node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABY94235.1 | ABY94236.1 | Teth39_0571 | Teth39_0572 | FHA domain containing protein; PFAM: Forkhead-associated protein. | PFAM: cell cycle protein; Belongs to the SEDS family. | 0.932 |
ABY94235.1 | ABY94237.1 | Teth39_0571 | Teth39_0573 | FHA domain containing protein; PFAM: Forkhead-associated protein. | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | 0.919 |
ABY94235.1 | uvrA | Teth39_0571 | Teth39_0570 | FHA domain containing protein; PFAM: Forkhead-associated protein. | Excinuclease ABC, A subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.809 |
ABY94235.1 | uvrB | Teth39_0571 | Teth39_0569 | FHA domain containing protein; PFAM: Forkhead-associated protein. | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.801 |
ABY94235.1 | uvrC | Teth39_0571 | Teth39_0574 | FHA domain containing protein; PFAM: Forkhead-associated protein. | Excinuclease ABC, C subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.766 |
ABY94236.1 | ABY94235.1 | Teth39_0572 | Teth39_0571 | PFAM: cell cycle protein; Belongs to the SEDS family. | FHA domain containing protein; PFAM: Forkhead-associated protein. | 0.932 |
ABY94236.1 | ABY94237.1 | Teth39_0572 | Teth39_0573 | PFAM: cell cycle protein; Belongs to the SEDS family. | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | 0.997 |
ABY94236.1 | polA | Teth39_0572 | Teth39_1474 | 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. | 0.443 |
ABY94236.1 | uvrA | Teth39_0572 | Teth39_0570 | PFAM: cell cycle protein; Belongs to the SEDS family. | Excinuclease ABC, A subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.797 |
ABY94236.1 | uvrB | Teth39_0572 | Teth39_0569 | PFAM: cell cycle protein; Belongs to the SEDS family. | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.788 |
ABY94236.1 | uvrC | Teth39_0572 | Teth39_0574 | PFAM: cell cycle protein; Belongs to the SEDS family. | Excinuclease ABC, C subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.783 |
ABY94237.1 | ABY94235.1 | Teth39_0573 | Teth39_0571 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | FHA domain containing protein; PFAM: Forkhead-associated protein. | 0.919 |
ABY94237.1 | ABY94236.1 | Teth39_0573 | Teth39_0572 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | PFAM: cell cycle protein; Belongs to the SEDS family. | 0.997 |
ABY94237.1 | uvrA | Teth39_0573 | Teth39_0570 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | Excinuclease ABC, A subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.778 |
ABY94237.1 | uvrB | Teth39_0573 | Teth39_0569 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.764 |
ABY94237.1 | uvrC | Teth39_0573 | Teth39_0574 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase. | Excinuclease ABC, C subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.772 |
ABY94579.1 | mfd | Teth39_0924 | Teth39_0169 | PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily. | 0.492 |
ABY94579.1 | mutL | Teth39_0924 | Teth39_1175 | PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. | 0.922 |
ABY94579.1 | polA | Teth39_0924 | Teth39_1474 | PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.966 |
ABY94579.1 | topA | Teth39_0924 | Teth39_1264 | PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | 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 [...] | 0.987 |