| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Shew_0011 | glyQ | Shew_0011 | Shew_0010 | KEGG: shm:Shewmr7_0010 DNA-3-methyladenine glycosylase I; TIGRFAM: DNA-3-methyladenine glycosylase I; PFAM: methyladenine glycosylase. | Glycine--tRNA ligase; PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: shm:Shewmr7_0009 glycyl-tRNA synthetase, alpha subunit. | 0.595 |
| Shew_0011 | glyS | Shew_0011 | Shew_0009 | KEGG: shm:Shewmr7_0010 DNA-3-methyladenine glycosylase I; TIGRFAM: DNA-3-methyladenine glycosylase I; PFAM: methyladenine glycosylase. | Glycine--tRNA ligase; KEGG: shm:Shewmr7_0008 glycyl-tRNA synthetase, beta subunit. | 0.585 |
| Shew_3218 | alaS | Shew_3218 | Shew_1217 | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | 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. | 0.400 |
| Shew_3218 | atpH | Shew_3218 | Shew_3848 | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | 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. | 0.552 |
| Shew_3218 | glyQ | Shew_3218 | Shew_0010 | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | Glycine--tRNA ligase; PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: shm:Shewmr7_0009 glycyl-tRNA synthetase, alpha subunit. | 0.666 |
| Shew_3218 | guaA | Shew_3218 | Shew_1298 | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.845 |
| Shew_3218 | metG | Shew_3218 | Shew_1573 | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | 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. | 0.423 |
| Shew_3218 | pheS | Shew_3218 | Shew_2216 | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | KEGG: she:Shewmr4_1808 phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase, class IIc; aminoacyl tRNA synthetase, class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.579 |
| alaS | Shew_3218 | Shew_1217 | Shew_3218 | 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: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | 0.400 |
| alaS | glyQ | Shew_1217 | Shew_0010 | 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. | Glycine--tRNA ligase; PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: shm:Shewmr7_0009 glycyl-tRNA synthetase, alpha subunit. | 0.725 |
| alaS | glyS | Shew_1217 | Shew_0009 | 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. | Glycine--tRNA ligase; KEGG: shm:Shewmr7_0008 glycyl-tRNA synthetase, beta subunit. | 0.692 |
| alaS | guaA | Shew_1217 | Shew_1298 | 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. | 0.681 |
| alaS | hisS | Shew_1217 | Shew_1291 | 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. | KEGG: sfr:Sfri_1117 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 0.691 |
| alaS | ileS | Shew_1217 | Shew_1099 | 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 1 subfamily. | 0.795 |
| alaS | metG | Shew_1217 | Shew_1573 | 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. | 0.841 |
| alaS | pheS | Shew_1217 | Shew_2216 | 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. | KEGG: she:Shewmr4_1808 phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase, class IIc; aminoacyl tRNA synthetase, class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.531 |
| atpH | Shew_3218 | Shew_3848 | Shew_3218 | 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. | PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: she:Shewmr4_0696 carbamoyl-phosphate synthase L chain, ATP-binding. | 0.552 |
| atpH | glyQ | Shew_3848 | Shew_0010 | 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. | Glycine--tRNA ligase; PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: shm:Shewmr7_0009 glycyl-tRNA synthetase, alpha subunit. | 0.599 |
| atpH | glyS | Shew_3848 | Shew_0009 | 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. | Glycine--tRNA ligase; KEGG: shm:Shewmr7_0008 glycyl-tRNA synthetase, beta subunit. | 0.445 |
| glyQ | Shew_0011 | Shew_0010 | Shew_0011 | Glycine--tRNA ligase; PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: shm:Shewmr7_0009 glycyl-tRNA synthetase, alpha subunit. | KEGG: shm:Shewmr7_0010 DNA-3-methyladenine glycosylase I; TIGRFAM: DNA-3-methyladenine glycosylase I; PFAM: methyladenine glycosylase. | 0.595 |