node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADR34179.1 | alaS | Sulku_1517 | Sulku_2228 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | 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. | 0.820 |
ADR34179.1 | aspS | Sulku_1517 | Sulku_1002 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | aspartate--tRNA(Asn) ligase; 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. | 0.983 |
ADR34179.1 | gatA | Sulku_1517 | Sulku_0788 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.997 |
ADR34179.1 | gatB | Sulku_1517 | Sulku_0822 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.965 |
ADR34179.1 | gatC | Sulku_1517 | Sulku_1172 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.997 |
ADR34179.1 | guaA | Sulku_1517 | Sulku_0331 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.980 |
ADR34179.1 | hisS | Sulku_1517 | Sulku_1234 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | COGs: COG0124 Histidyl-tRNA synthetase; InterPro IPR015807: IPR002314: IPR006195: IPR004516; KEGG: tdn:Suden_1130 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.668 |
ADR34179.1 | valS | Sulku_1517 | Sulku_0712 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | 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. | 0.763 |
ADR34482.1 | aspS | Sulku_1822 | Sulku_1002 | Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876; KEGG: sdl:Sdel_0752 protein of unknown function DUF28; PFAM: protein of unknown function DUF28; SPTR: UPF0082 protein Sdel_0752; PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | aspartate--tRNA(Asn) ligase; 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 |
adk-2 | aspS | Sulku_1001 | Sulku_1002 | Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | aspartate--tRNA(Asn) ligase; 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. | 0.845 |
adk-2 | guaA | Sulku_1001 | Sulku_0331 | Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.516 |
alaS | ADR34179.1 | Sulku_2228 | Sulku_1517 | 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: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | 0.820 |
alaS | aspS | Sulku_2228 | Sulku_1002 | 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. | aspartate--tRNA(Asn) ligase; 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. | 0.911 |
alaS | gatB | Sulku_2228 | Sulku_0822 | 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/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.410 |
alaS | guaA | Sulku_2228 | Sulku_0331 | 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. | 0.706 |
alaS | hisS | Sulku_2228 | Sulku_1234 | 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: COG0124 Histidyl-tRNA synthetase; InterPro IPR015807: IPR002314: IPR006195: IPR004516; KEGG: tdn:Suden_1130 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.636 |
alaS | valS | Sulku_2228 | Sulku_0712 | 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. | 0.869 |
aspS | ADR34179.1 | Sulku_1002 | Sulku_1517 | aspartate--tRNA(Asn) ligase; 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. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058: IPR020059: IPR018027: IPR001412: IPR 020060: IPR004514; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; GatB domain; TIGRFAM: glutaminyl-tRNA synthetase. | 0.983 |
aspS | ADR34482.1 | Sulku_1002 | Sulku_1822 | aspartate--tRNA(Asn) ligase; 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. | Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876; KEGG: sdl:Sdel_0752 protein of unknown function DUF28; PFAM: protein of unknown function DUF28; SPTR: UPF0082 protein Sdel_0752; PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | 0.825 |
aspS | adk-2 | Sulku_1002 | Sulku_1001 | aspartate--tRNA(Asn) ligase; 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. | Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | 0.845 |