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 |
| ftsH | ftsW | MSMEG_6105 | MSMEG_4228 | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | 0.480 |
| ftsH | secY | MSMEG_6105 | MSMEG_1483 | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.745 |
| ftsW | ftsH | MSMEG_4228 | MSMEG_6105 | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.480 |
| ftsW | murG | MSMEG_4228 | MSMEG_4227 | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | 0.999 |
| ftsW | pbpB | MSMEG_4228 | MSMEG_4233 | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. | 0.999 |
| ftsW | secY | MSMEG_4228 | MSMEG_1483 | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.583 |
| murG | ftsW | MSMEG_4227 | MSMEG_4228 | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | 0.999 |
| murG | pbpB | MSMEG_4227 | MSMEG_4233 | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. | 0.988 |
| murG | secY | MSMEG_4227 | MSMEG_1483 | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.555 |
| pbpB | ftsW | MSMEG_4233 | MSMEG_4228 | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | 0.999 |
| pbpB | murG | MSMEG_4233 | MSMEG_4227 | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | 0.988 |
| pbpB | secY | MSMEG_4233 | MSMEG_1483 | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.472 |
| secY | ftsH | MSMEG_1483 | MSMEG_6105 | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.745 |
| secY | ftsW | MSMEG_1483 | MSMEG_4228 | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Cell division protein FtsW; Identified by match to protein family HMM PF01098; match to protein family HMM TIGR02614; Belongs to the SEDS family. | 0.583 |
| secY | murG | MSMEG_1483 | MSMEG_4227 | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | 0.555 |
| secY | pbpB | MSMEG_1483 | MSMEG_4233 | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. | 0.472 |