Protein Family Models

Date:

2024-08-14

This domain represents the N-terminal DNA-binding domain found in the PriA protein. The 3'BD, which has been shown to bind the 3' end of the leading-strand arm of replication fork structures. [1]. 24379377. Structural mechanisms of PriA-mediated DNA replication restart.. Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel. SR, Sandler SJ, Ha T, Keck JL;. Proc Natl Acad Sci U S A. 2014;111:1373-1378.. [2]. 17464287. Structural basis of the 3'-end recognition of a leading strand. in stalled replication forks by PriA.. Sasaki K, Ose T, Okamoto N, Maenaka K, Tanaka T, Masai H, Saito. M, Shirai T, Kohda D;. EMBO J. 2007;26:2584-2593. (from Pfam)

Date:

2024-08-14

This is the C-terminal domain found in PriA DNA helicase, a multifunctional enzyme that mediates the process of restarting prematurely terminated DNA replication reactions in bacteria. The C-terminal domain (CTD) bears similarity to the S10 subunit which binds branched rRNA within the bacterial ribosome. The C-terminal domain is part of the helicase domain of PriA proteins. It acts together with the 3' DNA-binding domain to form a site for binding ssDNA-binding protein (SSB) [1]. [1]. 24379377. Structural mechanisms of PriA-mediated DNA replication restart.. Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel. SR, Sandler SJ, Ha T, Keck JL;. Proc Natl Acad Sci U S A. 2014;111:1373-1378. (from Pfam)

Date:

2024-08-14

This is a cys-rich region (CRR) domain found in PriA DNA helicases. In bacteria, the replication restart process is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). The CRR region which is embedded within the C-terminal helicase lobe has been identified to bind two Zn2+ ions. This 50-residue insertion forms a structure on the surface of the helicase core in which two Zn2+ ions are coordinated by invariant Cys residues. Biochemical experiments have shown that sequence changes to Zn2+-binding Cys residues in the PriA CRR can eliminate helicase, but not ATPase, activity and can block assembly of PriB onto DNA-bound PriA, implicating the CRR in multiple functions in PriA [1]. [1]. 24379377. Structural mechanisms of PriA-mediated DNA replication restart.. Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel. SR, Sandler SJ, Ha T, Keck JL;. Proc Natl Acad Sci U S A. 2014;111:1373-1378. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression. [1]. 10322435. Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and. related families.. de la Cruz J, Kressler D, Linder P;. Trends Biochem Sci 1999;24:192-198.. [2]. 9862990. The DEAD box RNA helicase family in Arabidopsis thaliana.. Aubourg S, Kreis M, Lecharny A;. Nucleic Acids Res 1999;27:628-636. (from Pfam)

Date:

2024-08-14

The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase. (from Pfam)

Date:

2024-08-14