Protein Family Models

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 [1,2]. 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 [3]. 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 [2,3]. This entry also includes bacterial proteins of unknown function. [1]. 7812447. Sequence and organization of the lactococcal prolate-headed bIL67 phage genome. Schouler C, Ehrlich SD, Chopin MC;. Microbiology 1994;140:3061-3069. [2]. 28100693. Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism. Xu RG, Jenkins HT, Chechik M, Blagova EV, Lopatina A, Klimuk E, Minakhin L, Severinov K, Greive SJ, Antson AA;. Nucleic Acids Res. 2017;45:3580-3590. [3]. 26150523. Structure and mechanism of the ATPase that powers viral genome packaging. Hilbert BJ, Hayes JA, Stone NP, Duffy CM, Sankaran B, Kelch BA;. Proc Natl Acad Sci U S A. 2015;112:E3792-E3799. (from Pfam)

Date:

2024-10-16