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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: J Neurochem. 2011 Oct 4;119(4):772–784. doi: 10.1111/j.1471-4159.2011.07468.x

Table 1.

Alignments of mouse, human and fish class III myosins in those regions where mMyo3B contains a phosphorylated residue.

Regiona Sequencesb Sequencesb
Kinase domain graphic file with name nihms323088t1.jpg graphic file with name nihms323088t2.jpg
Loop2 region of the myosin domain graphic file with name nihms323088t3.jpg graphic file with name nihms323088t4.jpg
Tail domain graphic file with name nihms323088t5.jpg graphic file with name nihms323088t6.jpg
a

Regions are as described in Figure 1

b

Alignments of sequences from the database were performed in ClustalW. Amino acids highlighted in black are conserved in all six sequences, those in dark gray are conserved in five of the six sequences; those in light gray are conserved in at least four of the six sequences Amino acids in red were identified as autophosphorylation sites in this study; those in blue are predicted autophosphorylation sites. Superscript numbers indicate the position of the autophosphorylated residue in the sequence of mMyo3B or 3A. See Figure 1. Accession numbers: mMyo3A, AY101368; mMyo3B, NM_177376; hMYO3B (human), AF369908; hMYO3A, BC119811; fMyo3B (fish, bass), AF512506; fMyo3A, AF003249.