Protein Family Models

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 Pfam:PF14574 (residues 207-630). This entry pertains to the middle region. This region contains residues in their alpha-helices (H6 and H7) that mediate dimerization with subdomain I of the C-terminal domain. [1]. 22431597. 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. 2012;109:5235-5240. (from Pfam)

Date:

2024-08-14

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. [1]. 22431597. 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. 2012;109:5235-5240. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

ATP-binding protein is a DUF4445 domain-containing protein that may catalyze ATP hydrolysis or phosphoryl transfer, perhaps coupled to an energetically uphill electron transfer, similar to Carboxydothermus hydrogenoformans iron-sulfur cluster binding protein

Date:

2017-03-02