Protein Family Models

The helicase associated domain (HA2) has an all alpha-helical fold and consists of a N-terminal winged-helix (WH) domain (Pfam:PF04408) and a C-terminal degenerate helical-bundle domain, referred to as the ratchet-like domain [1,2,3]. These domains collaborate with the RecA domains at the N-terminal in completing an RNA binding channel to allow the helicases to keep a stable grip on the RNA [3]. This entry represents the ratchet-like domain, which may be important for RNA translocation [1,2]. [1]. 26545078. Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. Prabu JR, Muller M, Thomae AW, Schussler S, Bonneau F, Becker PB, Conti E;. Mol Cell. 2015;60:487-499. [2]. 31409651. Structural and functional characterisation of human RNA helicase DHX8 provides insights into the mechanism of RNA-stimulated ADP release. Felisberto-Rodrigues C, Thomas JC, McAndrew C, Le Bihan YV, Burke R, Workman P, van Montfort RLM;. Biochem J. 2019;476:2521-2543. [3]. 32179686. Structural basis for DEAH-helicase activation by G-patch proteins. Studer MK, Ivanovic L, Weber ME, Marti S, Jonas S;. Proc Natl Acad Sci U S A. 2020;117:7159-7170. (from Pfam)

Date:

2024-10-16

This presumed domain is functionally uncharacterised. This domain is found in bacteria. This domain is typically between 582 to 594 amino acids in length. This domain is found associated with Pfam:PF07717, Pfam:PF00271, Pfam:PF04408. (from Pfam)

Date:

2024-08-14

This family is found towards the C-terminus of the DEAD-box helicases (Pfam:PF00270). In these helicases it is apparently always found in association with Pfam:PF04408. There do seem to be a couple of instances where it occurs by itself - e.g. Swiss:Q84VZ2. The structure PDB:3i4u adopts an OB-fold. helicases (Pfam:PF00270). In these helicases it is apparently always found in association with Pfam:PF04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins [1]. [1]. 20512115. Prp43p contains a processive helicase structural architecture with a specific regulatory domain. Walbott H, Mouffok S, Capeyrou R, Lebaron S, Humbert O, van Tilbeurgh H, Henry Y, Leulliot N;. EMBO J. 2010;29:2194-2204. [2]. 20696886. Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells. Kim T, Pazhoor S, Bao M, Zhang Z, Hanabuchi S, Facchinetti V, Bover L, Plumas J, Chaperot L, Qin J, Liu YJ;. Proc Natl Acad Sci U S A. 2010; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

The helicase associated domain (HA2) has an all alpha-helical fold and consists of a N-terminal winged-helix (WH) domain and a C-terminal degenerate helical-bundle domain, referred to as the ratchet-like domain [1,2,3]. These domains collaborate with RecA domains at the N-terminal in completing an RNA binding channel to allow the helicases to keep a stable grip on the RNA [3] and assure its correct function. This entry represents the WH domain, which connects the N- (RecA domains) and C-terminal domains (ratchet-like and OB-fold) of helicases. [1]. 26545078. Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. Prabu JR, Muller M, Thomae AW, Schussler S, Bonneau F, Becker PB, Conti E;. Mol Cell. 2015;60:487-499. [2]. 31409651. Structural and functional characterisation of human RNA helicase DHX8 provides insights into the mechanism of RNA-stimulated ADP release. Felisberto-Rodrigues C, Thomas JC, McAndrew C, Le Bihan YV, Burke R, Workman P, van Montfort RLM;. Biochem J. 2019;476:2521-2543. [3]. 32179686. Structural basis for DEAH-helicase activation by G-patch proteins. Studer MK, Ivanovic L, Weber ME, Marti S, Jonas S;. Proc Natl Acad Sci U S A. 2020;117:7159-7170. (from Pfam)

Date:

2024-10-16

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:

2024-10-16

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

This HMM represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB.

Gene:

hrpA

Date:

2024-05-14