2RQW,2KYM


Conserved Protein Domain Family
SH3_Bem1p_2
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cd11879: SH3_Bem1p_2 
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Second Src Homology 3 domain of Bud emergence protein 1 and similar domains
Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. 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.
Links
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Statistics
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PSSM-Id: 212812
Aligned: 13 rows
Threshold Bit Score: 103.565
Created: 27-Oct-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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peptide ligand
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Structure:2KYM: Lodderomyces elongisporus Bem1p second SH3 domain binds Ste20p peptide; contacts at 4A.
  • Structure:2RQW: Saccharomyces cerevisiae Bem1p second SH3 domains binds Ste20p-Prr peptide; contacts at 4A.
  • Comment:SH3 domains bind proline-rich ligands, preferentially to PxxP motifs.
  • 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             #    # ##               #  ## #         # # # ##   
2RQW_A         4 YAIVLYDFKAEKADELTTYVGENLFICAHHNCEWFIAKPIGRlGGPGLVPVGFVSI 59  baker's yeast
2KYM_A         5 FAVTLYEFKAERDDELDVSPGENLSICAHYDYEWFIAKPINRlGGPGLVPVSYVRI 60  Lodderomyces elongisporus NRRL YB-4239
730721       127 FGIVQFDFAAERPDELEAKAGEAIIIIARSNHEWLVAKPIGRlGGPGLIPLSFIQL 182 fission yeast
XP_002397195 132 YAIVLHDFEAERADELDAKRGDAITVVAQSNREWFVAKPIGRlGRPGLIPVSFVEI 187 Moniliophthora perniciosa FA553
CCA74015     145 YAVVQHDFQAERPDELDAKAGDAISVVAHSNREWFVAKPIGRlGGPGLIPASFLEV 200 Piriformospora indica
NP_593744    127 FGIVQFDFAAERPDELEAKAGEAIIIIARSNHEWLVAKPIGRlGGPGLIPLSFIQL 182 Schizosaccharomyces pombe 972h-
EFW96686      96 YGRLLYDFKAERQDELDVSAGDSIIICAHHEYEWFIGKFFDKiGEPGLVPVSYVQL 151 Pichia angusta DL-1
XP_505956    181 HGVVLYDFQAERPDELQASKGDNIIIQAQSNHEWFVAKPVGRlGGPGLIPASFIEI 236 Yarrowia lipolytica CLIB122
XP_001730053 149 FATIKYDFKAELPHELSVKEGDGVFVVARSNEEWLVAKPLEYvGMPGLIPTNYITF 204 Malassezia globosa CBS 7966
EGG04919     176 FGTVKYDFTAERTDELDAKRGESLVIMAHSESQWFVVKPIGRlGGPGLIPLNFVEV 231 Melampsora larici-populina 98AG31
114914       159 YAIVLYDFKAEKADELTTYVGENLFICAHHNCEWFIAKPIGRlGGPGLVPVGFVSI 214 baker's yeast
EGR51343     149 YGVVMYDFNAERSDELEAKAGEAIIVIAQSNPEWFVAKPIGRlGGPGLIPVSFIEL 204 Trichoderma reesei QM6a
XP_001643219 166 SGIVLYDFKPERPDELEANAGDKITIYAHHNDEWFIASHTDSsGKPYLIPIDFVSI 221 Vanderwaltozyma polyspora DSM 70294

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