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 |
| hsdM | hsdS | STM4525 | STM4524 | DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family. | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | 0.999 |
| hsdM | mod | STM4525 | STM0357 | DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family. | DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4. | 0.914 |
| hsdM | ydaL | STM4525 | STM1658 | DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family. | Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187. | 0.897 |
| hsdS | hsdM | STM4524 | STM4525 | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family. | 0.999 |
| hsdS | mod | STM4524 | STM0357 | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4. | 0.913 |
| hsdS | recA | STM4524 | STM2829 | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | DNA strand exchange and recombination protein; 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. | 0.481 |
| hsdS | ydaL | STM4524 | STM1658 | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187. | 0.897 |
| mod | hsdM | STM0357 | STM4525 | DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4. | DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family. | 0.914 |
| mod | hsdS | STM0357 | STM4524 | DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4. | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | 0.913 |
| mod | ydaL | STM0357 | STM1658 | DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4. | Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187. | 0.580 |
| recA | hsdS | STM2829 | STM4524 | DNA strand exchange and recombination protein; 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. | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | 0.481 |
| ydaL | hsdM | STM1658 | STM4525 | Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187. | DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family. | 0.897 |
| ydaL | hsdS | STM1658 | STM4524 | Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187. | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | 0.897 |
| ydaL | mod | STM1658 | STM0357 | Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187. | DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4. | 0.580 |