| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0934 | MJ_0935 | MJ_0934 | MJ_0935 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.952 |
| MJ_0934 | MJ_0936 | MJ_0934 | MJ_0936 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.597 |
| MJ_0934 | purD | MJ_0934 | MJ_0937 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.432 |
| MJ_0935 | MJ_0934 | MJ_0935 | MJ_0934 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.952 |
| MJ_0935 | MJ_0936 | MJ_0935 | MJ_0936 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.816 |
| MJ_0935 | MJ_1020 | MJ_0935 | MJ_1020 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ1020. | 0.431 |
| MJ_0935 | MJ_1317 | MJ_0935 | MJ_1317 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Hypothetical protein; Similar to GP:1449355 percent identity: 24.14; identified by sequence similarity; putative. | 0.472 |
| MJ_0935 | MJ_1560 | MJ_0935 | MJ_1560 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Multidrug-efflux transporter (bmr1); Similar to GB:L25604 SP:P33449 GB:M33768 PID:142606 PID:409287 percent identity: 28.57; identified by sequence similarity; putative. | 0.472 |
| MJ_0935 | alaS | MJ_0935 | MJ_0564 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | alanyl-tRNA synthetase (alaS); 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) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala). | 0.501 |
| MJ_0935 | purD | MJ_0935 | MJ_0937 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.448 |
| MJ_0935 | rtcA | MJ_0935 | MJ_0025 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Hypothetical protein; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). | 0.447 |
| MJ_0936 | MJ_0934 | MJ_0936 | MJ_0934 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.597 |
| MJ_0936 | MJ_0935 | MJ_0936 | MJ_0935 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.816 |
| MJ_0936 | purD | MJ_0936 | MJ_0937 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.898 |
| MJ_1020 | MJ_0935 | MJ_1020 | MJ_0935 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ1020. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.431 |
| MJ_1317 | MJ_0935 | MJ_1317 | MJ_0935 | Hypothetical protein; Similar to GP:1449355 percent identity: 24.14; identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.472 |
| MJ_1560 | MJ_0935 | MJ_1560 | MJ_0935 | Multidrug-efflux transporter (bmr1); Similar to GB:L25604 SP:P33449 GB:M33768 PID:142606 PID:409287 percent identity: 28.57; identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.472 |
| alaS | MJ_0935 | MJ_0564 | MJ_0935 | alanyl-tRNA synthetase (alaS); 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) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala). | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.501 |
| alaS | purD | MJ_0564 | MJ_0937 | alanyl-tRNA synthetase (alaS); 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) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala). | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.487 |
| purD | MJ_0934 | MJ_0937 | MJ_0934 | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.432 |