PF14574

C-terminal domain of RACo the ASKHA domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameRACo_C_ter
ClanActin_ATPase
Author Bateman A;0000-0002-6982-4660 El-Gebali S;0000-0003-1378-5495
Sequence Ontology0000417

Description

This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain (residues 207-630). This entry is specific for the C-terminal domain which harbors the ATP-binding site. Structural studies show that the C-terminal domain contains the conserved beta-beta-beta-alpha-beta-alpha-beta-alpha topology characteristic of the ASKHA (acetate and sugar kinases/heat shock protein 70/actin). Despite the low-sequence identity shared between members of the ASKHA super family, they show a common central fold. Members of the ASKHA include proteins that catalyze phosphoryl transfers or hydrolysis of ATP in a variety of biological contexts. Asp, Asn, Glu, and Gln residues are well conserved in the core of the ASKHA proteins, where they interact with the phosphates of ATP and the bound Mg2+ ions.

References

1. Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein. Hennig SE, Jeoung JH, Goetzl S, Dobbek H. Proc. Natl. Acad. Sci. U.S.A. 109, 5235-40, (2012). View articlePMID: 22431597

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.