| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bsel_0002 | Bsel_1344 | Bsel_0002 | Bsel_1344 | 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, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | 0.993 |
| Bsel_0002 | Bsel_1957 | Bsel_0002 | Bsel_1957 | 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: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | 0.991 |
| Bsel_0002 | Bsel_2020 | Bsel_0002 | Bsel_2020 | 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: geo:Geob_3171 DNA-directed DNA polymerase; PFAM: UMUC domain protein DNA-repair protein; Belongs to the DNA polymerase type-Y family. | 0.906 |
| Bsel_0002 | dinG | Bsel_0002 | Bsel_2099 | 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 [...] | DnaQ family exonuclease/DinG family helicase; 3'-5' exonuclease. | 0.810 |
| Bsel_0002 | polA | Bsel_0002 | Bsel_1359 | 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 I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.993 |
| Bsel_0002 | recA | Bsel_0002 | Bsel_1811 | 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. | 0.842 |
| Bsel_0002 | topA | Bsel_0002 | Bsel_1733 | 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 topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.631 |
| Bsel_1344 | Bsel_0002 | Bsel_1344 | Bsel_0002 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | 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 [...] | 0.993 |
| Bsel_1344 | Bsel_1957 | Bsel_1344 | Bsel_1957 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | 0.708 |
| Bsel_1344 | Bsel_2020 | Bsel_1344 | Bsel_2020 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | KEGG: geo:Geob_3171 DNA-directed DNA polymerase; PFAM: UMUC domain protein DNA-repair protein; Belongs to the DNA polymerase type-Y family. | 0.591 |
| Bsel_1344 | dinG | Bsel_1344 | Bsel_2099 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | DnaQ family exonuclease/DinG family helicase; 3'-5' exonuclease. | 0.510 |
| Bsel_1344 | polA | Bsel_1344 | Bsel_1359 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.743 |
| Bsel_1344 | recA | Bsel_1344 | Bsel_1811 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | 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. | 0.553 |
| Bsel_1344 | topA | Bsel_1344 | Bsel_1733 | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.526 |
| Bsel_1957 | Bsel_0002 | Bsel_1957 | Bsel_0002 | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | 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 [...] | 0.991 |
| Bsel_1957 | Bsel_1344 | Bsel_1957 | Bsel_1344 | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sfu:Sfum_1225 DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein. | 0.708 |
| Bsel_1957 | Bsel_2020 | Bsel_1957 | Bsel_2020 | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | KEGG: geo:Geob_3171 DNA-directed DNA polymerase; PFAM: UMUC domain protein DNA-repair protein; Belongs to the DNA polymerase type-Y family. | 0.626 |
| Bsel_1957 | Bsel_2021 | Bsel_1957 | Bsel_2021 | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | SMART: GGDEF domain containing protein; response regulator receiver; TIGRFAM: diguanylate cyclase; KEGG: maq:Maqu_3442 response regulator receiver modulated diguanylate cyclase; PFAM: GGDEF domain containing protein; response regulator receiver. | 0.453 |
| Bsel_1957 | dinG | Bsel_1957 | Bsel_2099 | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | DnaQ family exonuclease/DinG family helicase; 3'-5' exonuclease. | 0.898 |
| Bsel_1957 | lexA | Bsel_1957 | Bsel_1832 | KEGG: geo:Geob_2372 ribonuclease H; PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2. | Transcriptional repressor, LexA family; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | 0.419 |