1ZUU


Conserved Protein Domain Family
SH3_Bzz1_1

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cd11912: SH3_Bzz1_1 
Click on image for an interactive view with Cn3D
First Src Homology 3 domain of Bzz1 and similar domains
Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first C-terminal SH3 domain. 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.
Statistics
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PSSM-Id: 212845
Aligned: 26 rows
Threshold Bit Score: 76.4934
Created: 1-Dec-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
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

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              # #  #   #                                  ##               # ##   
1ZUU_A          3 ENKVLYAYVQKDdDEITITPGDKISLVARDt----------------gSGWTKINNDtt-gETGLVPTTYIRI 58   baker's yeast
CAD21370      564 KAKMLYTFEAGGeGELSVLEGRELVVLEPDt----------------gSGWTRVRAGy---KEGNVPTSYVEI 617  Neurospora crassa
XP_002838320  562 IGRMIYTYSGTGeGEISIEAGAEVVVVEPDd----------------gSGWVMVRSGn---AEGLVPATYIDV 615  Tuber melanosporum M...
XP_002910720  534 TVRAIFDFPASSeFELAIRENETLYMLEPDd----------------gSGWVKVSNAr--gESGLVPATYIED 588  Coprinopsis cinerea ...
XP_003034577  574 TARVVFDFTPSSeFELAVREGTLVSVVEPDd----------------gSGWVKVADGs--gKSGLVPASYIEA 628  Schizophyllum commun...
EGG12636      550 KAKMLYGHEASTpFEVSAAESTLVTVITPDd----------------gSGWIKVETEd--gRQGLVPATYVEI 604  Melampsora larici-po...
EGP91202      569 HGKMLYTYQANGeGEISITEGQSFILVEPDd----------------gSGWIKVRPTsfgaVPGLVPSSYAEL 625  Mycosphaerella grami...
EGX50524      577 KGKMLYSYTAGGdGEISVGEGKEVIIVQPDd-----------------GGWTKVRNGt---VTGLVPTTYVET 629  Arthrobotrys oligosp...
CCA66848      525 WATVVFDFVASSpFEISVDEGTRVKVLEEDd----------------gSGWIKIYKEst-eKSGLVPASYLKL 580  Piriformospora indica
XP_002175576  538 TVQVLYDYVGTTdDDLNVKEGQMVVILQPDgmldksllcvgltpyldgTGWVRARSGs---AEGLVPASYLDL 607  Schizosaccharomyces ...

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