XB-IMG-170622
Xenbase Image ID: 170622
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Figure 2. Alignment of the XShal, XSha2, MBKl, and RCKl peptides.
XShal shares 89% identity with MBKl and RCKl (Tempel et
al., 1988; Stuhmer et al., 1989) but only 77% identity with XSha2, a
previously cloned XenopusS hakerg ene (Ribera, 1990). Identity with
XSha 1 is indicated by dashesg;a ps that were introduced to enhance the
alignment are indicated by dots. The one-letter amino acid code is used.
Unique features of the K 1.1 Shakegr enes include the carboxy-terminal
residues and the tyrosine at position 373. The region thought to specify
subunit assembly specificity (shadedba r) extends from amino acids 22
to 133 and 94% and 89% identical to the similar region in MBKl/RCKl
and XSha2, respectively. The putative transmembrane domains S&S6
are drawn into boxes. The putative pore (hatched bar, residues 354-
374) contains the tyrosine residue (373, asterisk)im plicated in determination
of TEA sensitivity. Consensus sites for CAMP-dependent protein
kinase C phosphorylation are found near the carboxy terminus in
the region indicated by a dashedli ne (residues 437-445). Alignment
was achieved using the MEGALIGN program (DNASTAR) followed by
adjustments done by eye. MBKl and RCKl sequences were downloaded
from the GenBank/EMBL database. Image published in: Ribera AB and Nguyen DA (1993) Copyright © 1993. This image is reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View |