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 |
| Htur_1469 | thi4 | Htur_1469 | Htur_1462 | PFAM: Phosphomethylpyrimidine kinase. | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | 0.490 |
| Htur_2542 | thi4 | Htur_2542 | Htur_1462 | Transcriptional regulator, XRE family; PFAM: Phosphomethylpyrimidine kinase. | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | 0.529 |
| Htur_3053 | thi4 | Htur_3053 | Htur_1462 | Metalloendopeptidase, glycoprotease family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belongs to the KAE1 / TsaD family. | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | 0.639 |
| Htur_3053 | topA | Htur_3053 | Htur_1458 | Metalloendopeptidase, glycoprotease family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belongs to the KAE1 / TsaD family. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.634 |
| Htur_3232 | thi4 | Htur_3232 | Htur_1462 | TIGRFAM: phosphomethylpyrimidine kinase; PFAM: Phosphomethylpyrimidine kinase type-1; Phosphomethylpyrimidine kinase; KEGG: bra:BRADO5133 bifunctional: hydroxy- methylpyrimidine kinase (HMP kinase); hydroxy- phosphomethylpyrimidine kinase (HMP-P kinase). | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | 0.936 |
| Htur_3232 | thiC | Htur_3232 | Htur_1332 | TIGRFAM: phosphomethylpyrimidine kinase; PFAM: Phosphomethylpyrimidine kinase type-1; Phosphomethylpyrimidine kinase; KEGG: bra:BRADO5133 bifunctional: hydroxy- methylpyrimidine kinase (HMP kinase); hydroxy- phosphomethylpyrimidine kinase (HMP-P kinase). | Thiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. | 0.996 |
| thi4 | Htur_1469 | Htur_1462 | Htur_1469 | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | PFAM: Phosphomethylpyrimidine kinase. | 0.490 |
| thi4 | Htur_2542 | Htur_1462 | Htur_2542 | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | Transcriptional regulator, XRE family; PFAM: Phosphomethylpyrimidine kinase. | 0.529 |
| thi4 | Htur_3053 | Htur_1462 | Htur_3053 | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | Metalloendopeptidase, glycoprotease family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belongs to the KAE1 / TsaD family. | 0.639 |
| thi4 | Htur_3232 | Htur_1462 | Htur_3232 | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | TIGRFAM: phosphomethylpyrimidine kinase; PFAM: Phosphomethylpyrimidine kinase type-1; Phosphomethylpyrimidine kinase; KEGG: bra:BRADO5133 bifunctional: hydroxy- methylpyrimidine kinase (HMP kinase); hydroxy- phosphomethylpyrimidine kinase (HMP-P kinase). | 0.936 |
| thi4 | thiC | Htur_1462 | Htur_1332 | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | Thiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. | 0.747 |
| thi4 | topA | Htur_1462 | Htur_1458 | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.435 |
| thiC | Htur_3232 | Htur_1332 | Htur_3232 | Thiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. | TIGRFAM: phosphomethylpyrimidine kinase; PFAM: Phosphomethylpyrimidine kinase type-1; Phosphomethylpyrimidine kinase; KEGG: bra:BRADO5133 bifunctional: hydroxy- methylpyrimidine kinase (HMP kinase); hydroxy- phosphomethylpyrimidine kinase (HMP-P kinase). | 0.996 |
| thiC | thi4 | Htur_1332 | Htur_1462 | Thiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | 0.747 |
| topA | Htur_3053 | Htur_1458 | Htur_3053 | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | Metalloendopeptidase, glycoprotease family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belongs to the KAE1 / TsaD family. | 0.634 |
| topA | thi4 | Htur_1458 | Htur_1462 | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | Thiazole biosynthesis enzyme; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | 0.435 |