1OCU,1OCS


Conserved Protein Domain Family
PX_Grd19

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cd07295: PX_Grd19 
Click on image for an interactive view with Cn3D
The phosphoinositide binding Phox Homology domain of fungal Grd19
The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer.
Statistics
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PSSM-Id: 132828
View PSSM: cd07295
Aligned: 5 rows
Threshold Bit Score: 194.639
Threshold Setting Gi: 40889192
Created: 2-Mar-2009
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Structure:1OCU_A; Saccharomyces cerevisiae SNX3 (Grd19p) PX domain binds Phosphatidylinositol-3-Phosphate; defined at 3.5A contacts.
    View structure with Cn3D
  • Comment:Two basic residues are key in binding with phosphoinositides: one forms hydrogen bonds with the 3-phosphate of PI(3)P and another forms hydrogen bonds with the 4-and 5-hydroxyl groups of PI(3)P.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                      # #  #                         ## 
1OCU_A        35 FLEIEVHNPKTHIpngmdskgMFTDYEIICRTNLPSFHKRVSKVRRRYSDFEFFRKXLIKeismlnhpKVMVPHLPGKIl 114
1OCS_A        35 FLEIEVHNPKTHIpngmdskgMFTDYEIICRTNLPSFHKRVSKVRRRYSDFEFFRKXLIKeismlnhpKVMVPHLPGKIl 114
gi 85118936   22 FLEIEVRNPRTHGig----rhMYTDYEIVCRTNIPAFKLRQSTVRRRYSDFEYFRDILERes-----aRVTIPPLPGKVf 92
gi 19113272   24 ILEIDVINPQTHGig----rnMFTTYEIVCRTNMPYFRLHNSSVRRRYSEFEKFHDMLERes-----gRVSIPPLPGKIf 94
gi 119388971   8 FLEVEVRSPLTHGvg----rkMYTDYEIVTRTNIPAFKLRYSSVRRRYSDFEYFRDILERes-----tRVNIPPLPGKVf 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
Feature 1           #        #                                 
1OCU_A       115 lsnRFSNEVIEERRQGLNTWMQSVAGHPLLQsGSKVLVRFIEAEKF 160
1OCS_A       115 lsnRFSNEVIEERRQGLNTWMQSVAGHPLLQsGSKVLVRFIEAEKF 160
gi 85118936   93 t-nRFSDDVIEGRRAGLEKFLKIVVGHPLLQtGSKVLAAFVQDPNW 137
gi 19113272   95 t-qRFRDDVIEERRQGLENFLRLVAGHPLIQtHSRVLSSFLQSPEF 139
gi 119388971  79 t-nRFTDEVIEARREGLERFLQVVAGHPLLQtGSKVMAAFLQDSGW 123

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