node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | aspS | Mesil_2451 | Mesil_1884 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: 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; 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 2 subfamily. | 0.898 |
argS | glnS | Mesil_2451 | Mesil_1300 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058:IPR020060:IPR018027:IPR003789:IPR 011035:IPR020061:IPR004514:IPR020059; KEGG: dge:Dgeo_2188 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Asn/Gln amidotransferase; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SMART: Asn/Gln amidotransferase; SPTR: C1XXP8 Glutamyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; GatB domain; tRNA synthetases class I (E and Q), anti-codo [...] | 0.911 |
argS | gltX | Mesil_2451 | Mesil_1516 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.908 |
argS | ileS | Mesil_2451 | Mesil_2036 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 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. | 0.969 |
argS | leuS | Mesil_2451 | Mesil_1033 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | COGs: COG0495 Leucyl-tRNA synthetase; InterProIPR014729:IPR002302:IPR009008:IPR009080:IPR 001412:IPR015413:IPR013155; KEGG: tth:TTC1825 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: C1XM53 Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; 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. | 0.906 |
argS | lysS | Mesil_2451 | Mesil_2240 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | COGs: COG1190 Lysyl-tRNA synthetase (class II); InterProIPR018149:IPR002313:IPR004365:IPR012340:IPR 016027:IPR004364:IPR006195; KEGG: ttj:TTHA1041 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: C1XQ56 Lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; 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. | 0.886 |
argS | metG | Mesil_2451 | Mesil_1814 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.959 |
argS | pheT | Mesil_2451 | Mesil_3098 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR005121:IPR005146:IPR002547:IPR004532:IPR 005147:IPR020825:IPR012340:IPR016027:IPR009061; KEGG: tth:TTC1595 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/4 domain protein; tRNA synthetase B5; t-RNA-binding domain protein; ferredoxin-fold anticodon-binding; PRIAM: Phenylalanine--tRNA ligase; SMART: B3/4 domain protein; ferredoxin-fold anticodon-binding; tRNA synthetase B5; SPTR: C1XZG7 Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Fe [...] | 0.862 |
argS | proS | Mesil_2451 | Mesil_0089 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 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). | 0.950 |
argS | valS | Mesil_2451 | Mesil_2550 | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-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. | 0.764 |
aspS | argS | Mesil_1884 | Mesil_2451 | 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 2 subfamily. | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 0.898 |
aspS | glnS | Mesil_1884 | Mesil_1300 | 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 2 subfamily. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058:IPR020060:IPR018027:IPR003789:IPR 011035:IPR020061:IPR004514:IPR020059; KEGG: dge:Dgeo_2188 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Asn/Gln amidotransferase; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SMART: Asn/Gln amidotransferase; SPTR: C1XXP8 Glutamyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; GatB domain; tRNA synthetases class I (E and Q), anti-codo [...] | 0.794 |
aspS | gltX | Mesil_1884 | Mesil_1516 | 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 2 subfamily. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.636 |
aspS | ileS | Mesil_1884 | Mesil_2036 | 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 2 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 2 subfamily. | 0.824 |
aspS | leuS | Mesil_1884 | Mesil_1033 | 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 2 subfamily. | COGs: COG0495 Leucyl-tRNA synthetase; InterProIPR014729:IPR002302:IPR009008:IPR009080:IPR 001412:IPR015413:IPR013155; KEGG: tth:TTC1825 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: C1XM53 Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; 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. | 0.803 |
aspS | lysS | Mesil_1884 | Mesil_2240 | 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 2 subfamily. | COGs: COG1190 Lysyl-tRNA synthetase (class II); InterProIPR018149:IPR002313:IPR004365:IPR012340:IPR 016027:IPR004364:IPR006195; KEGG: ttj:TTHA1041 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: C1XQ56 Lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; 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. | 0.591 |
aspS | metG | Mesil_1884 | Mesil_1814 | 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 2 subfamily. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.956 |
aspS | pheT | Mesil_1884 | Mesil_3098 | 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 2 subfamily. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR005121:IPR005146:IPR002547:IPR004532:IPR 005147:IPR020825:IPR012340:IPR016027:IPR009061; KEGG: tth:TTC1595 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/4 domain protein; tRNA synthetase B5; t-RNA-binding domain protein; ferredoxin-fold anticodon-binding; PRIAM: Phenylalanine--tRNA ligase; SMART: B3/4 domain protein; ferredoxin-fold anticodon-binding; tRNA synthetase B5; SPTR: C1XZG7 Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Fe [...] | 0.710 |
aspS | proS | Mesil_1884 | Mesil_0089 | 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 2 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). | 0.879 |
glnS | argS | Mesil_1300 | Mesil_2451 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058:IPR020060:IPR018027:IPR003789:IPR 011035:IPR020061:IPR004514:IPR020059; KEGG: dge:Dgeo_2188 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Asn/Gln amidotransferase; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SMART: Asn/Gln amidotransferase; SPTR: C1XXP8 Glutamyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; GatB domain; tRNA synthetases class I (E and Q), anti-codo [...] | COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR015945:IPR014729:IPR008909:IPR009080:IPR 001412:IPR005148:IPR001278; KEGG: tth:TTC1906 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding domain protein; SPTR: C1XPJ2 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 0.911 |