Member database | Pfam |
Pfam type | domain |
Short name | RACo_C_ter |
Clan | Actin_ATPase |
Author | Bateman A;0000-0002-6982-4660 El-Gebali S;0000-0003-1378-5495 |
Sequence Ontology | 0000417 |
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