The domain within your query sequence starts at position 74 and ends at position 432; the E-value for the AFG1_ATPase domain shown below is 4.4e-110.
GPLDHYDFLIKSQELREDEHQRRVVQCLQKLQEDLKGYSIEEGGLFSKLFSRNKPPKGLY VYGDVGTGKTMVMDMFYAYVETKRKKRVHFHGFMLDVHRRIHHLKQSLPKRKAGFMAKSY DPIAPIAEEISQETSLLCFDEFQVTDIADAMILKQLFENLFKNGVVVVATSNRPPEDLYK NGLQRANFVPFIAVLKEYCDTLQLDSGVDYRKRELAPAGKLYYLTSEADVEAVVDKLFDE LAQKQNDLTSPRILKVQGRELRLNKACGSVADCTFEELCERPLGASDYLELSKNFDTVII RNIPQFSLAKRTQARRFITLIDNFYDFKVRIICSASAPISSLFLHQHQDSESDQSRILM
AFG1_ATPase |
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PFAM accession number: | PF03969 |
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Interpro abstract (IPR005654): | This P-loop motif-containing family of proteins includes AFG1, LACE1 and ZapE. ATPase family gene 1 (AFG1) is a 377 amino acid yeast protein with an ATPase motif typical of the family [ (PUBMED:1441755) ]. AFG1-like ATPase (also known as lactation elevated 1 or LACE1), the mammalian homologue of AGF1, is a mitochondrial integral membrane protein that is essential for maintenance of fused mitochondrial reticulum and lamellar cristae morphology. It has also been demonstrated that LACE1 mediates degradation of nuclear-encoded complex IV subunits COX4 (cytochrome c oxidase 4), COX5A and COX6A, and is required for normal activity of complexes III and IV of the respiratory chain [ (PUBMED:26759378) ]. ZapE is a cell division protein found in Gram-negative bacteria. The bacterial cell division process relies on the assembly, positioning, and constriction of FtsZ ring (the so-called Z-ring), a ring-like network that marks the future site of the septum of bacterial cell division. ZapE is a Z-ring associated protein required for cell division under low-oxygen conditions. It is an ATPase that appears at the constricting Z-ring late in cell division. It reduces the stability of FtsZ polymers in the presence of ATP in vitro [ (PUBMED:24595368) ]. |
GO function: | ATP binding (GO:0005524) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry AFG1_ATPase