| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EKY26350.1 | EKY26351.1 | HMPREF0216_01991 | HMPREF0216_01992 | Hypothetical protein; KEGG: tva:TVAG_387410 0.00070 viral A-type inclusion protein; K02331 DNA polymerase phi subunit; Psort location: Cytoplasmic, score: 7.50. | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.499 |
| EKY26351.1 | EKY26350.1 | HMPREF0216_01992 | HMPREF0216_01991 | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Hypothetical protein; KEGG: tva:TVAG_387410 0.00070 viral A-type inclusion protein; K02331 DNA polymerase phi subunit; Psort location: Cytoplasmic, score: 7.50. | 0.499 |
| EKY26351.1 | EKY26352.1 | HMPREF0216_01992 | HMPREF0216_01993 | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Hypothetical protein; KEGG: sds:SDEG_0334 1.9e-56 alpha/beta hydrolase K06889. | 0.488 |
| EKY26351.1 | guaA | HMPREF0216_01992 | HMPREF0216_03257 | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | 0.415 |
| EKY26351.1 | map | HMPREF0216_01992 | HMPREF0216_00499 | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.404 |
| EKY26351.1 | panC | HMPREF0216_01992 | HMPREF0216_00480 | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. | 0.437 |
| EKY26351.1 | proS | HMPREF0216_01992 | HMPREF0216_02430 | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 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 [...] | 0.495 |
| EKY26352.1 | EKY26351.1 | HMPREF0216_01993 | HMPREF0216_01992 | Hypothetical protein; KEGG: sds:SDEG_0334 1.9e-56 alpha/beta hydrolase K06889. | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.488 |
| guaA | EKY26351.1 | HMPREF0216_03257 | HMPREF0216_01992 | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.415 |
| guaA | map | HMPREF0216_03257 | HMPREF0216_00499 | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.964 |
| guaA | panC | HMPREF0216_03257 | HMPREF0216_00480 | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. | 0.612 |
| guaA | proS | HMPREF0216_03257 | HMPREF0216_02430 | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | 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 [...] | 0.745 |
| map | EKY26351.1 | HMPREF0216_00499 | HMPREF0216_01992 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.404 |
| map | guaA | HMPREF0216_00499 | HMPREF0216_03257 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | 0.964 |
| panC | EKY26351.1 | HMPREF0216_00480 | HMPREF0216_01992 | Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.437 |
| panC | guaA | HMPREF0216_00480 | HMPREF0216_03257 | Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | 0.612 |
| proS | EKY26351.1 | HMPREF0216_02430 | HMPREF0216_01992 | 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 [...] | Dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.495 |
| proS | guaA | HMPREF0216_02430 | HMPREF0216_03257 | 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 [...] | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | 0.745 |
STRING v12.5 is now available!
