| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO46281.1 | ADO49906.1 | Entcl_0002 | Entcl_3665 | 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: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | 0.983 |
| ADO46281.1 | dinB | Entcl_0002 | Entcl_3482 | 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. | 0.901 |
| ADO46281.1 | polA | Entcl_0002 | Entcl_4391 | 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; Belongs to the DNA polymerase type-A family. | 0.986 |
| ADO46281.1 | recA | Entcl_0002 | Entcl_1028 | 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. | 0.839 |
| ADO47765.1 | dinB | Entcl_1504 | Entcl_3482 | Transcriptional regulator, AraC family; TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; Ada metal-binding domain-containing protein; helix-turn-helix- domain containing protein AraC type; methylguanine DNA methyltransferase ribonuclease domain protein; KEGG: ecc:c2754 ADA regulatory protein; SMART: Helix-turn-helix, AraC domain. | 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. | 0.650 |
| ADO47765.1 | polA | Entcl_1504 | Entcl_4391 | Transcriptional regulator, AraC family; TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; Ada metal-binding domain-containing protein; helix-turn-helix- domain containing protein AraC type; methylguanine DNA methyltransferase ribonuclease domain protein; KEGG: ecc:c2754 ADA regulatory protein; SMART: Helix-turn-helix, AraC domain. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.622 |
| ADO47765.1 | recA | Entcl_1504 | Entcl_1028 | Transcriptional regulator, AraC family; TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; Ada metal-binding domain-containing protein; helix-turn-helix- domain containing protein AraC type; methylguanine DNA methyltransferase ribonuclease domain protein; KEGG: ecc:c2754 ADA regulatory protein; SMART: Helix-turn-helix, AraC domain. | 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. | 0.599 |
| ADO48140.1 | dinB | Entcl_1884 | Entcl_3482 | Peptidase S24/S26A/S26B, conserved region; KEGG: cko:CKO_01842 DNA polymerase V subunit UmuD; manually curated; PFAM: Peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 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. | 0.782 |
| ADO48140.1 | polA | Entcl_1884 | Entcl_4391 | Peptidase S24/S26A/S26B, conserved region; KEGG: cko:CKO_01842 DNA polymerase V subunit UmuD; manually curated; PFAM: Peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.408 |
| ADO48140.1 | recA | Entcl_1884 | Entcl_1028 | Peptidase S24/S26A/S26B, conserved region; KEGG: cko:CKO_01842 DNA polymerase V subunit UmuD; manually curated; PFAM: Peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 family. | 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. | 0.915 |
| ADO48371.1 | dinB | Entcl_2117 | Entcl_3482 | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: stm:STM1998 DNA polymerase V subunit UmuD; Belongs to the peptidase S24 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. | 0.782 |
| ADO48371.1 | polA | Entcl_2117 | Entcl_4391 | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: stm:STM1998 DNA polymerase V subunit UmuD; Belongs to the peptidase S24 family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.408 |
| ADO48371.1 | recA | Entcl_2117 | Entcl_1028 | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: stm:STM1998 DNA polymerase V subunit UmuD; Belongs to the peptidase S24 family. | 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. | 0.915 |
| ADO48687.1 | dinB | Entcl_2436 | Entcl_3482 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing 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. | 0.762 |
| ADO48687.1 | polA | Entcl_2436 | Entcl_4391 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing 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. | 0.469 |
| ADO48687.1 | recA | Entcl_2436 | Entcl_1028 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing 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. | 0.660 |
| ADO49906.1 | ADO46281.1 | Entcl_3665 | Entcl_0002 | KEGG: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | 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 [...] | 0.983 |
| ADO49906.1 | dinB | Entcl_3665 | Entcl_3482 | KEGG: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | 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. | 0.801 |
| ADO49906.1 | lexA | Entcl_3665 | Entcl_4125 | KEGG: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | Transcriptional repressor, LexA family; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. 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. | 0.424 |
| ADO49906.1 | polA | Entcl_3665 | Entcl_4391 | KEGG: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.903 |