| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP2015_7 | dnaA | PP2015_7 | PP2015_1 | Hypothetical protein. | Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. | 0.404 |
| PP2015_7 | glyQ | PP2015_7 | PP2015_5 | Hypothetical protein. | Pfam:pfam02091 Glycyl-tRNA synthetase alpha subunit. | 0.734 |
| PP2015_7 | glyS | PP2015_7 | PP2015_6 | Hypothetical protein. | Pfam:pfam02092 Glycyl-tRNA synthetase beta subunit. | 0.734 |
| alaS | glnS | PP2015_3481 | PP2015_1679 | Alanine--tRNA ligase; 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. | Glutamine--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. | 0.642 |
| alaS | glyQ | PP2015_3481 | PP2015_5 | Alanine--tRNA ligase; 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. | Pfam:pfam02091 Glycyl-tRNA synthetase alpha subunit. | 0.724 |
| alaS | glyS | PP2015_3481 | PP2015_6 | Alanine--tRNA ligase; 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. | Pfam:pfam02092 Glycyl-tRNA synthetase beta subunit. | 0.708 |
| alaS | hisS | PP2015_3481 | PP2015_509 | Alanine--tRNA ligase; 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. | Histidine--tRNA ligase; Pfam:pfam00587 tRNA synthetase class II core domain (G, H, P, S and T). | 0.589 |
| alaS | ileS | PP2015_3481 | PP2015_853 | Alanine--tRNA ligase; 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. | Isoleucine--tRNA ligase; 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 1 subfamily. | 0.806 |
| alaS | metG | PP2015_3481 | PP2015_1282 | Alanine--tRNA ligase; 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. | 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. | 0.891 |
| alaS | pheT | PP2015_3481 | PP2015_2354 | Alanine--tRNA ligase; 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. | Phenylalanine--tRNA ligase beta subunit; Pfam:pfam03483 B3/4 domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.862 |
| alaS | valS | PP2015_3481 | PP2015_2783 | Alanine--tRNA ligase; 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. | Valine--tRNA ligase; 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. | 0.896 |
| dnaA | PP2015_7 | PP2015_1 | PP2015_7 | Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. | Hypothetical protein. | 0.404 |
| dnaA | glyQ | PP2015_1 | PP2015_5 | Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. | Pfam:pfam02091 Glycyl-tRNA synthetase alpha subunit. | 0.724 |
| dnaA | glyS | PP2015_1 | PP2015_6 | Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. | Pfam:pfam02092 Glycyl-tRNA synthetase beta subunit. | 0.692 |
| dnaA | valS | PP2015_1 | PP2015_2783 | Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. | Valine--tRNA ligase; 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. | 0.506 |
| glnS | alaS | PP2015_1679 | PP2015_3481 | Glutamine--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. | Alanine--tRNA ligase; 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. | 0.642 |
| glnS | glyQ | PP2015_1679 | PP2015_5 | Glutamine--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. | Pfam:pfam02091 Glycyl-tRNA synthetase alpha subunit. | 0.612 |
| glnS | hisS | PP2015_1679 | PP2015_509 | Glutamine--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. | Histidine--tRNA ligase; Pfam:pfam00587 tRNA synthetase class II core domain (G, H, P, S and T). | 0.585 |
| glnS | ileS | PP2015_1679 | PP2015_853 | Glutamine--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. | Isoleucine--tRNA ligase; 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 1 subfamily. | 0.881 |
| glnS | metG | PP2015_1679 | PP2015_1282 | Glutamine--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. | 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. | 0.874 |