node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Psed_3574 | Psed_3576 | Psed_3574 | Psed_3576 | PFAM: Methyltransferase type 12; KEGG: msp:Mspyr1_25700 ribosomal protein L11 methylase. | KEGG: ami:Amir_1700 beta-lactamase domain protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | 0.777 |
Psed_3574 | hisS | Psed_3574 | Psed_3575 | PFAM: Methyltransferase type 12; KEGG: msp:Mspyr1_25700 ribosomal protein L11 methylase. | PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: nfa:nfa36640 histidyl-tRNA synthetase. | 0.804 |
Psed_3576 | Psed_3574 | Psed_3576 | Psed_3574 | KEGG: ami:Amir_1700 beta-lactamase domain protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | PFAM: Methyltransferase type 12; KEGG: msp:Mspyr1_25700 ribosomal protein L11 methylase. | 0.777 |
Psed_3576 | aspS | Psed_3576 | Psed_3570 | KEGG: ami:Amir_1700 beta-lactamase domain protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | 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. | 0.405 |
Psed_3576 | hisS | Psed_3576 | Psed_3575 | KEGG: ami:Amir_1700 beta-lactamase domain protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: nfa:nfa36640 histidyl-tRNA synthetase. | 0.841 |
argS | aspS | Psed_1662 | Psed_3570 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | 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. | 0.674 |
argS | guaA | Psed_1662 | Psed_5346 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.983 |
argS | hisS | Psed_1662 | Psed_3575 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: nfa:nfa36640 histidyl-tRNA synthetase. | 0.800 |
argS | lysS | Psed_1662 | Psed_6116 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; TIGRFAM: Lysyl-tRNA synthetase, class II; HAMAP: Lysyl-tRNA synthetase, class II; KEGG: gob:Gobs_0637 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.933 |
argS | pheT | Psed_1662 | Psed_3838 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: amd:AMED_6050 phenylalanyl-tRNA synthetase beta chain; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.947 |
argS | thrS | Psed_1662 | Psed_3613 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | TIGRFAM: Threonyl-tRNA synthetase, class IIa; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Threonyl/alanyl tRNA synthetase, SAD; Anticodon-binding; KEGG: svi:Svir_14910 threonyl-tRNA synthetase; SMART: Threonyl/alanyl tRNA synthetase, SAD; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.706 |
argS | valS | Psed_1662 | Psed_1973 | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | 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. | 0.912 |
aspS | Psed_3576 | Psed_3570 | Psed_3576 | 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. | KEGG: ami:Amir_1700 beta-lactamase domain protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | 0.405 |
aspS | argS | Psed_3570 | Psed_1662 | 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. | KEGG: sen:SACE_6300 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. | 0.674 |
aspS | guaA | Psed_3570 | Psed_5346 | 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. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.841 |
aspS | hisS | Psed_3570 | Psed_3575 | 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. | PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: nfa:nfa36640 histidyl-tRNA synthetase. | 0.882 |
aspS | lysS | Psed_3570 | Psed_6116 | 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. | PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; TIGRFAM: Lysyl-tRNA synthetase, class II; HAMAP: Lysyl-tRNA synthetase, class II; KEGG: gob:Gobs_0637 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.630 |
aspS | pheT | Psed_3570 | Psed_3838 | 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. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: amd:AMED_6050 phenylalanyl-tRNA synthetase beta chain; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.919 |
aspS | thrS | Psed_3570 | Psed_3613 | 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. | TIGRFAM: Threonyl-tRNA synthetase, class IIa; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Threonyl/alanyl tRNA synthetase, SAD; Anticodon-binding; KEGG: svi:Svir_14910 threonyl-tRNA synthetase; SMART: Threonyl/alanyl tRNA synthetase, SAD; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.767 |
aspS | valS | Psed_3570 | Psed_1973 | 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. | 0.822 |