| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | aspS | Deba_1140 | Deba_0878 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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. | 0.820 |
| alaS | atpH | Deba_1140 | Deba_0285 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | 0.418 |
| alaS | glyQ | Deba_1140 | Deba_1978 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR002310:IPR006194; KEGG: sat:SYN_01536 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit; PRIAM: Glycine--tRNA ligase; SPTR: Q2LVI0 Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit. | 0.778 |
| alaS | glyS | Deba_1140 | Deba_1977 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR002311:IPR008909:IPR006194:IPR015944; KEGG: gsu:GSU0579 glycyl-tRNA synthetase subunit beta; PFAM: glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain protein; PRIAM: Glycine--tRNA ligase; SPTR: Q1K046 Glycine--tRNA ligase; TIGRFAM: glycyl-tRNA synthetase, beta subunit; PFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit. | 0.729 |
| alaS | guaA | Deba_1140 | Deba_2372 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.682 |
| alaS | hisS | Deba_1140 | Deba_0877 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR015807:IPR006195:IPR004154:IPR002314:IPR 004516; KEGG: ppd:Ppro_1381 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: A1ANS7 Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; manually curated; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.786 |
| alaS | metG | Deba_1140 | Deba_0235 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.908 |
| alaS | pheS | Deba_1140 | Deba_0831 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; InterProIPR004529:IPR006195:IPR010978:IPR004188:IPR 002319; KEGG: sfu:Sfum_0428 phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; aminoacyl tRNA synthetase class II domain protein; SPTR: C8QYJ1 Phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA syn [...] | 0.535 |
| alaS | valS | Deba_1140 | Deba_2001 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.875 |
| aspS | alaS | Deba_0878 | Deba_1140 | 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. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.820 |
| aspS | glyQ | Deba_0878 | Deba_1978 | 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. | COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR002310:IPR006194; KEGG: sat:SYN_01536 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit; PRIAM: Glycine--tRNA ligase; SPTR: Q2LVI0 Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit. | 0.705 |
| aspS | glyS | Deba_0878 | Deba_1977 | 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. | COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR002311:IPR008909:IPR006194:IPR015944; KEGG: gsu:GSU0579 glycyl-tRNA synthetase subunit beta; PFAM: glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain protein; PRIAM: Glycine--tRNA ligase; SPTR: Q1K046 Glycine--tRNA ligase; TIGRFAM: glycyl-tRNA synthetase, beta subunit; PFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit. | 0.732 |
| aspS | guaA | Deba_0878 | Deba_2372 | 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. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.902 |
| aspS | hisS | Deba_0878 | Deba_0877 | 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. | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR015807:IPR006195:IPR004154:IPR002314:IPR 004516; KEGG: ppd:Ppro_1381 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: A1ANS7 Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; manually curated; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.960 |
| aspS | metG | Deba_0878 | Deba_0235 | 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 synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.752 |
| aspS | pheS | Deba_0878 | Deba_0831 | 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. | COGs: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; InterProIPR004529:IPR006195:IPR010978:IPR004188:IPR 002319; KEGG: sfu:Sfum_0428 phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; aminoacyl tRNA synthetase class II domain protein; SPTR: C8QYJ1 Phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA syn [...] | 0.713 |
| aspS | trmD | Deba_0878 | Deba_3165 | 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. | tRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. | 0.475 |
| aspS | valS | Deba_0878 | Deba_2001 | 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. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.868 |
| atpH | alaS | Deba_0285 | Deba_1140 | ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.418 |
| atpH | glyQ | Deba_0285 | Deba_1978 | ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR002310:IPR006194; KEGG: sat:SYN_01536 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit; PRIAM: Glycine--tRNA ligase; SPTR: Q2LVI0 Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit. | 0.682 |