Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DR97_1214 | lepA | DR97_1214 | DR97_1216 | DUF4845 domain-containing protein | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | 0.661 |
| DR97_1214 | lepB_1 | DR97_1214 | DR97_1215 | DUF4845 domain-containing protein | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.786 |
| DR97_1214 | rnc | DR97_1214 | DR97_1213 | DUF4845 domain-containing protein | Ribonuclease 3; Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre- crRNA and tracrRNA of type II CRISPR loci if present in the organism | 0.895 |
| DR97_1863 | lepB_1 | DR97_1863 | DR97_1215 | Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.942 |
| DR97_1863 | lepB_2 | DR97_1863 | DR97_491 | Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.829 |
| DR97_1863 | secA | DR97_1863 | DR97_1581 | Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family | Protein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family | 0.757 |
| DR97_1863 | secY | DR97_1863 | DR97_3668 | Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently | 0.688 |
| DR97_1863 | yidC | DR97_1863 | DR97_2947 | Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family | Membrane protein insertase YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins | 0.820 |
| drrA | lepA | DR97_5131 | DR97_1216 | annotation not available | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | 0.496 |
| drrA | lepB_1 | DR97_5131 | DR97_1215 | annotation not available | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.876 |
| drrA | lepB_2 | DR97_5131 | DR97_491 | annotation not available | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.876 |
| lepA | DR97_1214 | DR97_1216 | DR97_1214 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | DUF4845 domain-containing protein | 0.661 |
| lepA | drrA | DR97_1216 | DR97_5131 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | annotation not available | 0.496 |
| lepA | lepB_1 | DR97_1216 | DR97_1215 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.995 |
| lepA | lepB_2 | DR97_1216 | DR97_491 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | 0.921 |
| lepA | rnc | DR97_1216 | DR97_1213 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | Ribonuclease 3; Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre- crRNA and tracrRNA of type II CRISPR loci if present in the organism | 0.874 |
| lepA | secA | DR97_1216 | DR97_1581 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | Protein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family | 0.782 |
| lepA | secY | DR97_1216 | DR97_3668 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently | 0.681 |
| lepA | yidC | DR97_1216 | DR97_2947 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | Membrane protein insertase YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins | 0.589 |
| lepB_1 | DR97_1214 | DR97_1215 | DR97_1214 | sigpep_I_bact: signal peptidase I; Belongs to the peptidase S26 family | DUF4845 domain-containing protein | 0.786 |
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