node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | aspS-2 | Marky_0762 | Marky_1319 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 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. | 0.851 |
argS | glnS | Marky_0762 | Marky_1626 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; HAMAP: Glutaminyl-tRNA synthetase, bacterial; InterProIPR020058:IPR020059:IPR018027:IPR004514:IPR 022861; KEGG: tra:Trad_2932 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; PRIAM: Glutamine--tRNA ligase; SMART: Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; IMG reference gene:2504661234; PFAM: tRNA synthetases class I (E a [...] | 0.915 |
argS | gltX | Marky_0762 | Marky_0769 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 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). | 0.923 |
argS | ileS | Marky_0762 | Marky_1232 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 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. | 0.974 |
argS | leuS | Marky_0762 | Marky_1980 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR015413:IPR013155; KEGG: ttj:TTHA0161 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); PRIAM: Valine--tRNA ligase., Leucine--tRNA ligase; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; IMG reference gene:2504661594; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family. | 0.921 |
argS | lysS | Marky_0762 | Marky_1108 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | COGs: COG1190 Lysyl-tRNA synthetase (class II); HAMAP: Lysyl-tRNA synthetase, class II; InterPro IPR002313:IPR004365:IPR004364; KEGG: opr:Ocepr_1046 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Lysine--tRNA ligase; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; IMG reference gene:2504660699; 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 aminoacy [...] | 0.906 |
argS | metG | Marky_0762 | Marky_1180 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 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. | 0.950 |
argS | pheT | Marky_0762 | Marky_1783 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterProIPR002547:IPR005146:IPR005147:IPR005121:IPR 004532; KEGG: opr:Ocepr_1546 phenylalanyl-tRNA synthetase beta subunit; PFAM: B3/B4 tRNA-binding domain; tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SMART: B3/B4 tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase, beta subunit; [...] | 0.852 |
argS | proS | Marky_0762 | Marky_2124 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 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). | 0.957 |
argS | valS | Marky_0762 | Marky_0868 | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 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. | 0.737 |
aspS-2 | argS | Marky_1319 | Marky_0762 | 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; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 0.851 |
aspS-2 | glnS | Marky_1319 | Marky_1626 | 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; HAMAP: Glutaminyl-tRNA synthetase, bacterial; InterProIPR020058:IPR020059:IPR018027:IPR004514:IPR 022861; KEGG: tra:Trad_2932 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; PRIAM: Glutamine--tRNA ligase; SMART: Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; IMG reference gene:2504661234; PFAM: tRNA synthetases class I (E a [...] | 0.721 |
aspS-2 | gltX | Marky_1319 | Marky_0769 | 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). | 0.586 |
aspS-2 | ileS | Marky_1319 | Marky_1232 | 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. | 0.835 |
aspS-2 | leuS | Marky_1319 | Marky_1980 | 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; InterPro IPR002302:IPR015413:IPR013155; KEGG: ttj:TTHA0161 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); PRIAM: Valine--tRNA ligase., Leucine--tRNA ligase; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; IMG reference gene:2504661594; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family. | 0.708 |
aspS-2 | lysS | Marky_1319 | Marky_1108 | 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); HAMAP: Lysyl-tRNA synthetase, class II; InterPro IPR002313:IPR004365:IPR004364; KEGG: opr:Ocepr_1046 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Lysine--tRNA ligase; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; IMG reference gene:2504660699; 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 aminoacy [...] | 0.562 |
aspS-2 | metG | Marky_1319 | Marky_1180 | 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. | 0.944 |
aspS-2 | pheT | Marky_1319 | Marky_1783 | 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; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterProIPR002547:IPR005146:IPR005147:IPR005121:IPR 004532; KEGG: opr:Ocepr_1546 phenylalanyl-tRNA synthetase beta subunit; PFAM: B3/B4 tRNA-binding domain; tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SMART: B3/B4 tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase, beta subunit; [...] | 0.710 |
aspS-2 | proS | Marky_1319 | Marky_2124 | 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). | 0.868 |
glnS | argS | Marky_1626 | Marky_0762 | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; HAMAP: Glutaminyl-tRNA synthetase, bacterial; InterProIPR020058:IPR020059:IPR018027:IPR004514:IPR 022861; KEGG: tra:Trad_2932 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; PRIAM: Glutamine--tRNA ligase; SMART: Asn/Gln amidotransferase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; IMG reference gene:2504661234; PFAM: tRNA synthetases class I (E a [...] | COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: opr:Ocepr_1555 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl tRNA synthetase, class Ic, N-terminal; Arginyl-tRNA synthetase, class Ic, core; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; IMG reference gene:2504660350; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRN [...] | 0.915 |