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 |
| AOI81430.1 | proS | WI67_02690 | WI67_02700 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.534 |
| AOI81430.1 | rppH_3 | WI67_02690 | WI67_02695 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.785 |
| AOI82762.1 | rppH_3 | WI67_10045 | WI67_02695 | DNAase; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.623 |
| AOI83719.1 | rppH_3 | WI67_15265 | WI67_02695 | Peptidase S41; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S41A family. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.554 |
| dapE | dapF | WI67_11035 | WI67_16430 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.931 |
| dapE | dapF-2 | WI67_11035 | WI67_31870 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.601 |
| dapE | rppH_3 | WI67_11035 | WI67_02695 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.615 |
| dapF | dapE | WI67_16430 | WI67_11035 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 0.931 |
| dapF | rppH_3 | WI67_16430 | WI67_02695 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.752 |
| dapF-2 | dapE | WI67_31870 | WI67_11035 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 0.601 |
| dapF-2 | rppH_3 | WI67_31870 | WI67_02695 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.741 |
| nnrD | rppH_3 | WI67_10165 | WI67_02695 | Bifunctional ADP-dependent (S)-NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-spec [...] | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.799 |
| proS | AOI81430.1 | WI67_02700 | WI67_02690 | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.534 |
| proS | rppH_3 | WI67_02700 | WI67_02695 | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.544 |
| rnr | rppH_3 | WI67_07680 | WI67_02695 | Ribonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | 0.543 |
| rppH_3 | AOI81430.1 | WI67_02695 | WI67_02690 | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.785 |
| rppH_3 | AOI82762.1 | WI67_02695 | WI67_10045 | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | DNAase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.623 |
| rppH_3 | AOI83719.1 | WI67_02695 | WI67_15265 | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | Peptidase S41; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S41A family. | 0.554 |
| rppH_3 | dapE | WI67_02695 | WI67_11035 | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 0.615 |
| rppH_3 | dapF | WI67_02695 | WI67_16430 | RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.752 |
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