| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0124 | MJ_0130 | MJ_0124 | MJ_0130 | Type I restriction-modification enzyme 2, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 32.31; identified by sequence similarity; putative; To M.jannaschii MJ1214. | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | 0.899 |
| MJ_0124 | MJ_0132 | MJ_0124 | MJ_0132 | Type I restriction-modification enzyme 2, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 32.31; identified by sequence similarity; putative; To M.jannaschii MJ1214. | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | 0.981 |
| MJ_0124 | MJ_1218 | MJ_0124 | MJ_1218 | Type I restriction-modification enzyme 2, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 32.31; identified by sequence similarity; putative; To M.jannaschii MJ1214. | Type I restriction-modification enzyme 1, S subunit; Identified by sequence similarity; putative. | 0.911 |
| MJ_0124 | MJ_1531 | MJ_0124 | MJ_1531 | Type I restriction-modification enzyme 2, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 32.31; identified by sequence similarity; putative; To M.jannaschii MJ1214. | Type I restriction-modification enzyme, S subunit, putative; Similar to GB:X17591 PID:40467 percent identity: 37.84; identified by sequence similarity; putative; To M.jannaschii MJ0130 and MJ1218. | 0.907 |
| MJ_0130 | MJ_0124 | MJ_0130 | MJ_0124 | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | Type I restriction-modification enzyme 2, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 32.31; identified by sequence similarity; putative; To M.jannaschii MJ1214. | 0.899 |
| MJ_0130 | MJ_0131 | MJ_0130 | MJ_0131 | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0131. | 0.749 |
| MJ_0130 | MJ_0132 | MJ_0130 | MJ_0132 | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | 0.990 |
| MJ_0130 | MJ_1214 | MJ_0130 | MJ_1214 | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | Type I restriction-modification enzyme 1, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 27.55; identified by sequence similarity; putative. | 0.901 |
| MJ_0130 | mjaIVMP | MJ_0130 | MJ_1328 | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | Modification methylase, type II R/M system; This methylase recognizes the double-stranded sequence GTNNAC, causes specific methylation on ? on both strands, and protects the DNA from cleavage by the MjaIV endonuclease. | 0.546 |
| MJ_0131 | MJ_0130 | MJ_0131 | MJ_0130 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0131. | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | 0.749 |
| MJ_0131 | MJ_0132 | MJ_0131 | MJ_0132 | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0131. | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | 0.702 |
| MJ_0132 | MJ_0124 | MJ_0132 | MJ_0124 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Type I restriction-modification enzyme 2, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 32.31; identified by sequence similarity; putative; To M.jannaschii MJ1214. | 0.981 |
| MJ_0132 | MJ_0130 | MJ_0132 | MJ_0130 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | 0.990 |
| MJ_0132 | MJ_0131 | MJ_0132 | MJ_0131 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0131. | 0.702 |
| MJ_0132 | MJ_1214 | MJ_0132 | MJ_1214 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Type I restriction-modification enzyme 1, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 27.55; identified by sequence similarity; putative. | 0.981 |
| MJ_0132 | MJ_1218 | MJ_0132 | MJ_1218 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Type I restriction-modification enzyme 1, S subunit; Identified by sequence similarity; putative. | 0.977 |
| MJ_0132 | MJ_1531 | MJ_0132 | MJ_1531 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Type I restriction-modification enzyme, S subunit, putative; Similar to GB:X17591 PID:40467 percent identity: 37.84; identified by sequence similarity; putative; To M.jannaschii MJ0130 and MJ1218. | 0.975 |
| MJ_0132 | mjaIVMP | MJ_0132 | MJ_1328 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Modification methylase, type II R/M system; This methylase recognizes the double-stranded sequence GTNNAC, causes specific methylation on ? on both strands, and protects the DNA from cleavage by the MjaIV endonuclease. | 0.561 |
| MJ_0132 | rqcH | MJ_0132 | MJ_1625 | Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family. | Conserved hypothetical protein; Probably part of the ribosome quality control system (RQC). May mediate the addition of alanine residues (Ala tailing) to incompletely synthesized nascent chains from stalled ribosomes, leading to their degradation; Belongs to the NEMF family. | 0.553 |
| MJ_1214 | MJ_0130 | MJ_1214 | MJ_0130 | Type I restriction-modification enzyme 1, R subunit; Similar to GB:L42023 PID:1007240 PID:1221415 PID:1205524 PID:1574743 percent identity: 27.55; identified by sequence similarity; putative. | Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...] | 0.901 |