| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DVU_1180 | DVU_3364 | DVU_1180 | DVU_3364 | Hypothetical protein; Identified by Glimmer2; putative. | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | 0.424 |
| DVU_1944 | DVU_3364 | DVU_1944 | DVU_3364 | Pyruvate ferredoxin oxidoreductase, iron-sulfur binding subunit, putative; Identified by match to protein family HMM PF00037. | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | 0.461 |
| DVU_2753 | DVU_3364 | DVU_2753 | DVU_3364 | Identified by match to protein family HMM TIGR01909. | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | 0.438 |
| DVU_3364 | DVU_1180 | DVU_3364 | DVU_1180 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | Hypothetical protein; Identified by Glimmer2; putative. | 0.424 |
| DVU_3364 | DVU_1944 | DVU_3364 | DVU_1944 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | Pyruvate ferredoxin oxidoreductase, iron-sulfur binding subunit, putative; Identified by match to protein family HMM PF00037. | 0.461 |
| DVU_3364 | DVU_2753 | DVU_3364 | DVU_2753 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | Identified by match to protein family HMM TIGR01909. | 0.438 |
| DVU_3364 | aspS | DVU_3364 | DVU_3367 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.457 |
| DVU_3364 | def | DVU_3364 | DVU_3366 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | Polypeptide 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. | 0.619 |
| DVU_3364 | fmt | DVU_3364 | DVU_3365 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | methionyl-tRNA formyltransferase; 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. | 0.573 |
| DVU_3364 | hisS | DVU_3364 | DVU_3368 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | histidyl-tRNA synthetase; Identified by similarity to SP:P04804; match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442. | 0.439 |
| DVU_3364 | sun | DVU_3364 | DVU_3363 | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | Sun protein; Identified by match to protein family HMM PF01029; match to protein family HMM PF01189; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.563 |
| aspS | DVU_3364 | DVU_3367 | DVU_3364 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | 0.457 |
| aspS | def | DVU_3367 | DVU_3366 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Polypeptide 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. | 0.636 |
| aspS | fmt | DVU_3367 | DVU_3365 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | methionyl-tRNA formyltransferase; 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. | 0.560 |
| aspS | hisS | DVU_3367 | DVU_3368 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | histidyl-tRNA synthetase; Identified by similarity to SP:P04804; match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442. | 0.980 |
| aspS | sun | DVU_3367 | DVU_3363 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Sun protein; Identified by match to protein family HMM PF01029; match to protein family HMM PF01189; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.421 |
| def | DVU_3364 | DVU_3366 | DVU_3364 | Polypeptide 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. | Conserved hypothetical protein; Identified by similarity to OMNI:NTL01TT1406. | 0.619 |
| def | aspS | DVU_3366 | DVU_3367 | Polypeptide 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. | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.636 |
| def | fmt | DVU_3366 | DVU_3365 | Polypeptide 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. | methionyl-tRNA formyltransferase; 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. | 0.995 |
| def | hisS | DVU_3366 | DVU_3368 | Polypeptide 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. | histidyl-tRNA synthetase; Identified by similarity to SP:P04804; match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442. | 0.628 |
