| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEH44399.1 | alaS | Thein_0517 | Thein_2079 | COGs: COG0681 Signal peptidase I; InterProIPR000223:IPR019759:IPR019756:IPR019757:IPR 019758; KEGG: tye:THEYE_A0098 signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; PRIAM: Signal peptidase I; SPTR: Signal peptidase I; TIGRFAM: signal peptidase I; IMG reference gene:2505283811; PFAM: Peptidase S24-like; TIGRFAM: signal peptidase I, bacterial type. | 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. | 0.753 |
| AEH44399.1 | gltX | Thein_0517 | Thein_1322 | COGs: COG0681 Signal peptidase I; InterProIPR000223:IPR019759:IPR019756:IPR019757:IPR 019758; KEGG: tye:THEYE_A0098 signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; PRIAM: Signal peptidase I; SPTR: Signal peptidase I; TIGRFAM: signal peptidase I; IMG reference gene:2505283811; PFAM: Peptidase S24-like; TIGRFAM: signal peptidase I, bacterial type. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 0.564 |
| AEH44399.1 | metG | Thein_0517 | Thein_2120 | COGs: COG0681 Signal peptidase I; InterProIPR000223:IPR019759:IPR019756:IPR019757:IPR 019758; KEGG: tye:THEYE_A0098 signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; PRIAM: Signal peptidase I; SPTR: Signal peptidase I; TIGRFAM: signal peptidase I; IMG reference gene:2505283811; PFAM: Peptidase S24-like; TIGRFAM: signal peptidase I, bacterial type. | 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. | 0.592 |
| AEH44399.1 | secF | Thein_0517 | Thein_0169 | COGs: COG0681 Signal peptidase I; InterProIPR000223:IPR019759:IPR019756:IPR019757:IPR 019758; KEGG: tye:THEYE_A0098 signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; PRIAM: Signal peptidase I; SPTR: Signal peptidase I; TIGRFAM: signal peptidase I; IMG reference gene:2505283811; PFAM: Peptidase S24-like; TIGRFAM: signal peptidase I, bacterial type. | Protein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.838 |
| AEH45853.1 | alaS | Thein_2000 | Thein_2079 | Hypothetical protein; InterPro IPR018391; KEGG: dal:Dalk_4066 hypothetical protein; SPTR: Putative uncharacterized protein; IMG reference gene:2505285336. | 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. | 0.984 |
| alaS | AEH44399.1 | Thein_2079 | Thein_0517 | 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: COG0681 Signal peptidase I; InterProIPR000223:IPR019759:IPR019756:IPR019757:IPR 019758; KEGG: tye:THEYE_A0098 signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; PRIAM: Signal peptidase I; SPTR: Signal peptidase I; TIGRFAM: signal peptidase I; IMG reference gene:2505283811; PFAM: Peptidase S24-like; TIGRFAM: signal peptidase I, bacterial type. | 0.753 |
| alaS | AEH45853.1 | Thein_2079 | Thein_2000 | 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. | Hypothetical protein; InterPro IPR018391; KEGG: dal:Dalk_4066 hypothetical protein; SPTR: Putative uncharacterized protein; IMG reference gene:2505285336. | 0.984 |
| alaS | gltX | Thein_2079 | Thein_1322 | 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. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 0.796 |
| alaS | ileS | Thein_2079 | Thein_1381 | 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. | 0.803 |
| alaS | leuS | Thein_2079 | Thein_1827 | 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: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR001412:IPR015413:IPR013155; KEGG: ddf:DEFDS_0790 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; IMG reference gene:2505285153; 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. | 0.769 |
| alaS | metG | Thein_2079 | Thein_2120 | 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. | 0.869 |
| alaS | pheT | Thein_2079 | Thein_1597 | 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: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR004532:IPR002547:IPR005121:IPR005146:IPR 005147; KEGG: sfu:Sfum_0429 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; IMG reference gene:2505284919; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase [...] | 0.886 |
| alaS | secF | Thein_2079 | Thein_0169 | 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. | Protein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.842 |
| alaS | thrS | Thein_2079 | Thein_1592 | 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: COG0441 Threonyl-tRNA synthetase; InterProIPR018158:IPR002320:IPR006195:IPR004095:IPR 012947:IPR002314:IPR004154; KEGG: dak:DaAHT2_1245 threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Threonyl/alanyl tRNA synthetase SAD; TGS domain-containing protein; Anticodon-binding domain protein; SPTR: Threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; IMG reference gene:2505284914; PFAM: Anticodon binding domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: threonyl-tRNA synt [...] | 0.744 |
| alaS | valS | Thein_2079 | Thein_0907 | 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. | 0.842 |
| gltX | AEH44399.1 | Thein_1322 | Thein_0517 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | COGs: COG0681 Signal peptidase I; InterProIPR000223:IPR019759:IPR019756:IPR019757:IPR 019758; KEGG: tye:THEYE_A0098 signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; PRIAM: Signal peptidase I; SPTR: Signal peptidase I; TIGRFAM: signal peptidase I; IMG reference gene:2505283811; PFAM: Peptidase S24-like; TIGRFAM: signal peptidase I, bacterial type. | 0.564 |
| gltX | alaS | Thein_1322 | Thein_2079 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 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. | 0.796 |
| gltX | ileS | Thein_1322 | Thein_1381 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 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. | 0.919 |
| gltX | leuS | Thein_1322 | Thein_1827 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR001412:IPR015413:IPR013155; KEGG: ddf:DEFDS_0790 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; IMG reference gene:2505285153; 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. | 0.897 |
| gltX | metG | Thein_1322 | Thein_2120 | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 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. | 0.971 |