node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFL97571.1 | valS | Ornrh_1398 | Ornrh_1397 | Putative membrane protein; PFAM: VIT family. | 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. | 0.773 |
AFL98263.1 | alaS | Ornrh_2131 | Ornrh_1287 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-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. | 0.672 |
AFL98263.1 | argS | Ornrh_2131 | Ornrh_0258 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 0.582 |
AFL98263.1 | aspS | Ornrh_2131 | Ornrh_0127 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.419 |
AFL98263.1 | guaA | Ornrh_2131 | Ornrh_1330 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.519 |
AFL98263.1 | lysS | Ornrh_2131 | Ornrh_0165 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | lysyl-tRNA synthetase (class II); PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.717 |
AFL98263.1 | pheT | Ornrh_2131 | Ornrh_2200 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.513 |
AFL98263.1 | valS | Ornrh_2131 | Ornrh_1397 | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-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. | 0.732 |
alaS | AFL98263.1 | Ornrh_1287 | Ornrh_2131 | 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: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | 0.672 |
alaS | argS | Ornrh_1287 | Ornrh_0258 | 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. | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 0.411 |
alaS | aspS | Ornrh_1287 | Ornrh_0127 | 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; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.843 |
alaS | guaA | Ornrh_1287 | Ornrh_1330 | 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. | 0.584 |
alaS | ileS | Ornrh_1287 | Ornrh_1989 | 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 2 subfamily. | 0.764 |
alaS | leuS | Ornrh_1287 | Ornrh_0971 | 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: 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. | 0.793 |
alaS | lysS | Ornrh_1287 | Ornrh_0165 | 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. | lysyl-tRNA synthetase (class II); PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.687 |
alaS | pheT | Ornrh_1287 | Ornrh_2200 | 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; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.825 |
alaS | valS | Ornrh_1287 | Ornrh_1397 | 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. | 0.794 |
argS | AFL98263.1 | Ornrh_0258 | Ornrh_2131 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | 0.582 |
argS | alaS | Ornrh_0258 | Ornrh_1287 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-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. | 0.411 |
argS | aspS | Ornrh_0258 | Ornrh_0127 | arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.529 |