Conserved Protein Domain Family
PX_SNX_like

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cd06865: PX_SNX_like 
The phosphoinositide binding Phox Homology domain of SNX-like proteins
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. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.
Statistics
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PSSM-Id: 132775
View PSSM: cd06865
Aligned: 8 rows
Threshold Bit Score: 169.524
Threshold Setting Gi: 159486320
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                                                               ##   #                   
NP_200652    154 KITVSNPQKeqeisn----sivggnTYITYQITTRtnlpd----fggpsEFSVRRRF---RDVVTLADRLAETYRGFCIP 222 thale cress
EAZ33917     106 LIAVSDPTPeaepaats-lvpgsapTYISYLVTSArrg--------dhrRHAVRRRF---RDFVTLADRLAEAFRGHFVP 173 Japanese rice
XP_001765431 113 QVRVTDPEKvqepgss---lvpggtSYMTYKFTTHtnips-----ylgsDFTVRRRF---RDVVTLADTLAESYRGYFIP 181 Physcomitrella ...
CAL57623     187 KIWVSDPKIepdass-----tlvgkRVTHYKVTTRtnips-----yvhkEVVVWRRF---RDFVALDERLSAIHRGYFIP 253 Ostreococcus tauri
XP_001701189 329 TVTVHSPRKavapsr----ipglsdPYIVYKVTSRgaa---------vgEATVDRRF---RDVVALAETLAALFPGCFVP 392 Chlamydomonas r...
EAZ14006     156 QITVSEPKKhaepaagaagvipgsgSYFSYLITTRaa-----------dGGPVPREAalpRTLSPLRNALGRAYRGLFVP 224 Japanese rice
XP_002179568 418 KILVTDPLWlqsaar-----flggaPFWSYQIVAQllppgdvnpqvsagHWQVRRRF---RHVVALEDRLRQECPGAILP 489 Phaeodactylum t...
EED93831     396 KVVVSDPMLiqgtg------lfagpPHWTYLVTVYsknea-----ntqpVSAVRRRF---RHFVALEDRIHTSTPGAILP 461 Thalassiosira p...
Feature 1            ##                   #                              
NP_200652    223 PRPDKSVVesqv----mqkqEFVEQRRVALEKYLRRLSAHPVIRNSDELKVFLQVQ 274 thale cress
EAZ33917     174 PRPDKNTVesqv----mqrdEFVAQRRAALERYLWRLAEHPAIGPSDELRVFLQAE 225 Japanese rice
XP_001765431 182 PRPEKSVVesqv----mqkmEFIEQRRLALEKYLARLAAHPVLRHSEELRKFLQTE 233 Physcomitrella patens subsp. patens
CAL57623     254 PRPEKTVVsst-------geNFIQDRAVQLQHYLNRVASHSQLRLGDPLRIFLTHQ 302 Ostreococcus tauri
XP_001701189 393 PRPSRSAIegrr-----mlpAFIEERRVGIEKFLRRLVIHPVMGPAEATQVWLRSQ 443 Chlamydomonas reinhardtii
EAZ14006     225 ARPDKSIVegqv----mqrhEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 276 Japanese rice
XP_002179568 490 PRPDKHAAraieeastqqsaEFALLRTAELQVYLNQLITHPIVARSHTLRLFLSLQ 545 Phaeodactylum tricornutum CCAP 1055/1
EED93831     462 ARPDKHPAraieeatarqsaDFAMQRAQELSFYMNALVHHPYAGLSPELKLFLTLQ 517 Thalassiosira pseudonana CCMP1335

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