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 |
| argA | azo2831 | azo2830 | azo2831 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present. | 0.597 |
| argA | azo2832 | azo2830 | azo2832 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.576 |
| argA | suhB2 | azo2830 | azo2833 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | Inositol-1-monophosphatase(IMPase)(Inositol-1- phosphatase)(I-1-Pase).May act by enhancing the synthesis or degradation of phosphorylated messenger molecules. Catalytic activity: myo-inositol 1-phosphate + h(2)o = myo-inositol + phosphate. 36% Inositol_P. Pfam:PF00459; Inositol_P; 1; High confidence in function and specificity. | 0.425 |
| azo2831 | argA | azo2831 | azo2830 | Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present. | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | 0.597 |
| azo2831 | azo2832 | azo2831 | azo2832 | Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present. | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.738 |
| azo2831 | suhB2 | azo2831 | azo2833 | Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present. | Inositol-1-monophosphatase(IMPase)(Inositol-1- phosphatase)(I-1-Pase).May act by enhancing the synthesis or degradation of phosphorylated messenger molecules. Catalytic activity: myo-inositol 1-phosphate + h(2)o = myo-inositol + phosphate. 36% Inositol_P. Pfam:PF00459; Inositol_P; 1; High confidence in function and specificity. | 0.489 |
| azo2832 | argA | azo2832 | azo2830 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | 0.576 |
| azo2832 | azo2831 | azo2832 | azo2831 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present. | 0.738 |
| azo2832 | dnaJ1 | azo2832 | azo1062 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.447 |
| azo2832 | gidB | azo2832 | azo0142 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Probable methyltransferase GidB; Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. | 0.482 |
| azo2832 | ksgA | azo2832 | azo2884 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Dimethyladenosine transferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | 0.528 |
| azo2832 | mraW | azo2832 | azo0876 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | SAM dependent methyltransferase; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.575 |
| azo2832 | prmA | azo2832 | azo0861 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. | 0.798 |
| azo2832 | rlmB | azo2832 | azo0940 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | tRNA/rRNA methyltransferase; Specifically methylates the ribose of guanosine 2251 in 23S rRNA. | 0.450 |
| azo2832 | suhB2 | azo2832 | azo2833 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Inositol-1-monophosphatase(IMPase)(Inositol-1- phosphatase)(I-1-Pase).May act by enhancing the synthesis or degradation of phosphorylated messenger molecules. Catalytic activity: myo-inositol 1-phosphate + h(2)o = myo-inositol + phosphate. 36% Inositol_P. Pfam:PF00459; Inositol_P; 1; High confidence in function and specificity. | 0.584 |
| azo2832 | trmD | azo2832 | azo2900 | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | tRNA (guanine-N1-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. | 0.490 |
| dnaJ1 | azo2832 | azo1062 | azo2832 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.447 |
| dnaJ1 | ksgA | azo1062 | azo2884 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | Dimethyladenosine transferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | 0.478 |
| dnaJ1 | prmA | azo1062 | azo0861 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. | 0.698 |
| dnaJ1 | rlmB | azo1062 | azo0940 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | tRNA/rRNA methyltransferase; Specifically methylates the ribose of guanosine 2251 in 23S rRNA. | 0.798 |
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