node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EJO17647.1 | EJO22304.1 | HMPREF1148_0046 | HMPREF1148_1163 | Putative chemotaxis protein CheC. | Methyltransferase CheR, SAM binding domain protein. | 0.825 |
EJO17647.1 | EJO22918.1 | HMPREF1148_0046 | HMPREF1148_0798 | Putative chemotaxis protein CheC. | Flagellar hook capping protein N-terminal domain protein. | 0.852 |
EJO17647.1 | fliE | HMPREF1148_0046 | HMPREF1148_0026 | Putative chemotaxis protein CheC. | Flagellar hook-basal body complex protein FliE. | 0.857 |
EJO17647.1 | fliN | HMPREF1148_0046 | HMPREF1148_0060 | Putative chemotaxis protein CheC. | Flagellar motor switch protein FliN. | 0.994 |
EJO17647.1 | proS | HMPREF1148_0046 | HMPREF1148_1165 | Putative chemotaxis protein CheC. | proline--tRNA ligase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.628 |
EJO17647.1 | ybaK | HMPREF1148_0046 | HMPREF1148_1557 | Putative chemotaxis protein CheC. | YbaK/EbsC protein; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. | 0.622 |
EJO22304.1 | EJO17647.1 | HMPREF1148_1163 | HMPREF1148_0046 | Methyltransferase CheR, SAM binding domain protein. | Putative chemotaxis protein CheC. | 0.825 |
EJO22304.1 | EJO22918.1 | HMPREF1148_1163 | HMPREF1148_0798 | Methyltransferase CheR, SAM binding domain protein. | Flagellar hook capping protein N-terminal domain protein. | 0.452 |
EJO22304.1 | fliE | HMPREF1148_1163 | HMPREF1148_0026 | Methyltransferase CheR, SAM binding domain protein. | Flagellar hook-basal body complex protein FliE. | 0.569 |
EJO22304.1 | fliN | HMPREF1148_1163 | HMPREF1148_0060 | Methyltransferase CheR, SAM binding domain protein. | Flagellar motor switch protein FliN. | 0.920 |
EJO22304.1 | proS | HMPREF1148_1163 | HMPREF1148_1165 | Methyltransferase CheR, SAM binding domain protein. | proline--tRNA ligase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.786 |
EJO22304.1 | ybaK | HMPREF1148_1163 | HMPREF1148_1557 | Methyltransferase CheR, SAM binding domain protein. | YbaK/EbsC protein; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. | 0.622 |
EJO22918.1 | EJO17647.1 | HMPREF1148_0798 | HMPREF1148_0046 | Flagellar hook capping protein N-terminal domain protein. | Putative chemotaxis protein CheC. | 0.852 |
EJO22918.1 | EJO22304.1 | HMPREF1148_0798 | HMPREF1148_1163 | Flagellar hook capping protein N-terminal domain protein. | Methyltransferase CheR, SAM binding domain protein. | 0.452 |
EJO22918.1 | fliE | HMPREF1148_0798 | HMPREF1148_0026 | Flagellar hook capping protein N-terminal domain protein. | Flagellar hook-basal body complex protein FliE. | 0.996 |
EJO22918.1 | fliN | HMPREF1148_0798 | HMPREF1148_0060 | Flagellar hook capping protein N-terminal domain protein. | Flagellar motor switch protein FliN. | 0.968 |
EJO22918.1 | proS | HMPREF1148_0798 | HMPREF1148_1165 | Flagellar hook capping protein N-terminal domain protein. | proline--tRNA ligase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.622 |
EJO22918.1 | ybaK | HMPREF1148_0798 | HMPREF1148_1557 | Flagellar hook capping protein N-terminal domain protein. | YbaK/EbsC protein; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. | 0.622 |
aspS | metG | HMPREF1148_0832 | HMPREF1148_0401 | aspartate--tRNA ligase; 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. | Putative methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.814 |
aspS | proS | HMPREF1148_0832 | HMPREF1148_1165 | aspartate--tRNA ligase; 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. | proline--tRNA ligase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.779 |