| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO46281.1 | ADO48407.1 | Entcl_0002 | Entcl_2153 | 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: slt:Slit_1763 hypothetical protein. | 0.929 |
| ADO46281.1 | ADO48503.1 | Entcl_0002 | Entcl_2250 | 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 [...] | methylated-DNA/protein-cysteine methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.416 |
| ADO46281.1 | ADO49145.1 | Entcl_0002 | Entcl_2897 | 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 [...] | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | 0.771 |
| 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. | 0.962 |
| ADO46281.1 | ADO50107.1 | Entcl_0002 | Entcl_3867 | 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: cps:CPS_2945 putative DEAD/DEAH box helicase; PFAM: DEAD/DEAH box helicase domain protein; helicase domain protein; SMART: helicase domain protein; DEAD-like helicase. | 0.620 |
| ADO46281.1 | ADO50448.1 | Entcl_0002 | Entcl_4215 | 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: ATP-dependent DNA helicase RecQ; ATP-dependent DNA helicase, RecQ family; PFAM: RQC domain; DEAD/DEAH box helicase domain protein; helicase domain protein; HRDC domain protein; KEGG: cko:CKO_00161 ATP-dependent DNA helicase RecQ; SMART: HRDC domain protein; helicase domain protein; DEAD-like helicase. | 0.620 |
| ADO48407.1 | ADO46281.1 | Entcl_2153 | Entcl_0002 | KEGG: slt:Slit_1763 hypothetical protein. | 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 [...] | 0.929 |
| ADO48407.1 | ADO49145.1 | Entcl_2153 | Entcl_2897 | KEGG: slt:Slit_1763 hypothetical protein. | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | 0.691 |
| ADO48407.1 | ADO49906.1 | Entcl_2153 | Entcl_3665 | KEGG: slt:Slit_1763 hypothetical protein. | KEGG: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | 0.931 |
| ADO48503.1 | ADO46281.1 | Entcl_2250 | Entcl_0002 | methylated-DNA/protein-cysteine methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 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 [...] | 0.416 |
| ADO48503.1 | ADO49145.1 | Entcl_2250 | Entcl_2897 | methylated-DNA/protein-cysteine methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | 0.481 |
| ADO49145.1 | ADO46281.1 | Entcl_2897 | Entcl_0002 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | 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 [...] | 0.771 |
| ADO49145.1 | ADO48407.1 | Entcl_2897 | Entcl_2153 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | KEGG: slt:Slit_1763 hypothetical protein. | 0.691 |
| ADO49145.1 | ADO48503.1 | Entcl_2897 | Entcl_2250 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | methylated-DNA/protein-cysteine methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.481 |
| ADO49145.1 | ADO49147.1 | Entcl_2897 | Entcl_2899 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | PFAM: cell divisionFtsK/SpoIIIE; DNA translocase ftsK gamma; KEGG: cko:CKO_02181 DNA translocase FtsK. | 0.719 |
| ADO49145.1 | ADO49553.1 | Entcl_2897 | Entcl_3308 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | Copper-translocating P-type ATPase; KEGG: cko:CKO_02665 copper exporting ATPase; TIGRFAM: copper-translocating P-type ATPase; heavy metal translocating P-type ATPase; ATPase, P-type (transporting), HAD superfamily, subfamily IC; PFAM: E1-E2 ATPase-associated domain protein; Heavy metal transport/detoxification protein; Haloacid dehalogenase domain protein hydrolase. | 0.500 |
| ADO49145.1 | ADO49906.1 | Entcl_2897 | Entcl_3665 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | KEGG: kpn:KPN_00059 DNA polymerase II; PFAM: DNA polymerase B region; DNA polymerase B exonuclease; SMART: DNA-directed DNA polymerase B. | 0.481 |
| ADO49145.1 | ADO50107.1 | Entcl_2897 | Entcl_3867 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | KEGG: cps:CPS_2945 putative DEAD/DEAH box helicase; PFAM: DEAD/DEAH box helicase domain protein; helicase domain protein; SMART: helicase domain protein; DEAD-like helicase. | 0.698 |
| ADO49145.1 | ADO50448.1 | Entcl_2897 | Entcl_4215 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | TIGRFAM: ATP-dependent DNA helicase RecQ; ATP-dependent DNA helicase, RecQ family; PFAM: RQC domain; DEAD/DEAH box helicase domain protein; helicase domain protein; HRDC domain protein; KEGG: cko:CKO_00161 ATP-dependent DNA helicase RecQ; SMART: HRDC domain protein; helicase domain protein; DEAD-like helicase. | 0.698 |
| ADO49145.1 | lolA | Entcl_2897 | Entcl_2898 | AAA ATPase central domain protein; KEGG: kpu:KP1_1893 recombination factor protein RarA; PFAM: AAA ATPase central domain protein; SMART: AAA ATPase. | Outer membrane lipoprotein carrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.861 |
