node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABK70029.1 | aspS | MSMEG_3400 | MSMEG_3003 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF00392; match to protein family HMM PF01425; match to protein family HMM PF07729. | 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. | 0.598 |
ABK70029.1 | atpFH | MSMEG_3400 | MSMEG_4939 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF00392; match to protein family HMM PF01425; match to protein family HMM PF07729. | ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). | 0.512 |
ABK70029.1 | gatB | MSMEG_3400 | MSMEG_2367 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF00392; match to protein family HMM PF01425; match to protein family HMM PF07729. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.930 |
ABK70029.1 | gatC | MSMEG_3400 | MSMEG_2364 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF00392; match to protein family HMM PF01425; match to protein family HMM PF07729. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.873 |
ABK70548.1 | aspS | MSMEG_0485 | MSMEG_3003 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | 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. | 0.598 |
ABK70548.1 | atpFH | MSMEG_0485 | MSMEG_4939 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). | 0.478 |
ABK70548.1 | gatB | MSMEG_0485 | MSMEG_2367 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.942 |
ABK70548.1 | gatC | MSMEG_0485 | MSMEG_2364 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.891 |
ABK71083.1 | aspS | MSMEG_1090 | MSMEG_3003 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | 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. | 0.602 |
ABK71083.1 | atpFH | MSMEG_1090 | MSMEG_4939 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). | 0.478 |
ABK71083.1 | gatA | MSMEG_1090 | MSMEG_1088 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | glutamyl-tRNA(Gln)/aspartyl-tRNA(Asn) amidotransferase, A subunit; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | 0.663 |
ABK71083.1 | gatB | MSMEG_1090 | MSMEG_2367 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.928 |
ABK71083.1 | gatC | MSMEG_1090 | MSMEG_2364 | Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.903 |
ABK72052.1 | aspS | MSMEG_3970 | MSMEG_3003 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | 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. | 0.602 |
ABK72052.1 | atpFH | MSMEG_3970 | MSMEG_4939 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). | 0.480 |
ABK72052.1 | gatB | MSMEG_3970 | MSMEG_2367 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.928 |
ABK72052.1 | gatC | MSMEG_3970 | MSMEG_2364 | glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF01425; Belongs to the amidase family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.878 |
ABK72638.1 | aspS | MSMEG_2986 | MSMEG_3003 | Identified by match to protein family HMM PF01425; Belongs to the amidase family. | 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. | 0.603 |
ABK72638.1 | atpFH | MSMEG_2986 | MSMEG_4939 | Identified by match to protein family HMM PF01425; Belongs to the amidase family. | ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). | 0.479 |
ABK72638.1 | gatB | MSMEG_2986 | MSMEG_2367 | Identified by match to protein family HMM PF01425; Belongs to the amidase family. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.951 |