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 |
| def | fmt | b3287 | b3288 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | 0.998 |
| def | rlmN | b3287 | b2517 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Dual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. | 0.460 |
| def | rsmB | b3287 | b3289 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.824 |
| def | smg | b3287 | b3284 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | DUF494 family putative periplasmic protein; Belongs to the Smg family. | 0.628 |
| def | yrdB | b3287 | b3280 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | DUF1488 family protein. | 0.483 |
| def | yrdD | b3287 | b3283 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | ssDNA-binding protein, function unknown; Putative DNA topoisomerase; To H.influenzae HI_0656.1. | 0.587 |
| fmt | def | b3288 | b3287 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.998 |
| fmt | rlmN | b3288 | b2517 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | Dual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. | 0.426 |
| fmt | rsmB | b3288 | b3289 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.997 |
| fmt | smg | b3288 | b3284 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | DUF494 family putative periplasmic protein; Belongs to the Smg family. | 0.574 |
| fmt | yrdB | b3288 | b3280 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | DUF1488 family protein. | 0.479 |
| fmt | yrdD | b3288 | b3283 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | ssDNA-binding protein, function unknown; Putative DNA topoisomerase; To H.influenzae HI_0656.1. | 0.552 |
| rlmN | def | b2517 | b3287 | Dual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.460 |
| rlmN | fmt | b2517 | b3288 | Dual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | 0.426 |
| rlmN | rsmB | b2517 | b3289 | Dual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.944 |
| rsmB | def | b3289 | b3287 | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.824 |
| rsmB | fmt | b3289 | b3288 | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family. | 0.997 |
| rsmB | rlmN | b3289 | b2517 | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | Dual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. | 0.944 |
| rsmB | smg | b3289 | b3284 | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | DUF494 family putative periplasmic protein; Belongs to the Smg family. | 0.516 |
| rsmB | yrdB | b3289 | b3280 | 16S rRNA m(5)C967 methyltransferase, SAM-dependent; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | DUF1488 family protein. | 0.401 |
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