| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A0A484C0I6 | A0A484C0L2 | A0A484C0I6 | A0A484C0L2 | DNA polymerase. | MCM_lid domain-containing protein. | 0.971 |
| A0A484C0I6 | A0A484C4G4 | A0A484C0I6 | A0A484C4G4 | DNA polymerase. | Mcm10 domain-containing protein. | 0.987 |
| A0A484C0I6 | A0A484C6L1 | A0A484C0I6 | A0A484C6L1 | DNA polymerase. | AAA_16 domain-containing protein. | 0.699 |
| A0A484C0I6 | A0A484C818 | A0A484C0I6 | A0A484C818 | DNA polymerase. | DNA helicase; Belongs to the MCM family. | 0.995 |
| A0A484C0I6 | A0A484CG04 | A0A484C0I6 | A0A484CG04 | DNA polymerase. | CDT1 domain-containing protein. | 0.599 |
| A0A484C0I6 | A0A484CG57 | A0A484C0I6 | A0A484CG57 | DNA polymerase. | DNA helicase; Belongs to the MCM family. | 0.993 |
| A0A484C0I6 | A0A484CQC0 | A0A484C0I6 | A0A484CQC0 | DNA polymerase. | DNA helicase; Belongs to the MCM family. | 0.996 |
| A0A484C0I6 | A0A484D123 | A0A484C0I6 | A0A484D123 | DNA polymerase. | Origin recognition complex subunit 1; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. | 0.929 |
| A0A484C0I6 | A0A484D4K4 | A0A484C0I6 | A0A484D4K4 | DNA polymerase. | DNA primase; Belongs to the eukaryotic-type primase small subunit family. | 0.999 |
| A0A484C0I6 | MCM7 | A0A484C0I6 | A0A484CWU9 | DNA polymerase. | DNA replication licensing factor MCM7; Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differential [...] | 0.992 |
| A0A484C0L2 | A0A484C0I6 | A0A484C0L2 | A0A484C0I6 | MCM_lid domain-containing protein. | DNA polymerase. | 0.971 |
| A0A484C0L2 | A0A484C4G4 | A0A484C0L2 | A0A484C4G4 | MCM_lid domain-containing protein. | Mcm10 domain-containing protein. | 0.966 |
| A0A484C0L2 | A0A484C6L1 | A0A484C0L2 | A0A484C6L1 | MCM_lid domain-containing protein. | AAA_16 domain-containing protein. | 0.968 |
| A0A484C0L2 | A0A484C818 | A0A484C0L2 | A0A484C818 | MCM_lid domain-containing protein. | DNA helicase; Belongs to the MCM family. | 0.988 |
| A0A484C0L2 | A0A484CG04 | A0A484C0L2 | A0A484CG04 | MCM_lid domain-containing protein. | CDT1 domain-containing protein. | 0.982 |
| A0A484C0L2 | A0A484CG57 | A0A484C0L2 | A0A484CG57 | MCM_lid domain-containing protein. | DNA helicase; Belongs to the MCM family. | 0.987 |
| A0A484C0L2 | A0A484CQC0 | A0A484C0L2 | A0A484CQC0 | MCM_lid domain-containing protein. | DNA helicase; Belongs to the MCM family. | 0.988 |
| A0A484C0L2 | A0A484D123 | A0A484C0L2 | A0A484D123 | MCM_lid domain-containing protein. | Origin recognition complex subunit 1; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. | 0.979 |
| A0A484C0L2 | A0A484D4K4 | A0A484C0L2 | A0A484D4K4 | MCM_lid domain-containing protein. | DNA primase; Belongs to the eukaryotic-type primase small subunit family. | 0.974 |
| A0A484C0L2 | MCM7 | A0A484C0L2 | A0A484CWU9 | MCM_lid domain-containing protein. | DNA replication licensing factor MCM7; Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differential [...] | 0.986 |
