C-terminal domain of mitochondrial association factor 1 (MAF1), Alba4, and related proteins
Mitochondria play a role in the regulation of the innate immune response. Host mitochondria are recruited to the membranes that surround certain intracellular bacteria and parasites during infection, a phenomenon termed host mitochondrial association (HMA). In Toxoplasma gondii, HMA is driven by a gene family that encodes mitochondrial association factor 1 (MAF1) proteins. MAF1 is the parasite protein needed to recruit host mitochondria to the Toxoplasma-containing vacuole during infection. The T. gondii MAF1 locus harbors multiple distinct paralogs that differ in their ability to mediate HMA; these fall into two broad groups designated MAF1a and MAF1b based on residue percent identity. MAF1b paralogs, but not MAF1a paralogs, have been shown to be responsible for the HMA phenotype. This family also includes Plasmodium yeolii ALBA4 which has been shown to modulate its stage-specific interactions and the fates of specific mRNAs during the parasite's growth and transmission, acting to regulate the development of the parasite's transmission stages.
Feature 1:ADP ribose binding site [chemical binding site]
Evidence:
Comment:based on Toxoplasma gondii MAF1a and MAF1b binding ADP ribose
Structure:6BXT: Toxoplasma gondii MAF1a binds ADP ribose; contacts at 4A - View structure with Cn3D
Structure:6BXW: Toxoplasma gondii MAF1b binds ADP ribose; contacts at 4A - View structure with Cn3D
Comment:MAF1a and MAF1b (representative members of the A and B paralog groups) both bind ADP ribose, it has been suggested that ADP ribose binding represents an ancestral function of MAF1 prior to its neofunctionalization
Jiyao W et al.(2023). "The conserved domain database in 2023.",