Conserved Protein Domain Family
PX_Vps5p

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cd06861: PX_Vps5p 
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p
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. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1.
Statistics
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PSSM-Id: 132771
View PSSM: cd06861
Aligned: 10 rows
Threshold Bit Score: 190.641
Threshold Setting Gi: 169849281
Created: 10-Jul-2008
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
phosphoinosit..
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Comment:A majority of PX domain containing proteins binds phosphatidylinositol-3-phosphate (PI3P) at this site. In some cases, other phosphoinositides, such as PI4P or PI(3,4)P2, are the preferred substrates.
  • Comment:based on the structures of phosphatidylinositol-3-phosphate bound to other members of this superfamily
  • 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:
Feature 1                                                       ###                       ##      
Q92331        281 FKVEVKDPVKVGELTSIHVEYTVISESsll-------elkYAQVSRRYRDFRWLYRQLQNNHWGKVIPPPPEKQS-VGSF 352  baker's yeast
XP_570117     519 FQISVSDPTRVGDAVRGYTVYTIRTRTssph-----yqqsTFSCLRRFSDFLWLFEQLSHNNPGVIVPPMPDKHS-WGRF 592  Cryptococcus ...
XP_001831344  290 FVITVDDPQKVGDPLRPYIMYTVHTRTtspl-----fhksAFSVLRRYSDFVWLYEALCYNNPGVVVPPVPEKSS-FGRF 363  Coprinopsis c...
NP_587929     202 FYIQVHDPHTVKEITKSHTVYSVSTRLeehnq----psvsNVTVQRRYNDFAFLYQLLSNNHPGCIIPPIPEKQV-VGRF 276  fission yeast
XP_500143     252 FEISVGDPIKVGDITSSHTVYTVSTKTnhpn-----fktdAGSVTRRYSDFRWLFHALENKHPGIVVPPPPDKQA-VGRF 325  Yarrowia lipo...
XP_761434     681 FSIKVGDPQRIGDPISAHTVYTVRTTTdcph-----frssHFSSLRRYRDFRWLHAALVQNNPGIIVPPVPEKVS-IGRF 754  Ustilago mayd...
XP_715580     272 LEITVGDPTKVGDLTTAHVVYTIKTVNknldsk-ffpaveSVQVSRRYRDFRWIYHQLQNNHPGRIIPPPPSKQTfIGRF 350  Candida albic...
XP_001647400  275 FIINVTDPIKVGDMTSAHVEYLITSKSpll-------epnSSSVYRRYSDVRWLYRQLQSNHWGRVVPPPPEKQI-IGRF 346  Vanderwaltozy...
EDP50637      125 FEITVGDPHKVGDLTSSHIVYQVRTKTtska-----yrqpEFTVSRRYRDFLWLYNSMHNNNPGVVVPPPPEKQA-VGRF 198  Aspergillus f...
XP_002175392  150 YEITIHDPHKVGELTSAHTVYCVTSTVtypnaqspteskeELQVERRYRDFLLLYQLLGATHPGTIIPPAPEKQV-VGRF 228  Schizosacchar...
Feature 1                #                              
Q92331        353 KENFIENRRFQMESMLKKICQDPVLQKDKDFLLFLTSD 390  baker's yeast
XP_570117     593 EDQFVETRRLALEKCLKKITSNPILQLDPDLRLFLESD 630  Cryptococcus neoformans var. neoformans JEC21
XP_001831344  364 EDQFVRQRRLGLEKCIQKMANHPVLAKDPDLRLFLESD 401  Coprinopsis cinerea okayama7#130
NP_587929     277 DDEFIEQRRAALEVMLRKISAHPVLRDDYSFKLFLEAE 314  fission yeast
XP_500143     326 NEDFVEARRAALETMLQKVARHHLLQDDPDLQLFLQSE 363  Yarrowia lipolytica CLIB122
XP_761434     755 AAELVEARRVGLETCINKIANHPLLQQDDDFRLFLESE 792  Ustilago maydis 521
XP_715580     351 NENFIENRRLSLEKMLSKINHHPLLCNDPDFVMFLTSQ 388  Candida albicans SC5314
XP_001647400  347 QVNFIEYRRSQFELMLRDIANDPVLQKDDAFISFLTSV 384  Vanderwaltozyma polyspora DSM 70294
EDP50637      199 DTNFVESRRAALERMLNKIAAHPILQHDADLKIFLESE 236  Aspergillus fumigatus A1163
XP_002175392  229 DDEFVELRRASLEKMIRKIAQHPRLCQDDAFRYFLSAS 266  Schizosaccharomyces japonicus yFS275

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