Conserved Protein Domain Family
SH3_MYO15A

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cd12067: SH3_MYO15A 
Src Homology 3 domain of Myosin XVa
Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Statistics
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PSSM-Id: 213000
Aligned: 4 rows
Threshold Bit Score: 159.972
Created: 1-May-2012
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
peptide ligand
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Comment:based on the binding of peptide ligands to the SH3 domains of other superfamily members
  • Comment:SH3 domains typically bind proline-rich ligands, preferentially to PxxP motifs.
  • Citation:PMID 7664083
  • Citation:PMID 7735837
  • Comment:flanking hinge and loops (RT and n-Src) confer sequence specificity for ligand residues outside the core binding motif

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              # #  #   #                                            ##            # ##   
EAW55666     2873 YVVAVRNFLPEDPALLAFHKGDIIHLQPLEPPRVGYSAGCVVRRKVVYLEELRRRGPDFGWRFGTIHGRVGRFPSELVQP 2952 human
XP_001924051 3531 YVVAVRNYITDDRTLLSFHKGDIIRLQKMEGLDAGQYYGCIVKKKVILLEELKRDTPDFGWKFGAIHGRSGVFPVEFVQP 3610 zebrafish
XP_414818    2444 YVVAVRNYSPEDGAQLSFHKGDIIHLQPLEHPKRDHYYGCVVRKKVMYLEELKTGTQDFGWKFGAIHGRSGLFPAEYVQP 2523 chicken
XP_002935902 2276 YVVAVQNYVTEDKTLLSFHKGDIIRLQPLDGLKKGQNYGCVVRKKVMYLEELKRGTQDFGWKFGAIHSRAGVFPAECVQP 2355 western clawe...

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