node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CNF33401.1 | CNF33477.1 | ERS008532_03504 | ERS008532_03506 | Lipoprotein. | Uncharacterized protein conserved in bacteria. | 0.454 |
CNF33401.1 | dapF | ERS008532_03504 | ERS008532_03505 | Lipoprotein. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.647 |
CNF33401.1 | xerC | ERS008532_03504 | ERS008532_03507 | Lipoprotein. | Site-specific tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifical [...] | 0.549 |
CNF33401.1 | yfnB | ERS008532_03504 | ERS008532_03508 | Lipoprotein. | Flavin mononucleotide phosphatase. | 0.401 |
CNF33477.1 | CNF33401.1 | ERS008532_03506 | ERS008532_03504 | Uncharacterized protein conserved in bacteria. | Lipoprotein. | 0.454 |
CNF33477.1 | dapF | ERS008532_03506 | ERS008532_03505 | Uncharacterized protein conserved in bacteria. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.926 |
CNF33477.1 | uvrD | ERS008532_03506 | ERS008532_03509 | Uncharacterized protein conserved in bacteria. | DNA-dependent helicase II. | 0.601 |
CNF33477.1 | xerC | ERS008532_03506 | ERS008532_03507 | Uncharacterized protein conserved in bacteria. | Site-specific tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifical [...] | 0.892 |
CNF33477.1 | yfnB | ERS008532_03506 | ERS008532_03508 | Uncharacterized protein conserved in bacteria. | Flavin mononucleotide phosphatase. | 0.808 |
dapF | CNF33401.1 | ERS008532_03505 | ERS008532_03504 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Lipoprotein. | 0.647 |
dapF | CNF33477.1 | ERS008532_03505 | ERS008532_03506 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Uncharacterized protein conserved in bacteria. | 0.926 |
dapF | uvrD | ERS008532_03505 | ERS008532_03509 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | DNA-dependent helicase II. | 0.411 |
dapF | xerC | ERS008532_03505 | ERS008532_03507 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Site-specific tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifical [...] | 0.777 |
dapF | yfnB | ERS008532_03505 | ERS008532_03508 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Flavin mononucleotide phosphatase. | 0.550 |
dinP | recR | ERS008532_02889 | ERS008532_02784 | DNA polymerase IV; 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. | Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | 0.540 |
dinP | xerC | ERS008532_02889 | ERS008532_03507 | DNA polymerase IV; 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. | Site-specific tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifical [...] | 0.520 |
ftsK | recR | ERS008532_00183 | ERS008532_02784 | Putative cell division protein. | Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | 0.507 |
ftsK | uvrD | ERS008532_00183 | ERS008532_03509 | Putative cell division protein. | DNA-dependent helicase II. | 0.451 |
ftsK | xerC | ERS008532_00183 | ERS008532_03507 | Putative cell division protein. | Site-specific tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifical [...] | 0.637 |
recR | dinP | ERS008532_02784 | ERS008532_02889 | Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | DNA polymerase IV; 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. | 0.540 |