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 |
| Rv0428c | def | Rv0428c | Rv0429c | GCN5-related N-acetyltransferase; Rv0428c, (MTCY22G10.25c), len: 302 aa. Probable acetyltransferase. Contains GNAT (Gcn5-related N-acetyltransferase) domain in C-terminal part. See Vetting et al. 2005. | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 0.961 |
| Rv0428c | xthA | Rv0428c | Rv0427c | GCN5-related N-acetyltransferase; Rv0428c, (MTCY22G10.25c), len: 302 aa. Probable acetyltransferase. Contains GNAT (Gcn5-related N-acetyltransferase) domain in C-terminal part. See Vetting et al. 2005. | Probable exodeoxyribonuclease III protein XthA (exonuclease III) (EXO III) (AP endonuclease VI); Rv0427c, (MTCY22G10.24c), len: 291 aa. Probable xthA (alternate gene name: xth), exodeoxyribonuclease III protein (see citation below), similar to others e.g. EX3_ECOLI|P09030 exodeoxyribonuclease III from Escherichia Coli strain K12 (268 aa), FASTA scores: opt: 360, E(): 1.2e-17, (29.3% identity in 270 aa overlap); etc. Belongs to the AP/EXOA family of DNA repair enzymes. | 0.946 |
| def | Rv0428c | Rv0429c | Rv0428c | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | GCN5-related N-acetyltransferase; Rv0428c, (MTCY22G10.25c), len: 302 aa. Probable acetyltransferase. Contains GNAT (Gcn5-related N-acetyltransferase) domain in C-terminal part. See Vetting et al. 2005. | 0.961 |
| def | fmt | Rv0429c | Rv1406 | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | Probable methionyl-tRNA formyltransferase Fmt; 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. | 0.926 |
| def | mapB | Rv0429c | Rv2861c | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | 0.947 |
| def | rplI | Rv0429c | Rv0056 | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 50S ribosomal protein L9 RplI; Binds to the 23S rRNA. | 0.920 |
| def | rplQ | Rv0429c | Rv3456c | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | Rv3456c, (MTCY13E12.09c), len: 180 aa. rplQ, 50S ribosomal protein L17, equivalent to Q9X797|RL17_MYCLE|ML1956|MLCB1222.26c 50S ribosomal protein L17 from Mycobacterium leprae (170 aa), FASTA scores: opt: 874, E(): 9.5e-45, (81.85% identity in 171 aa overlap). Also highly similar to other e.g. O86775|RL17_STRCO|SC6G4.08 from Streptomyces coelicolor (168 aa), FASTA scores: opt: 609, E(): 3.7e-29, (60.0% identity in 170 aa overlap); BAB47931|MLR0326 from Rhizobium loti (Mesorhizobium loti) (143 aa), FASTA scores: opt: 404, E(): 3.7e-17, (49.65% identity in 139 aa overlap); Q9Z9H5|RL17_TH [...] | 0.915 |
| def | rplU | Rv0429c | Rv2442c | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 50S ribosomal protein L21 RplU; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.927 |
| def | rplV | Rv0429c | Rv0706 | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 50S ribosomal protein L22 RplV; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). | 0.924 |
| def | rpsT | Rv0429c | Rv2412 | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 30S ribosomal protein S20 RpsT; Binds directly to 16S ribosomal RNA; Belongs to the bacterial ribosomal protein bS20 family. | 0.924 |
| def | tig | Rv0429c | Rv2462c | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | Probable trigger factor (TF) protein Tig; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.934 |
| def | xthA | Rv0429c | Rv0427c | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | Probable exodeoxyribonuclease III protein XthA (exonuclease III) (EXO III) (AP endonuclease VI); Rv0427c, (MTCY22G10.24c), len: 291 aa. Probable xthA (alternate gene name: xth), exodeoxyribonuclease III protein (see citation below), similar to others e.g. EX3_ECOLI|P09030 exodeoxyribonuclease III from Escherichia Coli strain K12 (268 aa), FASTA scores: opt: 360, E(): 1.2e-17, (29.3% identity in 270 aa overlap); etc. Belongs to the AP/EXOA family of DNA repair enzymes. | 0.952 |
| fmt | def | Rv1406 | Rv0429c | Probable methionyl-tRNA formyltransferase Fmt; 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. | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 0.926 |
| fmt | mapB | Rv1406 | Rv2861c | Probable methionyl-tRNA formyltransferase Fmt; 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. | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | 0.423 |
| mapB | def | Rv2861c | Rv0429c | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Probable polypeptide deformylase Def (PDF) (formylmethionine 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 (By similarity); Belongs to the polypeptide deformylase family. | 0.947 |
| mapB | fmt | Rv2861c | Rv1406 | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Probable methionyl-tRNA formyltransferase Fmt; 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. | 0.423 |
| mapB | rplQ | Rv2861c | Rv3456c | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Rv3456c, (MTCY13E12.09c), len: 180 aa. rplQ, 50S ribosomal protein L17, equivalent to Q9X797|RL17_MYCLE|ML1956|MLCB1222.26c 50S ribosomal protein L17 from Mycobacterium leprae (170 aa), FASTA scores: opt: 874, E(): 9.5e-45, (81.85% identity in 171 aa overlap). Also highly similar to other e.g. O86775|RL17_STRCO|SC6G4.08 from Streptomyces coelicolor (168 aa), FASTA scores: opt: 609, E(): 3.7e-29, (60.0% identity in 170 aa overlap); BAB47931|MLR0326 from Rhizobium loti (Mesorhizobium loti) (143 aa), FASTA scores: opt: 404, E(): 3.7e-17, (49.65% identity in 139 aa overlap); Q9Z9H5|RL17_TH [...] | 0.689 |
| mapB | rplU | Rv2861c | Rv2442c | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | 50S ribosomal protein L21 RplU; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.708 |
| mapB | rplV | Rv2861c | Rv0706 | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | 50S ribosomal protein L22 RplV; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). | 0.948 |
| mapB | rpsT | Rv2861c | Rv2412 | Methionine aminopeptidase MapB (map) (peptidase M); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | 30S ribosomal protein S20 RpsT; Binds directly to 16S ribosomal RNA; Belongs to the bacterial ribosomal protein bS20 family. | 0.481 |
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