node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
UFO1_1656 | alaS | UFO1_1656 | UFO1_1929 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | Alanine-tRNA ligase, eukaryota/bacteria; 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. | 0.913 |
UFO1_1656 | aspS | UFO1_1656 | UFO1_1918 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | 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. | 0.719 |
UFO1_1656 | glyQ | UFO1_1656 | UFO1_2687 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | PFAM: glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; HAMAP : Glycyl-tRNA synthetase alpha subunit; KEGG: Glycyl-tRNA synthetase alpha subunit. | 0.671 |
UFO1_1656 | glyS | UFO1_1656 | UFO1_2686 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | TIGRFAM: glycyl-tRNA synthetase, beta subunit; HAMAP : Glycyl-tRNA synthetase beta subunit; KEGG: glyS, putative glycyl-tRNA synthetase beta subunit. | 0.645 |
UFO1_1656 | ileS | UFO1_1656 | UFO1_2320 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | 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. | 0.618 |
UFO1_1656 | ileS-2 | UFO1_1656 | UFO1_2412 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | 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. | 0.618 |
UFO1_1656 | leuS | UFO1_1656 | UFO1_2747 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | TIGRFAM: leucyl-tRNA synthetase; HAMAP : leucyl-tRNA synthetase class Ia; KEGG: leuS, putative leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.618 |
UFO1_1656 | proS | UFO1_1656 | UFO1_2537 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | 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 [...] | 0.510 |
UFO1_1656 | valS | UFO1_1656 | UFO1_2967 | KEGG: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | 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. | 0.764 |
UFO1_2685 | glyQ | UFO1_2685 | UFO1_2687 | Putative pyruvate, phosphate dikinase regulatory protein; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. | PFAM: glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; HAMAP : Glycyl-tRNA synthetase alpha subunit; KEGG: Glycyl-tRNA synthetase alpha subunit. | 0.586 |
UFO1_2685 | glyS | UFO1_2685 | UFO1_2686 | Putative pyruvate, phosphate dikinase regulatory protein; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. | TIGRFAM: glycyl-tRNA synthetase, beta subunit; HAMAP : Glycyl-tRNA synthetase beta subunit; KEGG: glyS, putative glycyl-tRNA synthetase beta subunit. | 0.727 |
alaS | UFO1_1656 | UFO1_1929 | UFO1_1656 | Alanine-tRNA ligase, eukaryota/bacteria; 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: truncated alanyl-tRNA synthetase; PFAM: Threonyl/alanyl tRNA synthetase SAD, Alanyl-tRNA synthetase, class IIc, phosphoesterase DHHA1; SMART: Threonyl/alanyl tRNA synthetase SAD. | 0.913 |
alaS | aspS | UFO1_1929 | UFO1_1918 | Alanine-tRNA ligase, eukaryota/bacteria; 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. | 0.767 |
alaS | glyQ | UFO1_1929 | UFO1_2687 | Alanine-tRNA ligase, eukaryota/bacteria; 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: glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; HAMAP : Glycyl-tRNA synthetase alpha subunit; KEGG: Glycyl-tRNA synthetase alpha subunit. | 0.671 |
alaS | glyS | UFO1_1929 | UFO1_2686 | Alanine-tRNA ligase, eukaryota/bacteria; 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. | TIGRFAM: glycyl-tRNA synthetase, beta subunit; HAMAP : Glycyl-tRNA synthetase beta subunit; KEGG: glyS, putative glycyl-tRNA synthetase beta subunit. | 0.648 |
alaS | ileS | UFO1_1929 | UFO1_2320 | Alanine-tRNA ligase, eukaryota/bacteria; 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. | 0.632 |
alaS | ileS-2 | UFO1_1929 | UFO1_2412 | Alanine-tRNA ligase, eukaryota/bacteria; 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. | 0.691 |
alaS | leuS | UFO1_1929 | UFO1_2747 | Alanine-tRNA ligase, eukaryota/bacteria; 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. | TIGRFAM: leucyl-tRNA synthetase; HAMAP : leucyl-tRNA synthetase class Ia; KEGG: leuS, putative leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.618 |
alaS | proS | UFO1_1929 | UFO1_2537 | Alanine-tRNA ligase, eukaryota/bacteria; 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 [...] | 0.536 |
alaS | valS | UFO1_1929 | UFO1_2967 | Alanine-tRNA ligase, eukaryota/bacteria; 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. | 0.812 |