The domain within your query sequence starts at position 21 and ends at position 87; the E-value for the ACT domain shown below is 4.3e-8.
VTLIFSLENEVGGLIKVLKIFQENHVSLLHIESRKSKQRNSEFEIFVDCDISREQLNDIF PLLKSHA
ACT |
---|
PFAM accession number: | PF01842 |
---|---|
Interpro abstract (IPR002912): | The ACT domain is found in a variety of contexts and is proposed to be a conserved regulatory binding fold. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure [ (PUBMED:11751050) ]. Most of the proteins in which it is found are involved in amino acid and purine metabolism:
|
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ACT