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Conserved domains on  [gi|33859789|ref|NP_766056|]
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sorting nexin-30 [Mus musculus]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10160658)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_SNX30 cd07667
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid ...
190-429 0e+00

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX30 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153351  Cd Length: 240  Bit Score: 504.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 190 HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSRVGESVKHVTGGYKLRSRPLEFAAISDYLDTFALKLGTIDRIAQRIIKE 269
Cdd:cd07667   1 HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSKMGESVKYVTGGYKLRSRPLEFAAIGDYLDTFALKLGTIDRIAQRIIKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 270 EIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIGNCSTALEELTDDITEEFLPVLREYVLYSDSMKGVLKKRDQVQA 349
Cdd:cd07667  81 EIEYLVELREYGPVYSTWSGLEGELAEPLEGVSACIGNCSTALEELTEDMTEDFLPVLREYILYSESMKNVLKKRDQVQA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 350 EYEAKLEAVALRKEERPKVPADVEKCQDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIPL 429
Cdd:cd07667 161 EYEAKLEAVALRKEERPKVPTDVEKCQDRVECFNADLKADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLTAWESIIPL 240
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
91-206 8.56e-77

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; 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 consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


:

Pssm-ID: 132770  Cd Length: 116  Bit Score: 234.54  E-value: 8.56e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd06860   1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAK 206
Cdd:cd06860  81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116
 
Name Accession Description Interval E-value
BAR_SNX30 cd07667
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid ...
190-429 0e+00

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX30 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153351  Cd Length: 240  Bit Score: 504.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 190 HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSRVGESVKHVTGGYKLRSRPLEFAAISDYLDTFALKLGTIDRIAQRIIKE 269
Cdd:cd07667   1 HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSKMGESVKYVTGGYKLRSRPLEFAAIGDYLDTFALKLGTIDRIAQRIIKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 270 EIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIGNCSTALEELTDDITEEFLPVLREYVLYSDSMKGVLKKRDQVQA 349
Cdd:cd07667  81 EIEYLVELREYGPVYSTWSGLEGELAEPLEGVSACIGNCSTALEELTEDMTEDFLPVLREYILYSESMKNVLKKRDQVQA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 350 EYEAKLEAVALRKEERPKVPADVEKCQDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIPL 429
Cdd:cd07667 161 EYEAKLEAVALRKEERPKVPTDVEKCQDRVECFNADLKADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLTAWESIIPL 240
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
91-206 8.56e-77

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; 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 consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 234.54  E-value: 8.56e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd06860   1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAK 206
Cdd:cd06860  81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
119-204 4.51e-23

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 92.30  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789   119 RVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFvvkgVVDRFSEEFVETRRKALDKFLKRITDHPVLSFNEH 198
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKR----WLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEV 76

                  ....*.
gi 33859789   199 FNVFLT 204
Cdd:pfam00787  77 LLEFLE 82
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
93-425 1.62e-21

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 96.79  E-value: 1.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTME---TYITYRITTKSTRVEFDL---PEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEK-FVVKGVV 165
Cdd:COG5391 133 STVSNPQSLTLLVDsrdKHTSYEIITVTNLPSFQLresRPLVVRRRYSDFESLHSILIKLLPLCAIPPLPSKkSNSEYYG 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 166 DRFSEEFVETRRKALDKFLKRITDHPVLS-------FNEHFNVFLTAKDLNAYKKQGIAL-LSRVGESVKHvtGGYKLRS 237
Cdd:COG5391 213 DRFSDEFIEERRQSLQNFLRRVSTHPLLSnyknsksWESHSTLLSSFIENRKSVPTPLSLdLTSTTQELDM--ERKELNE 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 238 RplefaaisdyLDTFALKLGTIDRIAQRIIKE------------EIEYLVELREygpvystwSALEGELAEPLE-----G 300
Cdd:COG5391 291 S----------TSKAIHNILSIFSLFEKILIQleseeesltrllESLNNLLLLV--------LNFSGVFAKRLEqnqnsI 352
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 301 VSACIGNCSTALEELTDDITeEFLPVLREYVLYSDSMKGVLKKRDQVQAEYEAKLEAVALRKEERPKV------------ 368
Cdd:COG5391 353 LNEGVVQAETLRSSLKELLT-QLQDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVsqqpegltsfsk 431
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 369 ------PADVEKCQDR----------------------MECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCL 420
Cdd:COG5391 432 lsyklrDFVQEKSRSKsieslqqdkekleeqlaiaekdAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENL 511

                ....*
gi 33859789 421 MAWES 425
Cdd:COG5391 512 EIWKS 516
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
97-204 5.71e-21

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 87.40  E-value: 5.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789     97 DPKKHVCTMETYITYRITTKStrvefDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKfVVKGVVDRFSEEFVETR 176
Cdd:smart00312   3 EPEKIGDGKHYYYVIEIETKT-----GLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGK-KLFGRLNNFSEEFIEKR 76
                           90       100
                   ....*....|....*....|....*....
gi 33859789    177 RKALDKFLKRITDHPVLS-FNEHFNVFLT 204
Cdd:smart00312  77 RRGLEKYLQSLLNHPELInHSEVVLEFLE 105
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
265-420 3.82e-04

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 41.94  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789   265 RIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIG-----------------NCSTALEELTDDITEEFLPVL 327
Cdd:pfam03114  44 KLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIEAGKDLGedssfgkaledygealkRLAQLLEQLDDRVETNFLDPL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789   328 REYVLYSDSMKGVLKKRDQVQAEYEAKLEAV-ALRKEERPKVPA------DVEKCQDRMECFNADLKADMERWQSNKRHD 400
Cdd:pfam03114 124 RNLLKEFKEIQKHRKKLERKRLDYDAAKTRVkKAKKKKSSKAKDesqaeeELRKAQAKFEESNEQLKALLPNLLSLEVEF 203
                         170       180
                  ....*....|....*....|
gi 33859789   401 FRQLLVGLADKNIQYYEKCL 420
Cdd:pfam03114 204 VVNQLVAFVEAQLDFHRQCY 223
BAR smart00721
BAR domain;
212-420 9.08e-03

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 37.75  E-value: 9.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789    212 KKQgialLSRVGESVKHVTGGyklrsrpLEFAAISDYLDTFALKLGTIDRIAQRIIKEEIEYL-------VELREY---- 280
Cdd:smart00721   3 KKQ----FNRAKQKVGEKVGK-------AEKTKLDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnpavrAKLASQkkls 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789    281 ---GPVYSTWSALEGelAEPLEGVSACIGNCSTALEELTDdITEEFLPVLREYVL-----YSDSMKGV---LKKRDQVQA 349
Cdd:smart00721  72 kslGEVYEGGDDGEG--LGADSSYGKALDKLGEALKKLLQ-VEESLSQVKRTFILpllnfLLGEFKEIkkaRKKLERKLL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789    350 EYEAKLEAV--ALRKEERPKVP------ADVEKCQDRMECFNADLKADMERWqSNKRHDFR-QLLVGLADKNIQYYEKCL 420
Cdd:smart00721 149 DYDSARHKLkkAKKSKEKKKDEklakaeEELRKAKQEFEESNAQLVEELPQL-VASRVDFFvNCLQALIEAQLNFHRESY 227
 
Name Accession Description Interval E-value
BAR_SNX30 cd07667
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid ...
190-429 0e+00

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX30 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153351  Cd Length: 240  Bit Score: 504.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 190 HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSRVGESVKHVTGGYKLRSRPLEFAAISDYLDTFALKLGTIDRIAQRIIKE 269
Cdd:cd07667   1 HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSKMGESVKYVTGGYKLRSRPLEFAAIGDYLDTFALKLGTIDRIAQRIIKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 270 EIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIGNCSTALEELTDDITEEFLPVLREYVLYSDSMKGVLKKRDQVQA 349
Cdd:cd07667  81 EIEYLVELREYGPVYSTWSGLEGELAEPLEGVSACIGNCSTALEELTEDMTEDFLPVLREYILYSESMKNVLKKRDQVQA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 350 EYEAKLEAVALRKEERPKVPADVEKCQDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIPL 429
Cdd:cd07667 161 EYEAKLEAVALRKEERPKVPTDVEKCQDRVECFNADLKADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLTAWESIIPL 240
BAR_SNX7_30 cd07624
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ...
227-429 9.32e-108

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX7, SNX30, and similar proteins. The specific functions of SNX7 and SNX30 have not been elucidated. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153308  Cd Length: 200  Bit Score: 316.63  E-value: 9.32e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 227 KHVTGGYKLRSRPLEFAAISDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIG 306
Cdd:cd07624   1 RNTSTMYLLKNRSPEFDKMNEYLTLFGEKLGTIERISQRIHKERIEYFDELKEYSPIFQLWSASETELAPLLEGVSSAVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 307 NCSTALEELTDDITEEFLPVLREYVLYSDSMKGVLKKRDQVQAEYEAKLEAVALRKEErpkVPADVEKCQDRMECFNADL 386
Cdd:cd07624  81 RCTAALEVLLSDHEFVFLPPLREYLLYSDAVKDVLKRRDQFQIEYELSVEELNKKRLE---LLKEVEKLQDKLECANADL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 33859789 387 KADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIPL 429
Cdd:cd07624 158 KADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEEVLPA 200
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
190-427 1.83e-87

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153350  Cd Length: 243  Bit Score: 266.38  E-value: 1.83e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 190 HPVLSFNEHFNVFLTAK--DLNAYKKQGIALLSRVGESVKHVTGGYK-LRSRPLEFAAISDYLDTFALKLGTIDRIAQRI 266
Cdd:cd07666   1 HPTLTFNEDFKIFLTAQawELSSHKKQGPGLLSRMGQTVKAVASSVRgVKNRPEEFTEMNEYVEAFSQKINVLDKISQRI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 267 IKEEIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIGNCSTALEELTDDITEEFLPVLREYVLYSDSMKGVLKKRDQ 346
Cdd:cd07666  81 YKEQREYFEELKEYGPIYTLWSASEEELADSLKGMASCIDRCCKATDKRMKGLSEQLLPVIHEYVLYSETLMGVIKRRDQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 347 VQAEYEAKLEAVALRKEERPKVPADVEKCQDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESI 426
Cdd:cd07666 161 IQAELDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFTDMAENNISYYEECLATWESF 240

                .
gi 33859789 427 I 427
Cdd:cd07666 241 L 241
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
91-206 8.56e-77

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; 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 consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 234.54  E-value: 8.56e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd06860   1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAK 206
Cdd:cd06860  81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
91-206 1.39e-76

The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; 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. SNX30 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX30 has yet to be elucidated.


Pssm-ID: 132816  Cd Length: 116  Bit Score: 233.82  E-value: 1.39e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd07283   1 LFVTVDDPKKHVCTMETYITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAK 206
Cdd:cd07283  81 EFVETRRKALDKFLKRIADHPVLSFNEHFNVFLTAK 116
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
91-206 8.91e-60

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; 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. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 190.57  E-value: 8.91e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd07284   1 IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMVERFNE 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAK 206
Cdd:cd07284  81 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
91-205 5.98e-33

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; 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. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor 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. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 120.38  E-value: 5.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEkfvvKGVVDRFSE 170
Cdd:cd06859   1 FEISVTDPVKVGDGMSAYVVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVEKYPGRIVPPPPE----KQAVGRFKV 76
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 33859789 171 --EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTA 205
Cdd:cd06859  77 kfEFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLES 113
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
91-204 1.67e-31

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. 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.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 116.62  E-value: 1.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVC-TMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVV-DRF 168
Cdd:cd06863   1 LECLVSDPQKELDgSSDTYISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKHRLEYITgDRF 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859789 169 SEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLT 204
Cdd:cd06863  81 SPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLE 116
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
93-205 3.39e-28

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.


Pssm-ID: 132771  Cd Length: 112  Bit Score: 107.44  E-value: 3.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEkfvvKGVVDRFSEEF 172
Cdd:cd06861   3 ITVGDPHKVGDLTSAHTVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPE----KQSVGRFDDNF 78
                        90       100       110
                ....*....|....*....|....*....|...
gi 33859789 173 VETRRKALDKFLKRITDHPVLSFNEHFNVFLTA 205
Cdd:cd06861  79 VEQRRAALEKMLRKIANHPVLQKDPDFRLFLES 111
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
93-212 6.34e-27

The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; 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. This subfamily consists of SNX9, SNX18, and similar proteins. They contain an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1.


Pssm-ID: 132772  Cd Length: 125  Bit Score: 104.32  E-value: 6.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKH--VCTMETYITYRITTKSTRVefdlpeySVRRRYQDFDWLRNKLEESQPTHLIPPLPEKfvvkGVVDRFSE 170
Cdd:cd06862   3 CTVTNPKKEskFKGLKSFIAYQITPTHTNV-------TVSRRYKHFDWLYERLVEKYSCIAIPPLPEK----QVTGRFEE 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAKDLNAYK 212
Cdd:cd06862  72 DFIEKRRERLELWMNRLARHPVLSQSEVFRHFLTCTDEKDWK 113
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
93-204 6.44e-27

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 103.59  E-value: 6.44e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTMETYITYRITTKSTrvefDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKgvvdRFSEEF 172
Cdd:cd06093   2 VSIPDYEKVKDGGKKYVVYIIEVTTQ----GGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFG----NLDPEF 73
                        90       100       110
                ....*....|....*....|....*....|..
gi 33859789 173 VETRRKALDKFLKRITDHPVLSFNEHFNVFLT 204
Cdd:cd06093  74 IEERRKQLEQYLQSLLNHPELRNSEELKEFLE 105
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
93-205 2.37e-26

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.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 102.50  E-value: 2.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTME------TYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVd 166
Cdd:cd06865   2 ITVSDPKKEQEPSRvplggpPYISYKVTTRTNIPSYTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQV- 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33859789 167 RFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTA 205
Cdd:cd06865  81 MQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTL 119
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
241-428 3.02e-24

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 100.12  E-value: 3.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 241 EFAAISDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALE----GELAEPLEGVSACIGNCSTALEELT 316
Cdd:cd07596   5 EFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEeevgGELGEALSKLGKAAEELSSLSEAQA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 317 DDITEEFLPVLREYVLYSDSMKGVLKKRDQVQAEYEAKLEAVALRKEERPK---------------------VPADVEKC 375
Cdd:cd07596  85 NQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKlkaapgikpakveeleeeleeAESALEEA 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 33859789 376 QDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIP 428
Cdd:cd07596 165 RKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLP 217
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
93-204 3.58e-24

The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; 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. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor.


Pssm-ID: 132774  Cd Length: 129  Bit Score: 97.05  E-value: 3.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKH-----VCTMETYITYRITTKSTR--VEFDLPE--YSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVV-- 161
Cdd:cd06864   3 ITVTEAEKRtggsaMNLKETYTVYLIETKIVEheSEEGLSKklSSLWRRYSEFELLRNYLVVTYPYVIVPPLPEKRAMfm 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 33859789 162 --KGVVDRFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLT 204
Cdd:cd06864  83 wqKLSSDTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLT 127
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
119-204 4.51e-23

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 92.30  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789   119 RVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFvvkgVVDRFSEEFVETRRKALDKFLKRITDHPVLSFNEH 198
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKR----WLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEV 76

                  ....*.
gi 33859789   199 FNVFLT 204
Cdd:pfam00787  77 LLEFLE 82
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
93-193 1.22e-21

The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; 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. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant.


Pssm-ID: 132815  Cd Length: 124  Bit Score: 89.73  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLeESQPTH---LIPPLPEKFVVK------G 163
Cdd:cd07282   3 IGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKL-ASKYLHvgyIVPPAPEKSIVGmtkvkvG 81
                        90       100       110
                ....*....|....*....|....*....|
gi 33859789 164 VVDRFSEEFVETRRKALDKFLKRITDHPVL 193
Cdd:cd07282  82 KEDSSSTEFVEKRRAALERYLQRTVKHPTL 111
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
93-425 1.62e-21

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 96.79  E-value: 1.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTME---TYITYRITTKSTRVEFDL---PEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEK-FVVKGVV 165
Cdd:COG5391 133 STVSNPQSLTLLVDsrdKHTSYEIITVTNLPSFQLresRPLVVRRRYSDFESLHSILIKLLPLCAIPPLPSKkSNSEYYG 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 166 DRFSEEFVETRRKALDKFLKRITDHPVLS-------FNEHFNVFLTAKDLNAYKKQGIAL-LSRVGESVKHvtGGYKLRS 237
Cdd:COG5391 213 DRFSDEFIEERRQSLQNFLRRVSTHPLLSnyknsksWESHSTLLSSFIENRKSVPTPLSLdLTSTTQELDM--ERKELNE 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 238 RplefaaisdyLDTFALKLGTIDRIAQRIIKE------------EIEYLVELREygpvystwSALEGELAEPLE-----G 300
Cdd:COG5391 291 S----------TSKAIHNILSIFSLFEKILIQleseeesltrllESLNNLLLLV--------LNFSGVFAKRLEqnqnsI 352
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 301 VSACIGNCSTALEELTDDITeEFLPVLREYVLYSDSMKGVLKKRDQVQAEYEAKLEAVALRKEERPKV------------ 368
Cdd:COG5391 353 LNEGVVQAETLRSSLKELLT-QLQDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVsqqpegltsfsk 431
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 369 ------PADVEKCQDR----------------------MECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCL 420
Cdd:COG5391 432 lsyklrDFVQEKSRSKsieslqqdkekleeqlaiaekdAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENL 511

                ....*
gi 33859789 421 MAWES 425
Cdd:COG5391 512 EIWKS 516
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
97-204 5.71e-21

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 87.40  E-value: 5.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789     97 DPKKHVCTMETYITYRITTKStrvefDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKfVVKGVVDRFSEEFVETR 176
Cdd:smart00312   3 EPEKIGDGKHYYYVIEIETKT-----GLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGK-KLFGRLNNFSEEFIEKR 76
                           90       100
                   ....*....|....*....|....*....
gi 33859789    177 RKALDKFLKRITDHPVLS-FNEHFNVFLT 204
Cdd:smart00312  77 RRGLEKYLQSLLNHPELInHSEVVLEFLE 105
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
91-193 7.72e-20

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; 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. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 84.73  E-value: 7.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEE--SQPTHLIPPLPEKFVVK------ 162
Cdd:cd07281   1 LKVSITDPEKIGDGMNAYVVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEkhSQNGFIVPPPPEKSLIGmtkvkv 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 33859789 163 GVVDRFSEEFVETRRKALDKFLKRITDHPVL 193
Cdd:cd07281  81 GKEDSSSAEFLERRRAALERYLQRIVSHPSL 111
BAR_Atg24p cd07628
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg24p; BAR domains are ...
241-428 7.20e-19

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg24p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Atg24p is involved in membrane fusion events at the vacuolar surface during pexophagy. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153312  Cd Length: 185  Bit Score: 83.86  E-value: 7.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 241 EFAAISDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALE-GELAEPLEGVSACIGNCSTALEELTDDI 319
Cdd:cd07628   5 EFLEIREKSDKLDENLTKIDKIFAKVVKRQSDLSVDYADLATQFQKLGSLEsGEITEPFKIFSESLSQFSTSLRVLNKYT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 320 TEEFLPVLREYVLYSDSMKGVLKKRDQVQAEYEAkLEAVALRKEerpkvpadVEKCQDRMECFNADLKADMERWQSNKRH 399
Cdd:cd07628  85 DENYLTSLKDLLHYILSLKNLIKLRDQKQLDYEE-LSDYLLTDE--------VENAKETSDAFNKEVLKEYPNFERIKKQ 155
                       170       180
                ....*....|....*....|....*....
gi 33859789 400 DFRQLLVGLADKNIQYYEKCLMAWESIIP 428
Cdd:cd07628 156 EIKDSLGALADGHIDFYQGLVEDWEKVEP 184
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
94-213 1.04e-18

The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; 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. SNX18, like SNX9, contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1.


Pssm-ID: 132819  Cd Length: 127  Bit Score: 81.64  E-value: 1.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  94 TVDDPKKHVC--TMETYITYRITTKSTRVEfdlpeysVRRRYQDFDWLRNKLEESQPTHLIPPLPEKfvvkGVVDRFSEE 171
Cdd:cd07286   4 TIDDPTKQTKfkGMKSYISYKLVPSHTGLQ-------VHRRYKHFDWLYARLAEKFPVISVPHIPEK----QATGRFEED 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33859789 172 FVETRRKALDKFLKRITDHPVLSFNEHFNVFLT--AKDLNAYKK 213
Cdd:cd07286  73 FISKRRKGLIWWMDHMCSHPVLARCDAFQHFLTcpSTDEKAWKQ 116
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
91-208 2.40e-18

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related 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. This subfamily is composed of SNX3, SNX12, and fungal Grd19. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. SNX3/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.


Pssm-ID: 132804  Cd Length: 123  Bit Score: 80.58  E-value: 2.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEEsQPTHLIPPLPEK-----FVVKGVV 165
Cdd:cd06894   2 LEIDVVNPQTHGVGKKRFTDYEVRMRTNLPVFKKKESSVRRRYSDFEWLRSELER-DSKIVVPPLPGKalkrqLPFRGDD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33859789 166 DRFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAKDL 208
Cdd:cd06894  81 GIFEEEFIEERRKGLETFINKVAGHPLAQNEKCLHMFLQEETI 123
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
91-193 1.25e-17

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.


Pssm-ID: 132828  Cd Length: 116  Bit Score: 78.31  E-value: 1.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFvvkgVVDRFSE 170
Cdd:cd07295   2 LEIEVRNPKTHGIGRGMFTDYEIVCRTNIPAFKLRVSSVRRRYSDFEYFRDILERESPRVMIPPLPGKI----FTNRFSD 77
                        90       100
                ....*....|....*....|...
gi 33859789 171 EFVETRRKALDKFLKRITDHPVL 193
Cdd:cd07295  78 EVIEERRQGLETFLQSVAGHPLL 100
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
93-203 5.77e-17

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; 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. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 76.22  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  93 VTVDDPKKHVCTMET-YITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEkfvvKGVVDRF-SE 170
Cdd:cd06898   2 VEVRDPRTHKEDDWGsYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPP----KNLFGRFnNE 77
                        90       100       110
                ....*....|....*....|....*....|...
gi 33859789 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNVFL 203
Cdd:cd06898  78 GFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFL 110
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
82-205 5.61e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; 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. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 73.42  E-value: 5.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  82 DDIDGEARDLFvtvddpKKHVctmetyiTYRITTKSTrvefdlpEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVV 161
Cdd:cd06866   5 VELVPEKKGLF------LKHV-------EYEVSSKRF-------KSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIG 64
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33859789 162 KGVvdrfSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTA 205
Cdd:cd06866  65 GSA----DREFLEARRRGLSRFLNLVARHPVLSEDELVRTFLTE 104
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
91-203 8.11e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; 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. SNX3 associates with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P). It 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. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume.


Pssm-ID: 132826  Cd Length: 123  Bit Score: 73.49  E-value: 8.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPThLIPPLPEKFVVKGVVDR--- 167
Cdd:cd07293   2 LEIDVTNPQTVGVGRGRFTTYEIRLKTNLPIFKLKESTVRRRYSDFEWLRSELERESKV-VVPPLPGKALFRQLPFRgdd 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 33859789 168 --FSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFL 203
Cdd:cd07293  81 giFDDSFIEERKQGLEQFLNKVAGHPLAQNERCLHMFL 118
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
91-209 3.31e-15

The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; 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. The specific function of SNX12 has yet to be elucidated.


Pssm-ID: 132827  Cd Length: 132  Bit Score: 72.00  E-value: 3.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  91 LFVTVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPThLIPPLPEKFVVKGVVDR--- 167
Cdd:cd07294   4 LEIDIFNPQTVGVGRNRFTTYEVRMRTNLPIFKLKESCVRRRYSDFEWLKNELERDSKI-VVPPLPGKALKRQLPFRgde 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33859789 168 --FSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAKDLN 209
Cdd:cd07294  83 giFEESFIEERRQGLEQFINKIAGHPLAQNERCLHMFLQDETID 126
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
95-212 6.16e-15

The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; 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. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization.


Pssm-ID: 132818  Cd Length: 126  Bit Score: 71.21  E-value: 6.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  95 VDDPKK--HVCTMETYITYRITTKSTrvefdlpEYSVRRRYQDFDWLRNKLEESQPTHL-IPPLPEKfvvkGVVDRFSEE 171
Cdd:cd07285   5 VADPRKgsKMYGLKSYIEYQLTPTNT-------NRSVNHRYKHFDWLYERLLVKFGLAIpIPSLPDK----QVTGRFEEE 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33859789 172 FVETRRKALDKFLKRITDHPVLSFNEHFNVFLTAKDLNAYK 212
Cdd:cd07285  74 FIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWK 114
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
107-203 1.08e-14

The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; 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. SNX41 and SNX42 (also called Atg20p) form dimers with SNX4, and are required in protein recycling from the sorting endosome (post-Golgi endosome) back to the late Golgi in yeast.


Pssm-ID: 132777  Cd Length: 112  Bit Score: 69.97  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 107 TYITYRITTKSTrvefdlpeySVRRRYQDFDWLRNKLEESQPTHLIPPLPEK-----FVVKGVVDRFSEEFVETRRKALD 181
Cdd:cd06867  17 SYIVYVIRLGGS---------EVKRRYSEFESLRKNLTRLYPTLIIPPIPEKhslkdYAKKPSKAKNDAKIIERRKRMLQ 87
                        90       100
                ....*....|....*....|..
gi 33859789 182 KFLKRITDHPVLSFNEHFNVFL 203
Cdd:cd06867  88 RFLNRCLQHPILRNDIVFQKFL 109
BAR_SNX4 cd07622
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid ...
227-431 1.36e-12

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153306  Cd Length: 201  Bit Score: 66.26  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 227 KHVTGGYKLRSRPLEFAAISDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGvsacIG 306
Cdd:cd07622   1 KALNASFRLRNPDKRFEDLKNYSDELQTNLNNLLKVRARLAERLYGVYKIHANYGRVFSEWSAIEKEMGDGLQK----AG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 307 NCSTALEELTDDITEE---FLPVLREYVLYSDSMKGVLKKRDQVQAEYEAKLEAVALRKEErpkVPADVEKCQDRMECFN 383
Cdd:cd07622  77 HYMDSYAASIDNGLEDeelIADQLKEYLFFADSLRAVCKKHELLQYDLEKAEDALANKKQQ---GEEAVKEAKDELNEFV 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 33859789 384 ADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIPLLQ 431
Cdd:cd07622 154 KKALEDVERFKKQKVRDLKEILISYAKLQIKLAKKGLQTWTNIKECLQ 201
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
112-203 1.59e-10

The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.


Pssm-ID: 132813  Cd Length: 120  Bit Score: 58.49  E-value: 1.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 112 RITTKstrvefDLPEYSV--RRRYQDFDWLRNKLEESQPTHL---IPPLPEKFVVKGVVDRFSEEFVETRRKALDKFLKR 186
Cdd:cd07280  28 TIETK------DLIGSSIvaYKRYSEFVQLREALLDEFPRHKrneIPQLPPKVPWYDSRVNLNKAWLEKRRRGLQYFLNC 101
                        90
                ....*....|....*..
gi 33859789 187 ITDHPVLSFNEHFNVFL 203
Cdd:cd07280 102 VLLNPVFGGSPVVKEFL 118
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
109-203 2.45e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; 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. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 58.53  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 109 ITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQPTH--LIPPLPEKFVVKGVVDRF-----------SEEFVET 175
Cdd:cd07291  17 VKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAglIIPPAPPKPDFDGPREKMqklgegegsmtKEEFAKM 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33859789 176 RRK------ALDK--------FLKRITDHPVLSFNEHFNVFL 203
Cdd:cd07291  97 KQEleaeylAVFKktvqvhevFLQRLSSHPSLSKDRNFHIFL 138
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
107-203 7.84e-10

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 56.13  E-value: 7.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 107 TYITYRITtkstrVEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDrfSEEFVETRRKALDKFLKR 186
Cdd:cd06897  14 PYTVYNIQ-----VRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFLSTSS--NPKLVEERRVGLEAFLRA 86
                        90
                ....*....|....*....
gi 33859789 187 ITDHPVLSFNEHFNV--FL 203
Cdd:cd06897  87 LLNDEDSRWRNSPAVkeFL 105
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
120-203 8.69e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; 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. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.


Pssm-ID: 132803 [Multi-domain]  Cd Length: 132  Bit Score: 51.00  E-value: 8.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 120 VEFDLPEYSVRRRYQDFDWLRNKLEESQ----------PTHLIPPLPekfvvKGVVDRfseEFVETRRKALDKFLKRITD 189
Cdd:cd06893  44 SEQPLATHTVNRRFREFLTLQTRLEENPkfrkimnvkgPPKRLFDLP-----FGNMDK---DKIEARRGLLETFLRQLCS 115
                        90
                ....*....|....
gi 33859789 190 HPVLSFNEHFNVFL 203
Cdd:cd06893 116 IPEISNSEEVQEFL 129
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
104-206 2.33e-07

The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132778  Cd Length: 120  Bit Score: 49.33  E-value: 2.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 104 TMETYITYRITTKSTRVEF--------DLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDrfseefVET 175
Cdd:cd06868  16 TSSGHVLYQIVVVTRLAAFksakhkeeDVVQFMVSKKYSEFEELYKKLSEKYPGTILPPLPRKALFVSESD------IRE 89
                        90       100       110
                ....*....|....*....|....*....|.
gi 33859789 176 RRKALDKFLKRITDHPVLSFNEHFNVFLTAK 206
Cdd:cd06868  90 RRAAFNDFMRFISKDEKLANCPELLEFLGVK 120
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
119-205 2.98e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; 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. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 48.91  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 119 RVEFDLPE-YSVRRRYQDFDWLRNKLEESQPTHLIPPLPEK--FVVKgvvdrfSEEFVETRRKALDKFLKRITDHPVLSF 195
Cdd:cd06877  35 RAKGHEPQhWSVLRRYNEFYVLESKLTEFHGEFPDAPLPSRriFGPK------SYEFLESKREIFEEFLQKLLQKPELRG 108
                        90
                ....*....|
gi 33859789 196 NEHFNVFLTA 205
Cdd:cd06877 109 SELLYDFLSP 118
BAR_Atg20p cd07629
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg20p; BAR domains are ...
257-426 2.98e-07

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg20p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The function of Atg20p is unknown but it has been shown to interact with Atg11p, which plays a role in linking cargo molecules with vesicle-forming components. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153313  Cd Length: 187  Bit Score: 50.47  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 257 GTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALE--GELAEPLEGVSACIGNCSTALEELTDDITEEFLPVLREYVLYS 334
Cdd:cd07629  22 GGMEKVNRRITKRLGDLAEDMADLGGRFNAFSLEEqkSELAEALEKVGQAVDSTYLATEALVGSLYYNINEPLSESAQFA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 335 DSMKGVLKKRDQVQAEYEAKLEAValrKEERPKVPADVEKCQdrmecfNADLKADMERWQSNKRHDFRQLLVGLADKNIQ 414
Cdd:cd07629 102 GVVRELLKYRKLKHVQYEMTKDSL---LESALVAASDDLVIS------STIKQKDLPRFQREREADLREILKNYSKYHKD 172
                       170
                ....*....|..
gi 33859789 415 YYEKCLMAWESI 426
Cdd:cd07629 173 WAKQNLEAWKEA 184
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
94-202 3.93e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. 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. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 48.47  E-value: 3.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  94 TVDDPKKHvctMETYITYRITTK--STRVEFDLPEYSVRRRYQDFdwlrNKL-EESQPTH-------LIPPLPEKFVVKg 163
Cdd:cd06881   6 TVTDTRRH---KKGYTEYKITSKvfSRSVPEDVSEVVVWKRYSDF----KKLhRELSRLHkqlylsgSFPPFPKGKYFG- 77
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33859789 164 vvdRFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVF 202
Cdd:cd06881  78 ---RFDAAVIEERRQAILELLDFVGNHPALYQSSAFQQF 113
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
126-205 1.22e-06

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 47.02  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 126 EYSVRRRYQDFDWLRNKLEESQP-THLipPLPEKfvvKGVVDRFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNVFLT 204
Cdd:cd06870  33 SWFVFRRYAEFDKLYESLKKQFPaSNL--KIPGK---RLFGNNFDPDFIKQRRAGLDEFIQRLVSDPKLLNHPDVRAFLQ 107

                .
gi 33859789 205 A 205
Cdd:cd06870 108 M 108
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
124-194 1.64e-06

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 46.97  E-value: 1.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33859789 124 LPEYS--VRRRYQDFDWLRNKLEESQpthLIPPLPEKFVVkGVVDRfseEFVETRRKALDKFLKRITDHPVLS 194
Cdd:cd06871  33 SPENSwqVIRRYNDFDLLNASLQISG---ISLPLPPKKLI-GNMDR---EFIAERQQGLQNYLNVILMNPILA 98
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
286-428 2.02e-06

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 48.21  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 286 TWSALEGELAEPLEGVSACIGNCSTALEELTDDITEEFLPVLREYVlysDSMKGVL----KKRDQVQAEYEAKLEAVA-L 360
Cdd:cd07307  44 LPDLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYL---KKDLKEIkkrrKKLDKARLDYDAAREKLKkL 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33859789 361 RK-----EERPKVPADVEKCQDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQYYEKCLMAWESIIP 428
Cdd:cd07307 121 RKkkkdsSKLAEAEEELQEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLP 193
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
112-194 2.06e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; 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. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 46.25  E-value: 2.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 112 RITTKSTRVEFDLPEY-SVRRRYQDFDWLRNKLEESQPtHLIPPLPEKFVVKgvvDRFSEEFVETRRKALDKFLKRITDH 190
Cdd:cd07276  19 RFTVYKIRVENKVGDSwFVFRRYTDFVRLNDKLKQMFP-GFRLSLPPKRWFK---DNFDPDFLEERQLGLQAFVNNIMAH 94

                ....
gi 33859789 191 PVLS 194
Cdd:cd07276  95 KDIA 98
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
109-203 2.30e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; 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. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p.


Pssm-ID: 132802  Cd Length: 141  Bit Score: 47.04  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 109 ITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQ--PTHLIPPLP---------EKFVVKG------VVDRF--- 168
Cdd:cd06892  17 VKFTVHTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENEdyAGLIIPPAPpkpdfdasrEKLQKLGegegsmTKEEFekm 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33859789 169 ----SEEFVETRRKAL---DKFLKRITDHPVLSFNEHFNVFL 203
Cdd:cd06892  97 kqelEAEYLAIFKKTVamhEVFLRRLASHPVLRNDANFRVFL 138
PX_RPK118_like cd07287
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ...
92-193 1.10e-05

The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. 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. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132820  Cd Length: 118  Bit Score: 44.57  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  92 FVTVDDPKKHvctMETYITYRITTK--STRVEFDLPEYSVRRRYQDFDWLRNKLEE-----SQPTHLIPPlpekFVVKGV 164
Cdd:cd07287   4 FYTVTDPRRH---PKGYTVYKVTARivSRKNPEDVQEIVVWKRYSDFKKLHKDLWQihknlCRQSELFPP----FAKAKV 76
                        90       100
                ....*....|....*....|....*....
gi 33859789 165 VDRFSEEFVETRRKALDKFLKRITDHPVL 193
Cdd:cd07287  77 FGRFDESVIEERRQCAEDLLQFSANIPAL 105
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
104-185 1.62e-05

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. 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. 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.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 43.81  E-value: 1.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 104 TMETYITYRITTKSTRVEfdlpeYSVRRRYQDFDWLRNKL--EESQPTHLIPPlpekfvvKGVVDRFSEEFVETRRKALD 181
Cdd:cd06875  13 TVEGYTVYIIEVKVGSVE-----WTVKHRYSDFAELHDKLvaEHKVDKDLLPP-------KKLIGNKSPSFVEKRRKELE 80

                ....
gi 33859789 182 KFLK 185
Cdd:cd06875  81 IYLQ 84
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
92-193 2.81e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; 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. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 43.42  E-value: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  92 FVTVDDPKKHvctMETYITYRITTK--STRVEFDLPEYSVRRRYQDFDWLRNKLEES-----QPTHLIPPLPEKfvvkGV 164
Cdd:cd07288   4 FYSVTDPRTH---PKGYTEYKVTAQfiSKKQPEDVKEVVVWKRYSDLKKLHGELAYThrnlfRRQEEFPPFPRA----QV 76
                        90       100
                ....*....|....*....|....*....
gi 33859789 165 VDRFSEEFVETRRKALDKFLKRITDHPVL 193
Cdd:cd07288  77 FGRFEAAVIEERRNAAEAMLLFTVNIPAL 105
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
107-196 3.55e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; 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. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 43.03  E-value: 3.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 107 TYITYRITTksTRVEFDLPEYS--VRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVvdrfSEEFVETRRKALDKFL 184
Cdd:cd06873  21 TYAVYAISV--TRIYPNGQEESwhVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNL----DRAFLEKRRKMLNQYL 94
                        90
                ....*....|..
gi 33859789 185 KRITDHPVLSFN 196
Cdd:cd06873  95 QSLLNPEVLDAN 106
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
94-204 3.62e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; 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. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 42.70  E-value: 3.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789  94 TVDDPKKHvctmetYITYRITTKSTRvEFDLPEYSVRRRYQDFDWLRNKLEESQPtHLIPPLpeKFVVKGVVDRFSEEFV 173
Cdd:cd07279  10 TVKEGEKK------YVVYQLAVVQTG-DPDTQPAFIERRYSDFLKLYKALRKQHP-QLMAKV--SFPRKVLMGNFSSELI 79
                        90       100       110
                ....*....|....*....|....*....|.
gi 33859789 174 ETRRKALDKFLKRITDHPVLSFNEHFNVFLT 204
Cdd:cd07279  80 AERSRAFEQFLGHILSIPNLRDSKAFLDFLQ 110
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
302-428 1.36e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153307  Cd Length: 224  Bit Score: 43.03  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 302 SACIGNC------STALEELTDdiTEE----------------FLPVLREYVLYSDSMKGVL------------------ 341
Cdd:cd07623  56 AAMLSNCeehtslSRALSQLAE--VEEkieqlhgeqadtdfyiLAELLKDYIGLIGAIKDVFhervkvwqnwqnaqqtlt 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 342 KKRDQvqaeyEAKLEAvALRKEERPKVPAD-------VEKCQDRMECFNADLKADMERWQSNKRHDFRQLLVGLADKNIQ 414
Cdd:cd07623 134 KKREA-----KAKLEL-SGRTDKLDQAQQEikeweakVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLN 207
                       170
                ....*....|....
gi 33859789 415 YYEKCLMAWESIIP 428
Cdd:cd07623 208 TQQQLIKYWEAFLP 221
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
109-203 2.04e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; 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. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 41.24  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 109 ITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRNKLEESQ--PTHLIPPLP---------EKF--VVKGVVDRFSEEFVET 175
Cdd:cd07292  17 VKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEdyAGYIIPPAPprpdfdasrEKLqkLGEGEGSMTKEEFTKM 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33859789 176 RRK------ALDK--------FLKRITDHPVLSFNEHFNVFL 203
Cdd:cd07292  97 KQEleaeylAIFKktvamhevFLCRVAAHPILRKDLNFHVFL 138
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
265-420 3.82e-04

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 41.94  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789   265 RIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIG-----------------NCSTALEELTDDITEEFLPVL 327
Cdd:pfam03114  44 KLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIEAGKDLGedssfgkaledygealkRLAQLLEQLDDRVETNFLDPL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789   328 REYVLYSDSMKGVLKKRDQVQAEYEAKLEAV-ALRKEERPKVPA------DVEKCQDRMECFNADLKADMERWQSNKRHD 400
Cdd:pfam03114 124 RNLLKEFKEIQKHRKKLERKRLDYDAAKTRVkKAKKKKSSKAKDesqaeeELRKAQAKFEESNEQLKALLPNLLSLEVEF 203
                         170       180
                  ....*....|....*....|
gi 33859789   401 FRQLLVGLADKNIQYYEKCL 420
Cdd:pfam03114 204 VVNQLVAFVEAQLDFHRQCY 223
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
123-205 2.44e-03

The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132779  Cd Length: 119  Bit Score: 37.65  E-value: 2.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 123 DLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKfvvkgvvDRFseeFVETRRKALDKFLKRITDHPVLSFNEHFNVF 202
Cdd:cd06869  46 EYRTIYVARRYSDFKKLHHDLKKEFPGKKLPKLPHK-------DKL---PREKLRLSLRQYLRSLLKDPEVAHSSILQEF 115

                ...
gi 33859789 203 LTA 205
Cdd:cd06869 116 LTS 118
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
129-204 3.54e-03

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. 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.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 37.67  E-value: 3.54e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33859789 129 VRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVkgvVDRFSE-EFVETRRKALDKFLKRITDHPVLSFNEHFNVFLT 204
Cdd:cd06876  59 VARRYSEFLELHKYLKKRYPGVLKLDFPQKRKI---SLKYSKtLLVEERRKALEKYLQELLKIPEVCEDEEFRKFLS 132
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
105-191 8.82e-03

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 35.79  E-value: 8.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789 105 METYITYRIttKSTRVEFDLPEYsVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVV-----KGVVDRfseefvetRRKA 179
Cdd:cd06883  13 PEKYYIYVV--KVTRENQTEPSF-VFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLgrshiKQVAER--------RKIE 81
                        90
                ....*....|..
gi 33859789 180 LDKFLKRITDHP 191
Cdd:cd06883  82 LNSYLKSLFNAS 93
BAR smart00721
BAR domain;
212-420 9.08e-03

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 37.75  E-value: 9.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789    212 KKQgialLSRVGESVKHVTGGyklrsrpLEFAAISDYLDTFALKLGTIDRIAQRIIKEEIEYL-------VELREY---- 280
Cdd:smart00721   3 KKQ----FNRAKQKVGEKVGK-------AEKTKLDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnpavrAKLASQkkls 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789    281 ---GPVYSTWSALEGelAEPLEGVSACIGNCSTALEELTDdITEEFLPVLREYVL-----YSDSMKGV---LKKRDQVQA 349
Cdd:smart00721  72 kslGEVYEGGDDGEG--LGADSSYGKALDKLGEALKKLLQ-VEESLSQVKRTFILpllnfLLGEFKEIkkaRKKLERKLL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859789    350 EYEAKLEAV--ALRKEERPKVP------ADVEKCQDRMECFNADLKADMERWqSNKRHDFR-QLLVGLADKNIQYYEKCL 420
Cdd:smart00721 149 DYDSARHKLkkAKKSKEKKKDEklakaeEELRKAKQEFEESNAQLVEELPQL-VASRVDFFvNCLQALIEAQLNFHRESY 227
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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