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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| THL1_1516 | THL1_3630 | THL1_1516 | THL1_3630 | Lytic transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Lytic transglycosylase. | 0.452 |
| THL1_1682 | THL1_3630 | THL1_1682 | THL1_3630 | Glycosyl transferase family 51. | Lytic transglycosylase. | 0.460 |
| THL1_1682 | THL1_5305 | THL1_1682 | THL1_5305 | Glycosyl transferase family 51. | Peptidase. | 0.541 |
| THL1_2119 | THL1_3630 | THL1_2119 | THL1_3630 | Lytic transglycosylase. | Lytic transglycosylase. | 0.504 |
| THL1_2346 | THL1_3630 | THL1_2346 | THL1_3630 | Glycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Lytic transglycosylase. | 0.509 |
| THL1_3630 | THL1_1516 | THL1_3630 | THL1_1516 | Lytic transglycosylase. | Lytic transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.452 |
| THL1_3630 | THL1_1682 | THL1_3630 | THL1_1682 | Lytic transglycosylase. | Glycosyl transferase family 51. | 0.460 |
| THL1_3630 | THL1_2119 | THL1_3630 | THL1_2119 | Lytic transglycosylase. | Lytic transglycosylase. | 0.504 |
| THL1_3630 | THL1_2346 | THL1_3630 | THL1_2346 | Lytic transglycosylase. | Glycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.509 |
| THL1_3630 | THL1_4883 | THL1_3630 | THL1_4883 | Lytic transglycosylase. | Penicillin-binding protein; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.460 |
| THL1_3630 | THL1_5007 | THL1_3630 | THL1_5007 | Lytic transglycosylase. | Lytic transglycosylase. | 0.446 |
| THL1_3630 | THL1_5305 | THL1_3630 | THL1_5305 | Lytic transglycosylase. | Peptidase. | 0.560 |
| THL1_3630 | mltF | THL1_3630 | THL1_1246 | Lytic transglycosylase. | Murein transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.485 |
| THL1_3630 | mtgA | THL1_3630 | THL1_238 | Lytic transglycosylase. | Peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.460 |
| THL1_4883 | THL1_3630 | THL1_4883 | THL1_3630 | Penicillin-binding protein; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | Lytic transglycosylase. | 0.460 |
| THL1_4883 | THL1_5114 | THL1_4883 | THL1_5114 | Penicillin-binding protein; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | Penicillin-binding protein 1C. | 0.922 |
| THL1_4883 | THL1_5305 | THL1_4883 | THL1_5305 | Penicillin-binding protein; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | Peptidase. | 0.965 |
| THL1_4883 | mtgA | THL1_4883 | THL1_238 | Penicillin-binding protein; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | Peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.609 |
| THL1_5007 | THL1_3630 | THL1_5007 | THL1_3630 | Lytic transglycosylase. | Lytic transglycosylase. | 0.446 |
| THL1_5114 | THL1_4883 | THL1_5114 | THL1_4883 | Penicillin-binding protein 1C. | Penicillin-binding protein; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.922 |
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