| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Apre_0002 | Apre_0675 | Apre_0002 | Apre_0675 | 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: sat:SYN_00896 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein. | 0.993 |
| Apre_0002 | Apre_0760 | Apre_0002 | Apre_0760 | 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: rod shape-determining protein RodA; PFAM: cell cycle protein; KEGG: wbm:Wbm0015 cell division membrane protein, FtsW; Belongs to the SEDS family. | 0.444 |
| Apre_0002 | Apre_0875 | Apre_0002 | Apre_0875 | 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: cell cycle protein; KEGG: bcy:Bcer98_2561 stage V sporulation protein E; Belongs to the SEDS family. | 0.531 |
| Apre_0002 | dinB | Apre_0002 | Apre_0224 | 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. | 0.967 |
| Apre_0002 | polA | Apre_0002 | Apre_1330 | 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. | 0.994 |
| Apre_0002 | recA | Apre_0002 | Apre_0618 | 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. | 0.832 |
| Apre_0222 | dinB | Apre_0222 | Apre_0224 | PFAM: protein of unknown function DUF955; KEGG: bcu:BCAH820_0553 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. | 0.622 |
| Apre_0675 | Apre_0002 | Apre_0675 | Apre_0002 | KEGG: sat:SYN_00896 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; 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 |
| Apre_0675 | dinB | Apre_0675 | Apre_0224 | KEGG: sat:SYN_00896 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP 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. | 0.556 |
| Apre_0675 | polA | Apre_0675 | Apre_1330 | KEGG: sat:SYN_00896 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.618 |
| Apre_0675 | recA | Apre_0675 | Apre_0618 | KEGG: sat:SYN_00896 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; 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. | 0.480 |
| Apre_0760 | Apre_0002 | Apre_0760 | Apre_0002 | TIGRFAM: rod shape-determining protein RodA; PFAM: cell cycle protein; KEGG: wbm:Wbm0015 cell division membrane protein, FtsW; Belongs to the SEDS family. | 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 [...] | 0.444 |
| Apre_0760 | dinB | Apre_0760 | Apre_0224 | TIGRFAM: rod shape-determining protein RodA; PFAM: cell cycle protein; KEGG: wbm:Wbm0015 cell division membrane protein, FtsW; 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. | 0.599 |
| Apre_0797 | dinB | Apre_0797 | Apre_0224 | Transcriptional regulator, XRE family; PFAM: helix-turn-helix domain protein; peptidase S24 and S26 domain protein; SMART: helix-turn-helix domain protein; KEGG: bce:BC3704 LexA repressor. | 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. | 0.757 |
| Apre_0797 | polA | Apre_0797 | Apre_1330 | Transcriptional regulator, XRE family; PFAM: helix-turn-helix domain protein; peptidase S24 and S26 domain protein; SMART: helix-turn-helix domain protein; KEGG: bce:BC3704 LexA repressor. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.428 |
| Apre_0797 | recA | Apre_0797 | Apre_0618 | Transcriptional regulator, XRE family; PFAM: helix-turn-helix domain protein; peptidase S24 and S26 domain protein; SMART: helix-turn-helix domain protein; KEGG: bce:BC3704 LexA repressor. | 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. | 0.975 |
| Apre_0875 | Apre_0002 | Apre_0875 | Apre_0002 | PFAM: cell cycle protein; KEGG: bcy:Bcer98_2561 stage V sporulation protein E; Belongs to the SEDS family. | 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 [...] | 0.531 |
| Apre_0875 | dinB | Apre_0875 | Apre_0224 | PFAM: cell cycle protein; KEGG: bcy:Bcer98_2561 stage V sporulation protein E; 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. | 0.599 |
| Apre_1042 | Apre_1063 | Apre_1042 | Apre_1063 | TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: eca:ECA2957 pyruvate-flavodoxin oxidoreductase. | TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: dal:Dalk_4144 pyruvate flavodoxin/ferredoxin oxidoreductase domain protein. | 0.999 |
| Apre_1042 | dinB | Apre_1042 | Apre_0224 | TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: eca:ECA2957 pyruvate-flavodoxin oxidoreductase. | 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. | 0.894 |