| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KWZ72892.1 | KWZ72893.1 | HMPREF3198_01246 | HMPREF3198_01247 | FeoA domain protein; Psort location: Cytoplasmic, score: 7.50. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.455 |
| KWZ72892.1 | KWZ72894.1 | HMPREF3198_01246 | HMPREF3198_01248 | FeoA domain protein; Psort location: Cytoplasmic, score: 7.50. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.455 |
| KWZ72893.1 | KWZ72892.1 | HMPREF3198_01247 | HMPREF3198_01246 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | FeoA domain protein; Psort location: Cytoplasmic, score: 7.50. | 0.455 |
| KWZ72893.1 | KWZ72894.1 | HMPREF3198_01247 | HMPREF3198_01248 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.773 |
| KWZ72893.1 | def | HMPREF3198_01247 | HMPREF3198_01249 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 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. | 0.497 |
| KWZ72893.1 | ispG | HMPREF3198_01247 | HMPREF3198_01251 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | 0.401 |
| KWZ72893.1 | proS | HMPREF3198_01247 | HMPREF3198_01250 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.497 |
| KWZ72894.1 | KWZ72892.1 | HMPREF3198_01248 | HMPREF3198_01246 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | FeoA domain protein; Psort location: Cytoplasmic, score: 7.50. | 0.455 |
| KWZ72894.1 | KWZ72893.1 | HMPREF3198_01248 | HMPREF3198_01247 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.773 |
| KWZ72894.1 | def | HMPREF3198_01248 | HMPREF3198_01249 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 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. | 0.606 |
| KWZ72894.1 | ispG | HMPREF3198_01248 | HMPREF3198_01251 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | 0.401 |
| KWZ72894.1 | proS | HMPREF3198_01248 | HMPREF3198_01250 | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.497 |
| def | KWZ72893.1 | HMPREF3198_01249 | HMPREF3198_01247 | 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. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.497 |
| def | KWZ72894.1 | HMPREF3198_01249 | HMPREF3198_01248 | 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. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.606 |
| def | ispG | HMPREF3198_01249 | HMPREF3198_01251 | 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. | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | 0.663 |
| def | proS | HMPREF3198_01249 | HMPREF3198_01250 | 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. | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.832 |
| ispG | KWZ72893.1 | HMPREF3198_01251 | HMPREF3198_01247 | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.401 |
| ispG | KWZ72894.1 | HMPREF3198_01251 | HMPREF3198_01248 | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | Hypothetical protein; Psort location: Cytoplasmic, score: 7.50. | 0.401 |
| ispG | def | HMPREF3198_01251 | HMPREF3198_01249 | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG 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. | 0.663 |
| ispG | proS | HMPREF3198_01251 | HMPREF3198_01250 | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.692 |