| Primary Identifier | IPR046461 | Type | Domain |
| Short Name | TerL_ATPase |
| description | Terminase large subunit (TerL) from bacteriophages and evolutionarily related viruses, is an important component of the DNA packing machinery and comprises an ATPase domain, which powers DNA translocation and a nuclease domain that cuts concatemeric DNA [, ]. TerL forms pentamers in which the ATPase domains form a ring distal to the capsid. This is the ATPase domain which contains a C-terminal subdomain that sits above the ATPase active site, called the "Lid subdomain"with reference to analogous lid subdomains found in other ATPases []. It contains a hydrophobic patch (Trp and Tyr residues) that mediates critical interactions in the interface between adjacent ATPase subunits and assists the positioning of the arginine finger residue that catalyses ATP hydrolysis [, ]. This domain is also found in uncharacterised proteins encoded by bacterial prophages, including YmfN from Escherichia coli. |
