| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| argS | aspC | Natgr_0694 | Natgr_2086 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | aspartyl-tRNA synthetase, archaeal type; 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). | 0.871 |
| argS | cysS | Natgr_0694 | Natgr_3816 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | PFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase. | 0.781 |
| argS | glyS | Natgr_0694 | Natgr_1431 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | glycyl-tRNA synthetase, dimeric type; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: glycyl-tRNA synthetase, dimeric type. | 0.818 |
| argS | hisS | Natgr_0694 | Natgr_2429 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.738 |
| argS | leuS | Natgr_0694 | Natgr_1393 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.679 |
| argS | lysS | Natgr_0694 | Natgr_3390 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | lysyl-tRNA synthetase (class II); PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.891 |
| argS | pyrG | Natgr_0694 | Natgr_1008 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.910 |
| argS | serS | Natgr_0694 | Natgr_1213 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.822 |
| argS | thrS | Natgr_0694 | Natgr_2477 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | threonyl-tRNA synthetase; PFAM: Anticodon binding domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetase class II core domain (G, H, P, S and T); TGS domain; TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.784 |
| aspC | argS | Natgr_2086 | Natgr_0694 | aspartyl-tRNA synthetase, archaeal type; 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). | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.871 |
| aspC | cysS | Natgr_2086 | Natgr_3816 | aspartyl-tRNA synthetase, archaeal type; 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). | PFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase. | 0.671 |
| aspC | glyS | Natgr_2086 | Natgr_1431 | aspartyl-tRNA synthetase, archaeal type; 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). | glycyl-tRNA synthetase, dimeric type; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: glycyl-tRNA synthetase, dimeric type. | 0.845 |
| aspC | hisS | Natgr_2086 | Natgr_2429 | aspartyl-tRNA synthetase, archaeal type; 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). | PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.707 |
| aspC | leuS | Natgr_2086 | Natgr_1393 | aspartyl-tRNA synthetase, archaeal type; 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). | PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.502 |
| aspC | lysS | Natgr_2086 | Natgr_3390 | aspartyl-tRNA synthetase, archaeal type; 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). | lysyl-tRNA synthetase (class II); PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.785 |
| aspC | serS | Natgr_2086 | Natgr_1213 | aspartyl-tRNA synthetase, archaeal type; 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). | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.747 |
| aspC | thrS | Natgr_2086 | Natgr_2477 | aspartyl-tRNA synthetase, archaeal type; 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). | threonyl-tRNA synthetase; PFAM: Anticodon binding domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetase class II core domain (G, H, P, S and T); TGS domain; TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.571 |
| aspC | topA | Natgr_2086 | Natgr_0834 | aspartyl-tRNA synthetase, archaeal type; 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). | Topoisomerase IA; 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 superco [...] | 0.721 |
| cysS | argS | Natgr_3816 | Natgr_0694 | PFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase. | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.781 |
| cysS | aspC | Natgr_3816 | Natgr_2086 | PFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase. | aspartyl-tRNA synthetase, archaeal type; 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). | 0.671 |