338 | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: aau:AAur_4164 single-strand binding protein. | 0.825 |
| Krad_0490 | dnaX | Krad_0490 | Krad_0466 | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | DNA polymerase III, subunits 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. | 0.923 |
| Krad_1577 | Krad_3215 | Krad_1577 | Krad_3215 | KEGG: tfu:Tfu_2899 hypothetical protein. | KEGG: sco:SCO1739 putative DNA polymerase III, alpha chain; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein; Belongs to the DNA polymerase type-C family. DnaE2 subfamily. | 0.762 |
| Krad_1769 | Krad_0002 | Krad_1769 | Krad_0002 | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | 0.922 |
| Krad_1769 | Krad_0490 | Krad_1769 | Krad_0490 | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | TIGRFAM: DNA polymerase III, delta prime subunit; SMART: AAA ATPase. | 0.969 |
| Krad_1769 | Krad_3215 | Krad_1769 | Krad_3215 | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | KEGG: sco:SCO1739 putative DNA polymerase III, alpha chain; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein; Belongs to the DNA polymerase type-C family. DnaE2 subfamily. | 0.704 |
| Krad_1769 | Krad_3422 | Krad_1769 | Krad_3422 | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III delta; KEGG: lxx:Lxx14720 DNA polymerase III, delta subunit. | 0.977 |
| Krad_1769 | dinB | Krad_1769 | Krad_3213 | TIGRFAM: DNA polymerase III, beta subunit; PFAM: DNA polymerase III beta chain; KEGG: aau:AAur_0002 DNA polymerase III, beta subunit. | DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.812 |