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 |
| SHG49889.1 | msrP | SAMN04488068_0454 | SAMN04488068_0798 | Ferredoxin-NADP reductase. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.687 |
| SHG49889.1 | msrQ | SAMN04488068_0454 | SAMN04488068_0797 | Ferredoxin-NADP reductase. | Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...] | 0.511 |
| SHG61962.1 | SHG61984.1 | SAMN04488068_0792 | SAMN04488068_0793 | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | Cysteine-rich CPXCG. | 0.594 |
| SHG61962.1 | SHG62009.1 | SAMN04488068_0792 | SAMN04488068_0794 | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.588 |
| SHG61962.1 | SHG62035.1 | SAMN04488068_0792 | SAMN04488068_0795 | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | XTP/dITP diphosphohydrolase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.577 |
| SHG61962.1 | msrP | SAMN04488068_0792 | SAMN04488068_0798 | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.474 |
| SHG61962.1 | msrQ | SAMN04488068_0792 | SAMN04488068_0797 | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...] | 0.474 |
| SHG61962.1 | rph | SAMN04488068_0792 | SAMN04488068_0796 | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.576 |
| SHG61984.1 | SHG61962.1 | SAMN04488068_0793 | SAMN04488068_0792 | Cysteine-rich CPXCG. | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | 0.594 |
| SHG61984.1 | SHG62009.1 | SAMN04488068_0793 | SAMN04488068_0794 | Cysteine-rich CPXCG. | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.740 |
| SHG61984.1 | SHG62035.1 | SAMN04488068_0793 | SAMN04488068_0795 | Cysteine-rich CPXCG. | XTP/dITP diphosphohydrolase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.740 |
| SHG61984.1 | SHG62125.1 | SAMN04488068_0793 | SAMN04488068_0799 | Cysteine-rich CPXCG. | Cysteine desulfuration protein SufE. | 0.452 |
| SHG61984.1 | msrP | SAMN04488068_0793 | SAMN04488068_0798 | Cysteine-rich CPXCG. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.621 |
| SHG61984.1 | msrQ | SAMN04488068_0793 | SAMN04488068_0797 | Cysteine-rich CPXCG. | Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...] | 0.621 |
| SHG61984.1 | rph | SAMN04488068_0793 | SAMN04488068_0796 | Cysteine-rich CPXCG. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.740 |
| SHG62009.1 | SHG61962.1 | SAMN04488068_0794 | SAMN04488068_0792 | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | LSU ribosomal protein L31P; Belongs to the bacterial ribosomal protein bL31 family. | 0.588 |
| SHG62009.1 | SHG61984.1 | SAMN04488068_0794 | SAMN04488068_0793 | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Cysteine-rich CPXCG. | 0.740 |
| SHG62009.1 | SHG62035.1 | SAMN04488068_0794 | SAMN04488068_0795 | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | XTP/dITP diphosphohydrolase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.828 |
| SHG62009.1 | SHG62125.1 | SAMN04488068_0794 | SAMN04488068_0799 | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Cysteine desulfuration protein SufE. | 0.497 |
| SHG62009.1 | msrP | SAMN04488068_0794 | SAMN04488068_0798 | Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.682 |
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