| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADQ03622.1 | ADQ04616.1 | Calow_0002 | Calow_1053 | 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, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: ate:Athe_1262 DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type. | 0.990 |
| ADQ03622.1 | dinB | Calow_0002 | Calow_2016 | 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. | 0.962 |
| ADQ03622.1 | polA | Calow_0002 | Calow_1220 | 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. | 0.990 |
| ADQ03622.1 | recA | Calow_0002 | Calow_0770 | 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. | 0.923 |
| ADQ03622.1 | topA | Calow_0002 | Calow_1871 | 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 [...] | 0.761 |
| ADQ04198.1 | dinB | Calow_0622 | Calow_2016 | KEGG: ate:Athe_0777 cell division protein FtsW; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; Belongs to the SEDS family. | 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. | 0.779 |
| ADQ04198.1 | polA | Calow_0622 | Calow_1220 | KEGG: ate:Athe_0777 cell division protein FtsW; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; Belongs to the SEDS family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.414 |
| ADQ04376.1 | dinB | Calow_0808 | Calow_2016 | Transcriptional regulator, XRE family; KEGG: afl:Aflv_0637 SOS-response transcriptional repressor LexA (HTH, RecA-mediated autopeptidase); PFAM: helix-turn-helix domain protein; Peptidase S24/S26A/S26B, conserved region; SMART: helix-turn-helix domain protein. | 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. | 0.877 |
| ADQ04376.1 | polA | Calow_0808 | Calow_1220 | Transcriptional regulator, XRE family; KEGG: afl:Aflv_0637 SOS-response transcriptional repressor LexA (HTH, RecA-mediated autopeptidase); PFAM: helix-turn-helix domain protein; Peptidase S24/S26A/S26B, conserved region; SMART: helix-turn-helix domain protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.427 |
| ADQ04376.1 | recA | Calow_0808 | Calow_0770 | Transcriptional regulator, XRE family; KEGG: afl:Aflv_0637 SOS-response transcriptional repressor LexA (HTH, RecA-mediated autopeptidase); PFAM: helix-turn-helix domain protein; Peptidase S24/S26A/S26B, conserved region; SMART: helix-turn-helix 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. | 0.963 |
| ADQ04376.1 | topA | Calow_0808 | Calow_1871 | Transcriptional regulator, XRE family; KEGG: afl:Aflv_0637 SOS-response transcriptional repressor LexA (HTH, RecA-mediated autopeptidase); PFAM: helix-turn-helix domain protein; Peptidase S24/S26A/S26B, conserved region; SMART: helix-turn-helix 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 [...] | 0.402 |
| ADQ04616.1 | ADQ03622.1 | Calow_1053 | Calow_0002 | DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: ate:Athe_1262 DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type. | 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 [...] | 0.990 |
| ADQ04616.1 | dinB | Calow_1053 | Calow_2016 | DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: ate:Athe_1262 DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type. | 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. | 0.686 |
| ADQ04616.1 | polA | Calow_1053 | Calow_1220 | DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: ate:Athe_1262 DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.759 |
| ADQ04616.1 | recA | Calow_1053 | Calow_0770 | DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: ate:Athe_1262 DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type. | 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. | 0.433 |
| ADQ04616.1 | topA | Calow_1053 | Calow_1871 | DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: ate:Athe_1262 DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type. | 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 [...] | 0.697 |
| ADQ05532.1 | dinB | Calow_2017 | Calow_2016 | KEGG: ate:Athe_2317 hypothetical protein. | 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. | 0.905 |
| dinB | ADQ03622.1 | Calow_2016 | Calow_0002 | 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. | 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 [...] | 0.962 |
| dinB | ADQ04198.1 | Calow_2016 | Calow_0622 | 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. | KEGG: ate:Athe_0777 cell division protein FtsW; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; Belongs to the SEDS family. | 0.779 |
| dinB | ADQ04376.1 | Calow_2016 | Calow_0808 | 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. | Transcriptional regulator, XRE family; KEGG: afl:Aflv_0637 SOS-response transcriptional repressor LexA (HTH, RecA-mediated autopeptidase); PFAM: helix-turn-helix domain protein; Peptidase S24/S26A/S26B, conserved region; SMART: helix-turn-helix domain protein. | 0.877 |