Conserved Protein Domain Family
SH3_FCHSD1_2
?
cd11895: SH3_FCHSD1_2 
Second Src Homology 3 domain of FCH and double SH3 domains protein 1
FCHSD1 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Links
?
Statistics
?
PSSM-Id: 212828
Aligned: 3 rows
Threshold Bit Score: 120.841
Created: 21-Nov-2011
Updated: 2-Oct-2020
Structure
?
Aligned Rows:
Download Cn3D
 
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
Scroll to Sequence Alignment Display
Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection: 
Feature 1          # #  #   #                     ##            # ##    
Q86WN1    550 LAQALYSYTGQSAEELSFPEGALIRLLPRAQDGVDDGFWRGEFGGRVGVFPSLLVEEL 607 human
NP_783615 548 LARALYSYTGQSEEELSFPEGALIRLLPRAQDGVDDGFWRGEFGGHVGVFPSLLVEEL 605 house mouse
XP_425188 631 LVRALYDYEGQSPEELSFPEGAIIRVLPRAEDEVDDGFWTGDFDGRVGVFPSLVVEEL 688 chicken

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap