| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABO_0007 | glyQ | ABO_0007 | ABO_0009 | Histidinol-phosphatase, putatitve; Identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00213; Function unclear. | (glycyl-tRNA synthetase tetrameric type alphasubunit) identified by sequence similarity; putative InterPro: Glycyl-tRNA synthetase alpha subunit; High confidence in function and specificity. | 0.590 |
| ABO_0007 | glyS | ABO_0007 | ABO_0008 | Histidinol-phosphatase, putatitve; Identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00213; Function unclear. | (glycyl-tRNA synthetase tetrameric type betasubunit) identified by match to TIGR protein family HMMTIGR00211 InterPro: Glycyl-tRNA synthetase beta subunit; High confidence in function and specificity. | 0.591 |
| ABO_0007 | tag | ABO_0007 | ABO_0010 | Histidinol-phosphatase, putatitve; Identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00213; Function unclear. | DNA-3-methyladenine glycosidase I; Identified by sequencesimilarity; putative InterPro: DNA-3-methyladenine glycosylase I; High confidence in function and specificity. | 0.467 |
| alarS | aspS | ABO_1798 | ABO_0749 | (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. | 0.825 |
| alarS | glyQ | ABO_1798 | ABO_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. | (glycyl-tRNA synthetase tetrameric type alphasubunit) identified by sequence similarity; putative InterPro: Glycyl-tRNA synthetase alpha subunit; High confidence in function and specificity. | 0.696 |
| alarS | glyS | ABO_1798 | ABO_0008 | (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. | (glycyl-tRNA synthetase tetrameric type betasubunit) identified by match to TIGR protein family HMMTIGR00211 InterPro: Glycyl-tRNA synthetase beta subunit; High confidence in function and specificity. | 0.686 |
| alarS | ileS | ABO_1798 | ABO_0459 | (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. | 0.735 |
| alarS | leuS | ABO_1798 | ABO_1947 | (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) identified by sequencesimilarity; putative InterPro: Leucyl-tRNA synthetase; High confidence in function and specificity; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.789 |
| alarS | pheT | ABO_1798 | ABO_1837 | (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. | Phenylalanyl-tRNA synthetase, beta subunit; Identified by sequence similarity; putative; High confidence in function and specificity; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.831 |
| alarS | proS | ABO_1798 | ABO_0739 | (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. | Prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.525 |
| alarS | valS | ABO_1798 | ABO_0492 | (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. | 0.866 |
| aspS | alarS | ABO_0749 | ABO_1798 | 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. | 0.825 |
| aspS | glyQ | ABO_0749 | ABO_0009 | 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. | (glycyl-tRNA synthetase tetrameric type alphasubunit) identified by sequence similarity; putative InterPro: Glycyl-tRNA synthetase alpha subunit; High confidence in function and specificity. | 0.530 |
| aspS | glyS | ABO_0749 | ABO_0008 | 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. | (glycyl-tRNA synthetase tetrameric type betasubunit) identified by match to TIGR protein family HMMTIGR00211 InterPro: Glycyl-tRNA synthetase beta subunit; High confidence in function and specificity. | 0.602 |
| aspS | ileS | ABO_0749 | ABO_0459 | 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 1 subfamily. | 0.578 |
| aspS | leuS | ABO_0749 | ABO_1947 | 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) identified by sequencesimilarity; putative InterPro: Leucyl-tRNA synthetase; High confidence in function and specificity; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.522 |
| aspS | pheT | ABO_0749 | ABO_1837 | 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. | Phenylalanyl-tRNA synthetase, beta subunit; Identified by sequence similarity; putative; High confidence in function and specificity; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.842 |
| aspS | proS | ABO_0749 | ABO_0739 | 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. | Prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.702 |
| aspS | valS | ABO_0749 | ABO_0492 | 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. | 0.832 |
| glyQ | ABO_0007 | ABO_0009 | ABO_0007 | (glycyl-tRNA synthetase tetrameric type alphasubunit) identified by sequence similarity; putative InterPro: Glycyl-tRNA synthetase alpha subunit; High confidence in function and specificity. | Histidinol-phosphatase, putatitve; Identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00213; Function unclear. | 0.590 |