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. 2010 Mar 1;78(5):2240–2247. doi: 10.1128/IAI.00100-10

FIG. 5.

FIG. 5.

Domain organization and sequence alignments of Sca2 WH2 and FH1-like domains. (A) Graphical illustration representing the domain organization of Sca2, a 1,821-amino-acid (aa) protein with a Sec-dependent secretion signal (SS) (aa 1 to 32), 4 putative WH2 domains (WH2-1, aa 454 to 479; WH2-2, aa 626 to 650; WH2-3, aa 702 to 730; and WH2-4, aa 1514 to 1538), an FH1 domain (aa 650 to 680), a proline-rich region (PRR) (aa 1057 to 1066), and an autotransporter domain (aa 1542 to 1821). The black arrowhead indicates the transposon insertion site in clone 9-7. (B) ClustalW amino acid sequence alignment of the four WH2 domains of Sca2 (R. rickettsii YP_001494228) and WH2-domain containing proteins from Homo sapiens, CAP1 (Q01518), CAP2 (P40123), WASP (P42768), N-WASP (O00401), WAVE1 (Q92558), WAVE2 (Q9Y6W5), and WAVE3 (Q9UPY6); from V. cholerae, VopF (AAZ32252); from V. parahaemolyticus, VopL (NP_800881); and from C. trachomatis, Tarp (YP_328278). (C) ClustalW amino acid sequence alignment of the Sca2 FH1-like domain and the portion of FH1 domain-containing proteins obtained through a BLASTp search. The accession numbers for proteins from humans are hDiap1, NP_001073280.1, and hFormin2, CAQ10135.1, and from mouse they are mDia1, AAH21396.1, and mFormin2, EDL13214.1. The consensus sequence was identified based upon a minimum of 75% amino acid identity at that position. Black shading indicates 100% similarity, and gray shading indicates >60% similarity.