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 |
| MJ_0570 | dph2 | MJ_0570 | MJ_0483 | Conserved hypothetical protein; Similar to PID:1256896 PID:1256896 PID:1360566 percent identity: 35.35; identified by sequence similarity; putative. | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | 0.708 |
| MJ_0570 | dphB | MJ_0570 | MJ_1274 | Conserved hypothetical protein; Similar to PID:1256896 PID:1256896 PID:1360566 percent identity: 35.35; identified by sequence similarity; putative. | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.894 |
| MJ_0570 | fusA | MJ_0570 | MJ_1048 | Conserved hypothetical protein; Similar to PID:1256896 PID:1256896 PID:1360566 percent identity: 35.35; identified by sequence similarity; putative. | Translation elongation factor EF-2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase [...] | 0.961 |
| MJ_1136 | MJ_1326 | MJ_1136 | MJ_1326 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | 0.422 |
| MJ_1136 | dph2 | MJ_1136 | MJ_0483 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | 0.523 |
| MJ_1136 | dphB | MJ_1136 | MJ_1274 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.597 |
| MJ_1136 | rio2 | MJ_1136 | MJ_1073 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Conserved hypothetical protein; Similar to SP:P40160 PID:1302211 PID:600058 percent identity: 34.52; identified by sequence similarity; putative; Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family. | 0.435 |
| MJ_1136 | rtcA | MJ_1136 | MJ_0025 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Hypothetical protein; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). | 0.750 |
| MJ_1136 | trm5b | MJ_1136 | MJ_0883 | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | Conserved hypothetical protein; Specifically methylates the N1 position of guanosine-37 in various tRNAs. | 0.507 |
| MJ_1275 | dphB | MJ_1275 | MJ_1274 | NA(+)/H(+) antiporter (napA); This is probably a Na(+)/H(+) antiporter; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.599 |
| MJ_1326 | MJ_1136 | MJ_1326 | MJ_1136 | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | 0.422 |
| MJ_1326 | dph2 | MJ_1326 | MJ_0483 | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | 0.419 |
| MJ_1326 | dphB | MJ_1326 | MJ_1274 | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.588 |
| MJ_1326 | fusA | MJ_1326 | MJ_1048 | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | Translation elongation factor EF-2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase [...] | 0.606 |
| MJ_1326 | rps4e | MJ_1326 | MJ_0468 | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | SSU ribosomal protein S4E; Similar to SP:P14023 PID:44760 percent identity: 70.49; identified by sequence similarity; putative; Belongs to the eukaryotic ribosomal protein eS4 family. | 0.845 |
| MJ_1326 | rtcA | MJ_1326 | MJ_0025 | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | Hypothetical protein; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). | 0.432 |
| dph2 | MJ_0570 | MJ_0483 | MJ_0570 | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | Conserved hypothetical protein; Similar to PID:1256896 PID:1256896 PID:1360566 percent identity: 35.35; identified by sequence similarity; putative. | 0.708 |
| dph2 | MJ_1136 | MJ_0483 | MJ_1136 | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | Conserved hypothetical protein; tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L- methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'- dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not sho [...] | 0.523 |
| dph2 | MJ_1326 | MJ_0483 | MJ_1326 | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | GTP-binding protein, member of GTP1/OBG-family; Similar to SP:P17103 PID:43450 percent identity: 50.68; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. | 0.419 |
| dph2 | dphB | MJ_0483 | MJ_1274 | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | Diphthine synthase (dph5); S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | 0.927 |
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