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We have solved the structure of a representative<jats:italic>E. tenella<\/jats:italic>SAG, EtSAG19, revealing that, despite a low level of sequence similarity, the entire<jats:italic>Eimeria<\/jats:italic>SAG family is unified by its three-layer \u03b1\u03b2\u03b1 fold which is related to that of the CAP superfamily. Furthermore, sequence comparisons show that the<jats:italic>Eimeria<\/jats:italic>SAG fold is conserved in surface antigens of the human coccidial parasite<jats:italic>Cyclospora cayetanensis<\/jats:italic>but this fold is unrelated to that of the SAGs\/SRS proteins expressed in other apicomplexans including<jats:italic>Plasmodium<\/jats:italic>species and the cyst-forming coccidia<jats:italic>Toxoplasma gondii<\/jats:italic>,<jats:italic>Neospora caninum<\/jats:italic>and<jats:italic>Besnoitia besnoiti<\/jats:italic>. However, despite having very different structures, Consurf analysis showed that<jats:italic>Eimeria<\/jats:italic>SAG and<jats:italic>Toxoplasma<\/jats:italic>SRS families each exhibit marked hotspots of sequence hypervariability that map to their surfaces distal to the membrane anchor. 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