node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Sthe_0458 | Sthe_1383 | Sthe_0458 | Sthe_1383 | KEGG: cur:cur_1297 hypothetical protein. | TIGRFAM: single-stranded-DNA-specific exonuclease RecJ; PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1; KEGG: cau:Caur_1134 single-stranded-DNA-specific exonuclease RecJ. | 0.473 |
Sthe_0458 | Sthe_1450 | Sthe_0458 | Sthe_1450 | KEGG: cur:cur_1297 hypothetical protein. | TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: cau:Caur_0870 single-strand binding protein. | 0.770 |
Sthe_0458 | dinG | Sthe_0458 | Sthe_1001 | KEGG: cur:cur_1297 hypothetical protein. | Exonuclease RNase T and DNA polymerase III; 3'-5' exonuclease. | 0.587 |
Sthe_0458 | polA | Sthe_0458 | Sthe_1591 | KEGG: cur:cur_1297 hypothetical protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.726 |
Sthe_0458 | topA | Sthe_0458 | Sthe_0383 | KEGG: cur:cur_1297 hypothetical 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 [...] | 0.856 |
Sthe_0516 | Sthe_1312 | Sthe_0516 | Sthe_1312 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | 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 [...] | 0.997 |
Sthe_0516 | Sthe_2045 | Sthe_0516 | Sthe_2045 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | DNA-directed DNA polymerase; PFAM: UMUC domain protein DNA-repair protein; KEGG: dau:Daud_0758 DNA-directed DNA polymerase. | 0.870 |
Sthe_0516 | dinB | Sthe_0516 | Sthe_2042 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | 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. | 0.870 |
Sthe_0516 | dinG | Sthe_0516 | Sthe_1001 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | Exonuclease RNase T and DNA polymerase III; 3'-5' exonuclease. | 0.923 |
Sthe_0516 | polA | Sthe_0516 | Sthe_1591 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.997 |
Sthe_0516 | recA | Sthe_0516 | Sthe_0924 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | 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. | 0.859 |
Sthe_0516 | topA | Sthe_0516 | Sthe_0383 | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | 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 [...] | 0.608 |
Sthe_1312 | Sthe_0516 | Sthe_1312 | Sthe_0516 | 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 [...] | PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B; KEGG: gsu:GSU3245 DNA polymerase II, putative. | 0.997 |
Sthe_1312 | Sthe_1383 | Sthe_1312 | Sthe_1383 | 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-stranded-DNA-specific exonuclease RecJ; PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1; KEGG: cau:Caur_1134 single-stranded-DNA-specific exonuclease RecJ. | 0.553 |
Sthe_1312 | Sthe_1450 | Sthe_1312 | Sthe_1450 | 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: cau:Caur_0870 single-strand binding protein. | 0.661 |
Sthe_1312 | Sthe_2045 | Sthe_1312 | Sthe_2045 | 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; PFAM: UMUC domain protein DNA-repair protein; KEGG: dau:Daud_0758 DNA-directed DNA polymerase. | 0.876 |
Sthe_1312 | Sthe_2148 | Sthe_1312 | Sthe_2148 | 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 repair protein RecN; May be involved in recombinational repair of damaged DNA. | 0.422 |
Sthe_1312 | dinB | Sthe_1312 | Sthe_2042 | 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. | 0.876 |
Sthe_1312 | dinG | Sthe_1312 | Sthe_1001 | 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 [...] | Exonuclease RNase T and DNA polymerase III; 3'-5' exonuclease. | 0.957 |
Sthe_1312 | lexA | Sthe_1312 | Sthe_1705 | 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 [...] | SOS-response transcriptional repressor, LexA; 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. | 0.494 |