| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FMG_0573 | FMG_1205 | FMG_0573 | FMG_1205 | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Putative phosphoesterase. | 0.433 |
| FMG_0646 | FMG_1205 | FMG_0646 | FMG_1205 | Alkyl hydroperoxide reductase. | Putative phosphoesterase. | 0.448 |
| FMG_1203 | FMG_1204 | FMG_1203 | FMG_1204 | Putative xanthine/uracil permease family protein. | Macrolide ABC transporter ATP-binding protein. | 0.762 |
| FMG_1203 | FMG_1205 | FMG_1203 | FMG_1205 | Putative xanthine/uracil permease family protein. | Putative phosphoesterase. | 0.602 |
| FMG_1203 | clpP | FMG_1203 | FMG_1208 | Putative xanthine/uracil permease family protein. | ATP-dependent protease Clp proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.463 |
| FMG_1203 | clpX | FMG_1203 | FMG_1207 | Putative xanthine/uracil permease family protein. | ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.474 |
| FMG_1203 | lon | FMG_1203 | FMG_1206 | Putative xanthine/uracil permease family protein. | ATP-dependent protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.602 |
| FMG_1204 | FMG_1203 | FMG_1204 | FMG_1203 | Macrolide ABC transporter ATP-binding protein. | Putative xanthine/uracil permease family protein. | 0.762 |
| FMG_1204 | FMG_1205 | FMG_1204 | FMG_1205 | Macrolide ABC transporter ATP-binding protein. | Putative phosphoesterase. | 0.610 |
| FMG_1204 | clpP | FMG_1204 | FMG_1208 | Macrolide ABC transporter ATP-binding protein. | ATP-dependent protease Clp proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.469 |
| FMG_1204 | clpX | FMG_1204 | FMG_1207 | Macrolide ABC transporter ATP-binding protein. | ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.476 |
| FMG_1204 | lon | FMG_1204 | FMG_1206 | Macrolide ABC transporter ATP-binding protein. | ATP-dependent protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.622 |
| FMG_1204 | tig | FMG_1204 | FMG_1209 | Macrolide ABC transporter ATP-binding protein. | FKBP-type peptidyl-prolyl cis-transisomerase; 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; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.498 |
| FMG_1205 | FMG_0573 | FMG_1205 | FMG_0573 | Putative phosphoesterase. | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.433 |
| FMG_1205 | FMG_0646 | FMG_1205 | FMG_0646 | Putative phosphoesterase. | Alkyl hydroperoxide reductase. | 0.448 |
| FMG_1205 | FMG_1203 | FMG_1205 | FMG_1203 | Putative phosphoesterase. | Putative xanthine/uracil permease family protein. | 0.602 |
| FMG_1205 | FMG_1204 | FMG_1205 | FMG_1204 | Putative phosphoesterase. | Macrolide ABC transporter ATP-binding protein. | 0.610 |
| FMG_1205 | clpP | FMG_1205 | FMG_1208 | Putative phosphoesterase. | ATP-dependent protease Clp proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.614 |
| FMG_1205 | clpX | FMG_1205 | FMG_1207 | Putative phosphoesterase. | ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.589 |
| FMG_1205 | lon | FMG_1205 | FMG_1206 | Putative phosphoesterase. | ATP-dependent protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.774 |