RNA-binding protein-related sequence in a malaria antigen, clustered-asparagine-rich protein

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Abstract

Members of the RNA-binding protein superfamily contain RNA binding domains of about 90 amino acids with a highly conserved motif 'GFGF'. Using the conserved motif with some variations G-(F/Y)-(G/A)-(F/Y)-(V/I)-X-(F/Y) as a probe, we screened protein sequences carrying identical amino acids in an NBRF-protein database. It has been found that the C-terminal portion of clustered asparagine-rich protein (CARP), a malaria antigen from Plasmodium falciparum, shows an unexpected sequence similarity with the RNA-binding protein superfamily for the C-terminal half of the RNA-binding domain. Dot matrix comparisons and alignment of these sequences as well as a statistical test have revealed highly significant sequence similarities. From these analyses, we conclude that the malaria antigen CARP belongs to a large family of the RNA-binding proteins. An evolutionary implication of the sequence similarity was also discussed. © 1990.

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APA

Kuma, K., Iwabe, N., Kawanishi, Y., & Miyata, T. (1990). RNA-binding protein-related sequence in a malaria antigen, clustered-asparagine-rich protein. FEBS Letters, 260(1), 67–69. https://doi.org/10.1016/0014-5793(90)80067-S

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