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 |
| Lmac_1871 | Lmac_1873 | Lmac_1871 | Lmac_1873 | Cytochrome c5. | Hypothetical protein. | 0.527 |
| Lmac_1871 | dsbB | Lmac_1871 | Lmac_1872 | Cytochrome c5. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.833 |
| Lmac_1871 | tgt_2 | Lmac_1871 | Lmac_1874 | Cytochrome c5. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.427 |
| Lmac_1873 | Lmac_1871 | Lmac_1873 | Lmac_1871 | Hypothetical protein. | Cytochrome c5. | 0.527 |
| Lmac_1873 | dsbB | Lmac_1873 | Lmac_1872 | Hypothetical protein. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.527 |
| Lmac_1873 | ppiB | Lmac_1873 | Lmac_1875 | Hypothetical protein. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.437 |
| Lmac_1873 | tgt_2 | Lmac_1873 | Lmac_1874 | Hypothetical protein. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.497 |
| dsbB | Lmac_1871 | Lmac_1872 | Lmac_1871 | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Cytochrome c5. | 0.833 |
| dsbB | Lmac_1873 | Lmac_1872 | Lmac_1873 | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Hypothetical protein. | 0.527 |
| dsbB | tgt_2 | Lmac_1872 | Lmac_1874 | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.427 |
| ppiB | Lmac_1873 | Lmac_1875 | Lmac_1873 | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Hypothetical protein. | 0.437 |
| ppiB | tgt_2 | Lmac_1875 | Lmac_1874 | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.704 |
| tgt_2 | Lmac_1871 | Lmac_1874 | Lmac_1871 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | Cytochrome c5. | 0.427 |
| tgt_2 | Lmac_1873 | Lmac_1874 | Lmac_1873 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | Hypothetical protein. | 0.497 |
| tgt_2 | dsbB | Lmac_1874 | Lmac_1872 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.427 |
| tgt_2 | ppiB | Lmac_1874 | Lmac_1875 | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.704 |