Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0095 | azo0839 | azo0095 | azo0839 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.862 |
| azo0095 | dinP | azo0095 | azo2786 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | 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. | 0.580 |
| azo0095 | dnaN | azo0095 | azo0002 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | DNA-directed DNA polymerase; 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 repl [...] | 0.811 |
| azo0095 | polA | azo0095 | azo3600 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.868 |
| azo0095 | recA | azo0095 | azo0507 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | Recombinase A; 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. | 0.926 |
| azo0095 | recQ | azo0095 | azo3318 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | ATP-dependent DNA helicase recQ (EC 3.6.1.-). INVOLVED IN THE RECF RECOMBINATION PATHWAY; ITS GENE EXPRESSION IS UNDER THE REGULATION OF THE SOS SYSTEM. IT IS A DNA HELICASE. recq: ATP-dependent DNA helicase RecQ; High confidence in function and specificity. | 0.987 |
| azo0095 | sbcC | azo0095 | azo0200 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | Exonuclease SbcC, putative; Nuclease sbcCD subunit C. SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3->5 double strand exonuclease that can open hairpins. It also has a 5 single-strand endonuclease activity (By similarity). sbcc: exonuclease SbcC; High confidence in function and specificity. | 0.883 |
| azo0095 | sbcD | azo0095 | azo0199 | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | Exonuclease SbcD, putative; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family. | 0.800 |
| azo0839 | azo0095 | azo0839 | azo0095 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | 0.862 |
| azo0839 | dinP | azo0839 | azo2786 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 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. | 0.729 |
| azo0839 | dnaN | azo0839 | azo0002 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | DNA-directed DNA polymerase; 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 repl [...] | 0.967 |
| azo0839 | polA | azo0839 | azo3600 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.986 |
| azo0839 | recA | azo0839 | azo0507 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Recombinase A; 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. | 0.931 |
| azo0839 | recQ | azo0839 | azo3318 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | ATP-dependent DNA helicase recQ (EC 3.6.1.-). INVOLVED IN THE RECF RECOMBINATION PATHWAY; ITS GENE EXPRESSION IS UNDER THE REGULATION OF THE SOS SYSTEM. IT IS A DNA HELICASE. recq: ATP-dependent DNA helicase RecQ; High confidence in function and specificity. | 0.940 |
| azo0839 | sbcC | azo0839 | azo0200 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Exonuclease SbcC, putative; Nuclease sbcCD subunit C. SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3->5 double strand exonuclease that can open hairpins. It also has a 5 single-strand endonuclease activity (By similarity). sbcc: exonuclease SbcC; High confidence in function and specificity. | 0.632 |
| azo0839 | sbcD | azo0839 | azo0199 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Exonuclease SbcD, putative; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family. | 0.749 |
| dinP | azo0095 | azo2786 | azo0095 | 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. | DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...] | 0.580 |
| dinP | azo0839 | azo2786 | azo0839 | 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. | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.729 |
| dinP | dnaN | azo2786 | azo0002 | 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. | DNA-directed DNA polymerase; 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 repl [...] | 0.974 |
| dinP | lexA | azo2786 | azo2064 | 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. | Repressor LexA; 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. | 0.931 |
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