1NM7,1N5Z


Conserved Protein Domain Family
SH3_Pex13p_fungal

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cd11771: SH3_Pex13p_fungal 
Click on image for an interactive view with Cn3D
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p
Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. 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: 212705
Aligned: 15 rows
Threshold Bit Score: 97.732
Created: 31-May-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide ligandputative Pex5p
Conserved site includes 12 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.
  • Comment:this site serves as the Pex14p binding site
  • Structure:1N5Z; Saccharomyces cerevisiae Pex13p SH3 domain binds Pex14p peptide; contacts at 4A.
  • 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             #    ##            ##                            #  ##           # # ##   
1NM7_A         9 FARALYDFVPENp----------eMEVALKKGDLMAILSKKdp---------lgRDSDWWKVRTKNGNIGYIPYNYIEI 68  baker's yeast
1N5Z_A        16 FARALYDFVPENp----------eMEVALKKGDLMAILSKKdp---------lgRDSDWWKVRTKNGNIGYIPYNYIEI 75  baker's yeast
O14136       226 FCKADYEFMSRDp----------gVEMSLKKGDIIAILSKTdt---------qgNPCEWWQGRKRSGETGWFPSNYCSI 285 Schizosaccharomy...
XP_501488    330 FCRANFDFVPENp----------qLELELRKGDLVAVLAKTdp---------mgNPSQWWRVRTRDGRSGYVPANYLEV 389 Yarrowia lipolyt...
XP_001839695 341 FARAKYPFTPSNp-----------NELALKEDEIVAIMGKLdprtgmevdprleVDGEWWKGRTREGREGWFPRKWVEI 408 Coprinopsis cine...
XP_003192858 293 FVRAKWEFMPSEd-----------WELGLGRDEIIAVLEKRg-----------eGQNSWWRGRTRDGRTGWFPANYVEL 349 Cryptococcus bac...
EFP74062     345 FVKAIHPYHPTTreedinqlnpieKELKFEKNEVIAVLLPMsie--------erRSMGWWKGRTRDGRIGWFPKNYVEE 415 Puccinia gramini...
CBQ73554     341 FVRALYAYPAADp-----------LELSLQPNDIVAVLSKHdpq--------tgAESAWWRGRTRDGRIGWFPSTYVES 400 Sporisorium reil...
EGV61996     225 FAKALYEFNPENp----------nIEIELKPNDLVAVLSRLdp---------lgNESKWWKVRSRSGKVGYVPSNYLTV 284 Candida tenuis A...
CAE76446     327 FCRVLYDFSPATqgnge---ivpgVDLEVHKGDLVAVLSKSdp---------lgQPSEWWKCRARDGRIGYLPATFLEV 393 Neurospora crassa

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