{PDOC51844}
{PS51844; SH3_LIKE}
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* Myosin N-terminal SH3-like domain profile *
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Members of  the  myosin  superfamily of actin-based motors act in a variety of
cellular functions  such  as  muscle contraction, cell and organelle movement,
membrane trafficking,  and  signal transduction. Although myosin motor domains
(see <PDOC51456>)  show a high degree of sequence conservation, the individual
myosin classes  are  clearly defined by differences in the head structure. The
N-terminal region  of myosins from different classes  varies greatly in length
and amino  acid composition among the individual members. Many myosins have an
SH3-like domain  at the N-terminus of the motor domain. This  includes myosins
in classes II, V, VI, XI, XXII and XXIV. The myosin N-terminal SH3-like domain
may mediate some aspect of the conformational communication that occurs within
the myosin  head  during actin and nucleotide binding. Part of this effect may
be mediated  through  interactions  with  the  neck-associated essential light
chains that are in close proximity to this portion of the head domain and also
transiently interact with actin [1,2,3,4].

The myosin  N-terminal  SH3-like  domain comprises ~50 amino acids and forms a
protruding, six-stranded,  antiparallel,  beta-barrel  domain (see <PDB:1OE9>)
with similarities to the SH3 domain (see <PDOC50002>) [1,5].

The profile we developed covers the entire myosin N-terminal SH3-like domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2017 / First entry.

[ 1] Fujita-Becker S., Tsiavaliaris G., Ohkura R., Shimada T.,
     Manstein D.J., Sutoh K.
     "Functional characterization of the N-terminal region of myosin-2."
     J. Biol. Chem. 281:36102-36109(2006).
     PubMed=16982629; DOI=10.1074/jbc.M605171200
[ 2] Lowey S., Saraswat L.D., Liu H., Volkmann N., Hanein D.
     "Evidence for an interaction between the SH3 domain and the N-terminal
     extension of the essential light chain in class II myosins."
     J. Mol. Biol. 371:902-913(2007).
     PubMed=17597155; DOI=10.1016/j.jmb.2007.05.080
[ 3] Mooseker M.S., Foth B.J.
     "The structural and functional diversity of the myosin family of
     actin-based molecular motors."
     (In) Myosins, Proteins and Cell Regulation, Vol 7, pp1-34, Springer,
     Dordrecht (2008).
[ 4] Heintzelman M.B., Enriquez M.E.
     "Myosin diversity in the diatom Phaeodactylum tricornutum."
     Cytoskeleton 67:142-151(2010).
     PubMed=20217677; DOI=10.1002/cm.20431
[ 5] Menetrey J., Bahloul A., Wells A.L., Yengo C.M., Morris C.A.,
     Sweeney H.L., Houdusse A.
     "The structure of the myosin VI motor reveals the mechanism of
     directionality reversal."
     Nature 435:779-785(2005).
     PubMed=15944696; DOI=10.1038/nature03592

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