node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Snov_0577 | Snov_1771 | Snov_0577 | Snov_1771 | 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: azc:AZC_2174 putative DNA polymerase III delta prime subunit. | 0.996 |
Snov_0577 | Snov_3144 | Snov_0577 | Snov_3144 | 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: azc:AZC_4554 cell division protein precursor; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; Belongs to the SEDS family. | 0.625 |
Snov_0577 | Snov_4502 | Snov_0577 | Snov_4502 | 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 [...] | SMART: DNA polymerase III beta chain; TIGRFAM: DNA polymerase III, beta subunit; KEGG: mrd:Mrad2831_2239 DNA polymerase III subunit beta; PFAM: DNA polymerase III beta chain. | 0.923 |
Snov_0577 | dinB | Snov_0577 | Snov_1504 | 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. | 0.899 |
Snov_0577 | lexA | Snov_0577 | Snov_1822 | 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 [...] | 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. | 0.415 |
Snov_0577 | polA | Snov_0577 | Snov_3875 | 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. | 0.997 |
Snov_0577 | recA | Snov_0577 | Snov_2163 | 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. | 0.717 |
Snov_1505 | dinB | Snov_1505 | Snov_1504 | KEGG: xau:Xaut_3858 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. | 0.733 |
Snov_1771 | Snov_0577 | Snov_1771 | Snov_0577 | KEGG: azc:AZC_2174 putative DNA polymerase III delta prime subunit. | 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 [...] | 0.996 |
Snov_1771 | Snov_4502 | Snov_1771 | Snov_4502 | KEGG: azc:AZC_2174 putative DNA polymerase III delta prime subunit. | SMART: DNA polymerase III beta chain; TIGRFAM: DNA polymerase III, beta subunit; KEGG: mrd:Mrad2831_2239 DNA polymerase III subunit beta; PFAM: DNA polymerase III beta chain. | 0.996 |
Snov_1771 | dinB | Snov_1771 | Snov_1504 | KEGG: azc:AZC_2174 putative DNA polymerase III delta prime subunit. | 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. | 0.751 |
Snov_1771 | polA | Snov_1771 | Snov_3875 | KEGG: azc:AZC_2174 putative DNA polymerase III delta prime subunit. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.948 |
Snov_1771 | recA | Snov_1771 | Snov_2163 | KEGG: azc:AZC_2174 putative DNA polymerase III delta prime subunit. | 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. | 0.722 |
Snov_3144 | Snov_0577 | Snov_3144 | Snov_0577 | KEGG: azc:AZC_4554 cell division protein precursor; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; 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 [...] | 0.625 |
Snov_3144 | dinB | Snov_3144 | Snov_1504 | KEGG: azc:AZC_4554 cell division protein precursor; 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. | 0.702 |
Snov_3144 | lexA | Snov_3144 | Snov_1822 | KEGG: azc:AZC_4554 cell division protein precursor; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; Belongs to the SEDS family. | 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. | 0.408 |
Snov_3144 | polA | Snov_3144 | Snov_3875 | KEGG: azc:AZC_4554 cell division protein precursor; 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; Belongs to the DNA polymerase type-A family. | 0.506 |
Snov_4045 | dinB | Snov_4045 | Snov_1504 | TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; Ada metal-binding domain protein; KEGG: sit:TM1040_2682 DNA-O6-methylguanine--protein-cysteine S-methyltransferase. | 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. | 0.621 |
Snov_4045 | lexA | Snov_4045 | Snov_1822 | TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; Ada metal-binding domain protein; KEGG: sit:TM1040_2682 DNA-O6-methylguanine--protein-cysteine S-methyltransferase. | 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. | 0.454 |
Snov_4045 | polA | Snov_4045 | Snov_3875 | TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; Ada metal-binding domain protein; KEGG: sit:TM1040_2682 DNA-O6-methylguanine--protein-cysteine S-methyltransferase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.665 |