Conserved Protein Domain Family
SH3_Sla1p_1

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cd11773: SH3_Sla1p_1 
First Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p
Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. 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: 212707
Aligned: 9 rows
Threshold Bit Score: 79.7758
Created: 17-May-2012
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
peptide ligand
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • 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              # #  #             #                  ##                           # ##
A6ZKU1          7 IYRAVYAYEPQtp----------eELAIQEDDLLYLLQKsdiDDWWTVKKRvigs--------dseePVGLVPSTY 64   Saccharomyces cer...
XP_571337       6 VAKALYDYQPQdp---------dtELAFHEDHILYIIDKe-dNDWWKAKLKddng--------gadgQVGLVPATY 63   Cryptococcus neof...
XP_002391000   12 VLKASYDYSPQsd----------dEITIKEDQILFLIERv-dEDWWKVKIKgntq--------eedtPVGLVPAAY 68   Moniliophthora pe...
Q4P3H6          6 LCKALYDYVAQae----------dELNLTEDDHLYILESd-dPEWWKAKLRrldehgtpiqddsddsTVGLVPANY 70   Ustilago maydis 521
A7E8B6          6 VYSAVYDYVPAge----------gELTIKEGDILYVLEKsteDDWWKAKKKasae--------dedePVGLIPNNY 63   Sclerotinia scler...
CCA66640       12 LYKALYAYESQgd----------dEVTMQEDQLVLLLDKs-dDDWSKVRLKqpsqq-------dlegPEGLVPAAY 69   Piriformospora in...
EGG12389        8 LVKAEYAYSPQte----------dELELEEDALYYLLEDd-dAEWHKVMLKtspss-------sdppKIGLVPATY 65   Melampsora larici...
Q6CHN0          8 VYQALYDYEARte----------dELTFSENSLLYLLEKsstDEWLKAKKAgpa----------gtnEIGLVPLTY 63   Yarrowia lipolyti...
O13736          9 IYKVLYSYEPQeinpgeeipenerEISIVEDEIVCLLEKg-eDDWYLVKRNvnsn--------dddeEIGIVPSNY 75   Schizosaccharomyc...

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