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In silico analysis of the cyclophilin repertoire of apicomplexan parasites

Jürgen Krücken1 email, Gisela Greif2 email and Georg von Samson-Himmelstjerna1 email

Institute for Parasitology, University of Veterinary Medicine Foundation, Bünteweg 17, 30559 Hannover, Germany

Bayer Animal Health GmbH, Research & Development, Leverkusen, Germany

author email corresponding author email

Parasites & Vectors 2009, 2:27doi:10.1186/1756-3305-2-27

Published: 25 June 2009

Additional files

Additional file 1:

Table S1: Cyclophilins from H. sapiens and S. pombe. Listing of the human and fission yeast Cyp repertoire used for comparison with apicomplexan Cyps. Accession-no., protein size and domain architecture are summarized.

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Additional file 2:

Figure S1 – Plasmodium-specific Cyps. Domain architecture and genomic organization of Plasmodium-specific Cyps.

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Additional file 3:

Figure S2 – PPIL6-like Cyp TgCyp36.7. Domain architecture and genomic organization of TgCyp36.7.

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Additional file 4:

Tables S2 and S3: Protein sequences used to analyse evolution of Cyp and FKBP domains in dual class immunophilins. Listing of the genes used for comparison with apicomplaxan FKBPs in Figures 5 and 6.

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Additional file 5:

Figure S3 – FCBP and CFBP proteins in non-apicomplexa. Domain architecture of FCBPs and CFBPs from non-apicomplexan organisms.

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Additional file 6:

Figure S4 – PPIL1-like Cyps. Domain architecture and genomic organization of PPIL1-like Cyps.

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Additional file 7:

Figure S5 – PPIL4-like Cyps. Domain architecture and genomic organization of ChCyp34.5, the only apicomplexan PPIL4-like Cyp which contains an RNA recognition motif.

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