2DL7


Conserved Protein Domain Family
SH3_FCHSD2_2
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cd11894: SH3_FCHSD2_2 
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Second Src Homology 3 domain of FCH and double SH3 domains protein 2
FCHSD2 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.
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Statistics
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PSSM-Id: 212827
Aligned: 3 rows
Threshold Bit Score: 113.11
Created: 21-Nov-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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peptide ligand
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
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
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1              # #  #   #                    ##            # ##   
2DL7_A         10 FVKALYDYEGQTDDELSFPEGAIIRILNKENQDDDGFWEGEFNGRIGVFPSVLVEE 65   human
CAG00919      548 YVRALYDYEGQADEELSFSEGAVIRLLSRDTQTDDGFWEGELNGRVGVFPSVLVED 603  spotted green pufferfish
NP_001096157  584 FVKALYEYDGQTDDELSFPEGAIIRILNKENQDDDGFWEGEFNGRIGVFPSVLVEE 639  western clawed frog

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