1CKA,3PVL,2DE0,2EYZ,2VGE,2H8H,1VYU,1RI9,2JXB,2RF0,1I1J,2KE9,1U3O,1UG1,1WXU,1X43,1X6B,1X6G,2CSQ,2CUD,2D8H,2ED0,2YUP,3A98,2E5K,3EHQ,1UHC,2DL5,1JEG,1J3T,1MUZ,1S1N,1UGV,1UJY,2D1X,2KGT,2YSQ,2DL8,2EBP,2ENM,1UHF,1WDX,2DIL,2DL7,2DLP,2DNU,1NM7,1UE9,1WFW,1WXT,1X2P,2CRE,2CT3,2CT4,2CUC,2DJQ,2DL3,2DL4,2DM1,2DMO,2EQI,2GQI,2YUN,2YUO,2JTE,2KXC,1K4U,1UFF,1UJ0,2K79,2VKN,2XMF,3I5R,1ABO,1GCP,1W70,2JS0,3KFV,1ARK,1H3H,2A08,2EW3,2FPD,2X3W,1Z9Z,2BTT,2FRY,2PQH,2RQW,3JV3,1KJW,1YN8,2FEI,2J6F,2RQT,1AZE,1M3A,2A28,2I0N,2DRK,1YNZ


Conserved Protein Domain Family
SH3
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cd00174: SH3 
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Src Homology 3 domain superfamily
Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins 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, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.
Links
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Statistics
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PSSM-Id: 212690
Aligned: 516 rows
Threshold Bit Score: 33.2051
Created: 1-Nov-2000
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:SH3 domains typically bind proline-rich ligands, preferentially to PxxP motifs.
  • Structure:1ABO; Mus musculus Abl tyrosine kinase SH3 domain binds 3bp-1 synthetic peptide; contacts at 4A.
  • Citation:PMID 7664083
  • Structure:1CKA; Mus musculus c-CRK SH3 domain binds C3p peptide; contacts at 4A.
  • Citation:PMID 7735837
  • Structure:2D1X: Human Cortactin SH3 domain binds Amap1-peptide; contacts at 4A.
  • 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           # #  #    #                    ##                     # ##
1CKA_A       3 YVRALFDFNGNde-eDLPFKKGDILRIRDKp---eEQWWNAEDSe--------gKRGMIPVPY 53   house mouse
2DE0_X     444 NQIAIYAHQPRta-dEIPMEPGDIIGVAGNh---wDGYSKGVNRkl-------gRTGLYPSYK 495  human
1RI9_A      42 TKVTTSITSKKwgtrDLQVKPGESLEVIQTt---dDTKVLCRNEe--------gKYGYVLRSY 93   human
1ABO_A       6 LFVALYDFVASgd-nTLSITKGEKLRVLGYnh--nGEWCEAQTKn---------GQGWVPSNY 56   house mouse
2BTT_A       4 KFEAAYDFPGSgsssELPLKKGDIVFISRDe---pSGWSLAKLLdg-------sKEGWVPTAY 56   baker's yeast
Q99469     348 IFRCVRTFIGCkeqgQITLKENQICVSSEEe---qDGFIRVLSGk---------KKGLIPLDV 398  human
584850      17 LYIAVNQYSKRme-dELNMKPGDKIKVITDdgeynDGWYYGRNLrt-------kEEGLYPAVF 71   baker's yeast
EFW43785  2091 AFRATHKFVPRhg-dELSMEVNDVVYILSEc---sDGWCIVRSRr---------GKGLVPRNR 2140 Capsaspora owczarzaki ATCC 30864
EGF82386   246 TYVTVFDYMPAkp-nELAVKLGDIINVHLTf---hDGWCLGENHqt-------gIAGMVPLYS 297  Batrachochytrium dendrobatidis JAM81
EGU12290   232 LHSAVQPHIPQra-dELRVKVGDRLIVIERf---dNGWFYGFNLtaeaerpeqqSLGCFPSSS 290  Rhodotorula glutinis ATCC 204091

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