RNA-binding protein-related sequence in a malaria antigen, clustered-asparagine-rich protein.
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.
Kuma
K
K
Department of Biology, Faculty of Science, Kyushu University, Fukuoka, Japan.
Iwabe
N
N
Kawanishi
Y
Y
Miyata
T
T
D000595:Amino Acid Sequence; D000818:Animals; D000953:Antigens, Protozoan / Q000302:isolation & purification*; D001216:Asparagine / Q000032:analysis*; D002352:Carrier Proteins / Q000302:isolation & purification*; D008288:Malaria / Q000235:genetics / Q000469:parasitology*; D015336:Molecular Probe Techniques; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000235:genetics / Q000276:immunology*; D016601:RNA-Binding Proteins; D012689:Sequence Homology, Nucleic Acid
D000953:Antigens, Protozoan; D002352:Carrier Proteins; D016601:RNA-Binding Proteins; D001216:Asparagine