node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AEU34364.1 | AEU35711.1 | AciX8_0003 | AciX8_1368 | 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 ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | 0.877 |
AEU34364.1 | AEU36386.1 | AciX8_0003 | AciX8_2056 | 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: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | 0.988 |
AEU34364.1 | AEU37059.1 | AciX8_0003 | AciX8_2749 | 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: aca:ACP_1624 PHP domain protein; PFAM: PHP, C-terminal; SMART: DNA-directed DNA polymerase X; Helix-hairpin-helix DNA-binding motif, class 1; Polymerase/histidinol phosphatase, N-terminal. | 0.647 |
AEU34364.1 | polA | AciX8_0003 | AciX8_1033 | 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. | 0.993 |
AEU34364.1 | rpoA | AciX8_0003 | AciX8_1027 | 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 RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.473 |
AEU34364.1 | rpoB | AciX8_0003 | AciX8_0788 | 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 RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.575 |
AEU35711.1 | AEU34364.1 | AciX8_1368 | AciX8_0003 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small 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 [...] | 0.877 |
AEU35711.1 | AEU36386.1 | AciX8_1368 | AciX8_2056 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | 0.868 |
AEU35711.1 | AEU37059.1 | AciX8_1368 | AciX8_2749 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | KEGG: aca:ACP_1624 PHP domain protein; PFAM: PHP, C-terminal; SMART: DNA-directed DNA polymerase X; Helix-hairpin-helix DNA-binding motif, class 1; Polymerase/histidinol phosphatase, N-terminal. | 0.761 |
AEU35711.1 | ku | AciX8_1368 | AciX8_1369 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | Ku protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | 0.984 |
AEU35711.1 | polA | AciX8_1368 | AciX8_1033 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small 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. | 0.879 |
AEU35711.1 | rpoA | AciX8_1368 | AciX8_1027 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | DNA-directed RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.515 |
AEU35711.1 | rpoB | AciX8_1368 | AciX8_0788 | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.465 |
AEU36386.1 | AEU34364.1 | AciX8_2056 | AciX8_0003 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | 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 [...] | 0.988 |
AEU36386.1 | AEU35711.1 | AciX8_2056 | AciX8_1368 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | DNA ligase D; KEGG: aca:ACP_3506 putative DNA ligase, ATP-dependent; TIGRFAM: DNA ligase D; DNA polymerase LigD, polymerase domain; DNA polymerase LigD, ligase domain; DNA ligase D, 3'-phosphoesterase domain; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; DNA primase, small subunit. | 0.868 |
AEU36386.1 | AEU37059.1 | AciX8_2056 | AciX8_2749 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | KEGG: aca:ACP_1624 PHP domain protein; PFAM: PHP, C-terminal; SMART: DNA-directed DNA polymerase X; Helix-hairpin-helix DNA-binding motif, class 1; Polymerase/histidinol phosphatase, N-terminal. | 0.864 |
AEU36386.1 | AEU37164.1 | AciX8_2056 | AciX8_2861 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | WD40 repeat-containing protein; KEGG: bge:BC1002_1278 WD40 repeat, subgroup; PFAM: WD40 repeat, subgroup; SMART: WD40 repeat. | 0.929 |
AEU36386.1 | gpmI | AciX8_2056 | AciX8_1415 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. | 0.896 |
AEU36386.1 | ku | AciX8_2056 | AciX8_1369 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | Ku protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | 0.780 |
AEU36386.1 | ligA | AciX8_2056 | AciX8_4264 | TIGRFAM: DNA ligase, ATP-dependent; KEGG: aca:ACP_2652 DNA ligase, ATP-dependent; PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, N-terminal; DNA ligase, ATP-dependent, C-terminal. | DNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | 0.922 |