| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RSc0521 | RSc0525 | RSc0521 | RSc0525 | Putative predicted metal-dependent hydrolase protein. | Probable signal peptide protein. | 0.548 |
| RSc0521 | glyQ | RSc0521 | RSc0526 | Putative predicted metal-dependent hydrolase protein. | Probable glycyl-trna synthetase alpha chain protein. | 0.623 |
| RSc0521 | glyS | RSc0521 | RSc0524 | Putative predicted metal-dependent hydrolase protein. | Probable glycyl-trna synthetase beta chain (glycine--trna ligasebeta chain) (glyrs) protein. | 0.759 |
| RSc0525 | RSc0521 | RSc0525 | RSc0521 | Probable signal peptide protein. | Putative predicted metal-dependent hydrolase protein. | 0.548 |
| RSc0525 | glyQ | RSc0525 | RSc0526 | Probable signal peptide protein. | Probable glycyl-trna synthetase alpha chain protein. | 0.773 |
| RSc0525 | glyS | RSc0525 | RSc0524 | Probable signal peptide protein. | Probable glycyl-trna synthetase beta chain (glycine--trna ligasebeta chain) (glyrs) protein. | 0.588 |
| alaS | aspS | RSc0797 | RSc0466 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | 0.912 |
| alaS | glyQ | RSc0797 | RSc0526 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable glycyl-trna synthetase alpha chain protein. | 0.721 |
| alaS | glyS | RSc0797 | RSc0524 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable glycyl-trna synthetase beta chain (glycine--trna ligasebeta chain) (glyrs) protein. | 0.746 |
| alaS | hisS | RSc0797 | RSc1216 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable histidyl-trna synthetase (histidine--trna ligase)(hisrs) protein. | 0.744 |
| alaS | ileS | RSc0797 | RSc2458 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable isoleucyl-trna synthetase protein; 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 1 subfamily. | 0.831 |
| alaS | pheS | RSc0797 | RSc1581 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable phenylalanyl-trna synthetase alpha chain (phenylalanine--trna ligase alpha chain) (phers) protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.609 |
| aspS | alaS | RSc0466 | RSc0797 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | 0.912 |
| aspS | glyQ | RSc0466 | RSc0526 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable glycyl-trna synthetase alpha chain protein. | 0.633 |
| aspS | glyS | RSc0466 | RSc0524 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable glycyl-trna synthetase beta chain (glycine--trna ligasebeta chain) (glyrs) protein. | 0.722 |
| aspS | hisS | RSc0466 | RSc1216 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable histidyl-trna synthetase (histidine--trna ligase)(hisrs) protein. | 0.934 |
| aspS | ileS | RSc0466 | RSc2458 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable isoleucyl-trna synthetase protein; 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 1 subfamily. | 0.805 |
| aspS | pheS | RSc0466 | RSc1581 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable phenylalanyl-trna synthetase alpha chain (phenylalanine--trna ligase alpha chain) (phers) protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.719 |
| atpH | glmU | RSc3320 | RSc0177 | Probable atp synthase delta chain protein; 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. | Probable udp-n-acetylglucosamine pyrophosphorylase protein; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat [...] | 0.402 |
| atpH | glyQ | RSc3320 | RSc0526 | Probable atp synthase delta chain protein; 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. | Probable glycyl-trna synthetase alpha chain protein. | 0.655 |