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 |
| azo1347 | azo1348 | azo1347 | azo1348 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | 0.671 |
| azo1347 | ccoG | azo1347 | azo1345 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | 0.703 |
| azo1347 | ccoH | azo1347 | azo1346 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | 0.731 |
| azo1347 | ccoN | azo1347 | azo1341 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] | 0.452 |
| azo1347 | ccoO | azo1347 | azo1342 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.475 |
| azo1347 | ccoP | azo1347 | azo1344 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.507 |
| azo1347 | ccoQ | azo1347 | azo1343 | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | Cbb3-type cytochrome oxidase, subunit ccoQ, 44% Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has PF05545,Cbb3-type cytochrome oxidase component FixQ; IPR008621;This family consists of several Cbb3-type cytochrome oxidase components (FixQ/CcoQ). FixQ is found in nitrogen fixing bacteria. Since nitrogen fixation is an energy-consuming process, effective symbioses depend on operation of a respiratory chain with a high affinity for O2, closely coupled to ATP production. This requirement is fulfilled by a special three-subunit terminal oxidase (cytochrome terminal oxidase cbb3), which was firs [...] | 0.510 |
| azo1348 | azo1347 | azo1348 | azo1347 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | 0.671 |
| azo1348 | ccoG | azo1348 | azo1345 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | 0.824 |
| azo1348 | ccoH | azo1348 | azo1346 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | 0.885 |
| azo1348 | ccoN | azo1348 | azo1341 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] | 0.472 |
| azo1348 | ccoO | azo1348 | azo1342 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.486 |
| azo1348 | ccoP | azo1348 | azo1344 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.657 |
| azo1348 | ccoQ | azo1348 | azo1343 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Cbb3-type cytochrome oxidase, subunit ccoQ, 44% Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has PF05545,Cbb3-type cytochrome oxidase component FixQ; IPR008621;This family consists of several Cbb3-type cytochrome oxidase components (FixQ/CcoQ). FixQ is found in nitrogen fixing bacteria. Since nitrogen fixation is an energy-consuming process, effective symbioses depend on operation of a respiratory chain with a high affinity for O2, closely coupled to ATP production. This requirement is fulfilled by a special three-subunit terminal oxidase (cytochrome terminal oxidase cbb3), which was firs [...] | 0.629 |
| ccoG | azo1347 | azo1345 | azo1347 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Hypothetical membrane protein. No homology to the data bank. No domain predicted. No signal peptide 1 TMH. | 0.703 |
| ccoG | azo1348 | azo1345 | azo1348 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | 0.824 |
| ccoG | ccoH | azo1345 | azo1346 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | 0.949 |
| ccoG | ccoN | azo1345 | azo1341 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] | 0.964 |
| ccoG | ccoO | azo1345 | azo1342 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.969 |
| ccoG | ccoP | azo1345 | azo1344 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.970 |
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