| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEJ62405.1 | valS | Spith_2150 | Spith_0441 | Quinolinate synthetase complex, A subunit; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 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. | 0.701 |
| alaS | argS | Spith_1371 | Spith_1048 | 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. | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | 0.543 |
| alaS | aspS | Spith_1371 | Spith_0145 | 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. | 0.808 |
| alaS | guaA | Spith_1371 | Spith_1028 | 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 (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.585 |
| alaS | ileS | Spith_1371 | Spith_1644 | 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. | Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.805 |
| alaS | leuS | Spith_1371 | Spith_0352 | 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. | PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR015945:IPR013155; KEGG: sta:STHERM_c03870 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Arginyl-tRNA synthetase, class Ic, core; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.836 |
| alaS | serS | Spith_1371 | Spith_1988 | 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. | 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). | 0.592 |
| alaS | valS | Spith_1371 | Spith_0441 | 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. | 0.872 |
| argS | alaS | Spith_1048 | Spith_1371 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | 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. | 0.543 |
| argS | aspS | Spith_1048 | Spith_0145 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | 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. | 0.604 |
| argS | guaA | Spith_1048 | Spith_1028 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.980 |
| argS | ileS | Spith_1048 | Spith_1644 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.935 |
| argS | leuS | Spith_1048 | Spith_0352 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR015945:IPR013155; KEGG: sta:STHERM_c03870 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Arginyl-tRNA synthetase, class Ic, core; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.811 |
| argS | rpoB | Spith_1048 | Spith_0512 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.615 |
| argS | serS | Spith_1048 | Spith_1988 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | 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). | 0.630 |
| argS | valS | Spith_1048 | Spith_0441 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | 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. | 0.693 |
| aspS | alaS | Spith_0145 | Spith_1371 | 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. | 0.808 |
| aspS | argS | Spith_0145 | Spith_1048 | 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. | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic. | 0.604 |
| aspS | guaA | Spith_0145 | Spith_1028 | 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 (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.827 |
| aspS | ileS | Spith_0145 | Spith_1644 | 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. | Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.678 |