node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mmah_0623 | aspS | Mmah_0623 | Mmah_0849 | COGs: COG0340 Biotin-(acetyl-CoA carboxylase) ligase; InterPro IPR003142:IPR013196:IPR004143:IPR004408; KEGG: gur:Gura_2817 biotin--acetyl-CoA-carboxylase ligase; PFAM: biotin/lipoate A/B protein ligase; Helix-turn-helix type 11 domain protein; biotin protein ligase domain protein; SPTR: Q8PVX6 Biotin--[acetyl-COA-carboxylase] synthetase; TIGRFAM: biotin/acetyl-CoA-carboxylase ligase; PFAM: HTH domain; Biotin protein ligase C terminal domain; Biotin/lipoate A/B protein ligase family; TIGRFAM: birA, biotin-[acetyl-CoA-carboxylase] ligase region; BirA biotin operon repressor domain. | 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). | 0.843 |
alaS | aspS | Mmah_0370 | Mmah_0849 | 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; 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). | 0.721 |
alaS | glyS | Mmah_0370 | Mmah_0690 | 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. | glycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). | 0.775 |
alaS | hisS | Mmah_0370 | Mmah_1484 | 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 IPR002314:IPR004154:IPR006195:IPR015807; KEGG: sat:SYN_02534 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Q12TM4 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; ATP phosphoribosyltransferase, regulatory subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.797 |
alaS | pheS | Mmah_0370 | Mmah_1736 | 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: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; InterPro IPR002319:IPR006195:IPR004529; KEGG: similar to predicted protein; K01889 phenylalanyl-tRNA synthetase alpha chain; PFAM: phenylalanyl-tRNA synthetase class IIc; PRIAM: Phenylalanine--tRNA ligase; SPTR: Q12W38 Phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit. | 0.515 |
alaS | pheT | Mmah_0370 | Mmah_1326 | 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: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterPro IPR005146:IPR005147:IPR004531; KEGG: phenylalanyl-tRNA synthetase beta chain (EC:6.1.1.20); K01890 phenylalanyl-tRNA synthetase beta chain; PFAM: tRNA synthetase B5; B3/4 domain protein; PRIAM: Phenylalanine--tRNA ligase; SPTR: Q12YP2 Phenylalanyl-tRNA synthetase beta chain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetases class II core domain (F); tRNA synthetase B5 domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.644 |
alaS | proS | Mmah_0370 | Mmah_0787 | 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. | 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). | 0.607 |
alaS | serS | Mmah_0370 | Mmah_1469 | 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. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec); Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily. | 0.651 |
alaS | thrS | Mmah_0370 | Mmah_1630 | 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. | Ser-tRNA(Thr) hydrolase; COGs: COG0441 Threonyl-tRNA synthetase; InterProIPR018158:IPR002314:IPR004154:IPR015011:IPR 006195:IPR002320; KEGG: dma:DMR_10590 threonyl-tRNA synthetase; PFAM: Threonyl-tRNA synthetase editing domain protein; Anticodon-binding domain protein; tRNA synthetase class II (G H P and S); SPTR: Q12WD4 Threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); Archaea-specific editing domain of threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II [...] | 0.588 |
aspS | Mmah_0623 | Mmah_0849 | Mmah_0623 | 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). | COGs: COG0340 Biotin-(acetyl-CoA carboxylase) ligase; InterPro IPR003142:IPR013196:IPR004143:IPR004408; KEGG: gur:Gura_2817 biotin--acetyl-CoA-carboxylase ligase; PFAM: biotin/lipoate A/B protein ligase; Helix-turn-helix type 11 domain protein; biotin protein ligase domain protein; SPTR: Q8PVX6 Biotin--[acetyl-COA-carboxylase] synthetase; TIGRFAM: biotin/acetyl-CoA-carboxylase ligase; PFAM: HTH domain; Biotin protein ligase C terminal domain; Biotin/lipoate A/B protein ligase family; TIGRFAM: birA, biotin-[acetyl-CoA-carboxylase] ligase region; BirA biotin operon repressor domain. | 0.843 |
aspS | alaS | Mmah_0849 | Mmah_0370 | 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). | 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. | 0.721 |
aspS | glyS | Mmah_0849 | Mmah_0690 | 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). | glycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). | 0.760 |
aspS | hisS | Mmah_0849 | Mmah_1484 | 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). | COGs: COG0124 Histidyl-tRNA synthetase; InterPro IPR002314:IPR004154:IPR006195:IPR015807; KEGG: sat:SYN_02534 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Q12TM4 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; ATP phosphoribosyltransferase, regulatory subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.709 |
aspS | pheS | Mmah_0849 | Mmah_1736 | 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). | COGs: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; InterPro IPR002319:IPR006195:IPR004529; KEGG: similar to predicted protein; K01889 phenylalanyl-tRNA synthetase alpha chain; PFAM: phenylalanyl-tRNA synthetase class IIc; PRIAM: Phenylalanine--tRNA ligase; SPTR: Q12W38 Phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit. | 0.585 |
aspS | pheT | Mmah_0849 | Mmah_1326 | 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). | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterPro IPR005146:IPR005147:IPR004531; KEGG: phenylalanyl-tRNA synthetase beta chain (EC:6.1.1.20); K01890 phenylalanyl-tRNA synthetase beta chain; PFAM: tRNA synthetase B5; B3/4 domain protein; PRIAM: Phenylalanine--tRNA ligase; SPTR: Q12YP2 Phenylalanyl-tRNA synthetase beta chain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetases class II core domain (F); tRNA synthetase B5 domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.565 |
aspS | proS | Mmah_0849 | Mmah_0787 | 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). | 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). | 0.844 |
aspS | sepS | Mmah_0849 | Mmah_0685 | 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). | phosphoserine-tRNA(Cys) ligase; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys). | 0.625 |
aspS | serS | Mmah_0849 | Mmah_1469 | 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). | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec); Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily. | 0.717 |
aspS | thrS | Mmah_0849 | Mmah_1630 | 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). | Ser-tRNA(Thr) hydrolase; COGs: COG0441 Threonyl-tRNA synthetase; InterProIPR018158:IPR002314:IPR004154:IPR015011:IPR 006195:IPR002320; KEGG: dma:DMR_10590 threonyl-tRNA synthetase; PFAM: Threonyl-tRNA synthetase editing domain protein; Anticodon-binding domain protein; tRNA synthetase class II (G H P and S); SPTR: Q12WD4 Threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); Archaea-specific editing domain of threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II [...] | 0.561 |
glyS | alaS | Mmah_0690 | Mmah_0370 | glycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). | 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. | 0.775 |