| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0039 | MJ_0168 | MJ_0039 | MJ_0168 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 44.44; identified by sequence similarity; putative. | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | 0.427 |
| MJ_0039 | MJ_0831 | MJ_0039 | MJ_0831 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 44.44; identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 35.87; identified by sequence similarity; putative; To M.jannaschii MJ0977. | 0.639 |
| MJ_0164 | MJ_0165 | MJ_0164 | MJ_0165 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0164. | Conserved hypothetical protein; Similar to GP:1653798 percent identity: 43.43; identified by sequence similarity; putative. | 0.927 |
| MJ_0164 | MJ_0168 | MJ_0164 | MJ_0168 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0164. | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | 0.443 |
| MJ_0164 | dtdA | MJ_0164 | MJ_0166 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0164. | Conserved hypothetical protein; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. | 0.853 |
| MJ_0164 | moaB | MJ_0164 | MJ_0167 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0164. | Molybdenum cofactor biosynthesis protein (moaB); Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor. | 0.681 |
| MJ_0165 | MJ_0164 | MJ_0165 | MJ_0164 | Conserved hypothetical protein; Similar to GP:1653798 percent identity: 43.43; identified by sequence similarity; putative. | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0164. | 0.927 |
| MJ_0165 | MJ_0168 | MJ_0165 | MJ_0168 | Conserved hypothetical protein; Similar to GP:1653798 percent identity: 43.43; identified by sequence similarity; putative. | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | 0.443 |
| MJ_0165 | dtdA | MJ_0165 | MJ_0166 | Conserved hypothetical protein; Similar to GP:1653798 percent identity: 43.43; identified by sequence similarity; putative. | Conserved hypothetical protein; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. | 0.931 |
| MJ_0165 | moaB | MJ_0165 | MJ_0167 | Conserved hypothetical protein; Similar to GP:1653798 percent identity: 43.43; identified by sequence similarity; putative. | Molybdenum cofactor biosynthesis protein (moaB); Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor. | 0.894 |
| MJ_0168 | MJ_0039 | MJ_0168 | MJ_0039 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 44.44; identified by sequence similarity; putative. | 0.427 |
| MJ_0168 | MJ_0164 | MJ_0168 | MJ_0164 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0164. | 0.443 |
| MJ_0168 | MJ_0165 | MJ_0168 | MJ_0165 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Conserved hypothetical protein; Similar to GP:1653798 percent identity: 43.43; identified by sequence similarity; putative. | 0.443 |
| MJ_0168 | MJ_0169 | MJ_0168 | MJ_0169 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Cell division inhibitor minD; Similar to GP:1001783 percent identity: 30.86; identified by sequence similarity; putative; Belongs to the ParA family. MinD subfamily. | 0.490 |
| MJ_0168 | MJ_0831 | MJ_0168 | MJ_0831 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 35.87; identified by sequence similarity; putative; To M.jannaschii MJ0977. | 0.436 |
| MJ_0168 | MJ_1533 | MJ_0168 | MJ_1533 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Conserved hypothetical protein; Similar to GB:X04021 PID:44719 PID:44720 percent identity: 67.05; identified by sequence similarity; putative. | 0.484 |
| MJ_0168 | albA | MJ_0168 | MJ_0212 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Conserved hypothetical protein; Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes; Belongs to the histone-like Alba family. | 0.429 |
| MJ_0168 | dtdA | MJ_0168 | MJ_0166 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Conserved hypothetical protein; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. | 0.512 |
| MJ_0168 | moaB | MJ_0168 | MJ_0167 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | Molybdenum cofactor biosynthesis protein (moaB); Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor. | 0.512 |
| MJ_0168 | thrS | MJ_0168 | MJ_1197 | Archaeal histone A1; Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). | threonyl-tRNA synthetase (thrS); Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine, but does not detectably transfer it to tRNA(Thr). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain. Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl- tRNA(Thr). Deacylates correctly charged glycyl- tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor [...] | 0.562 |