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Conserved domains on  [gi|357492829|ref|XP_003616703|]
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sorting nexin 2B [Medicago truncatula]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10246345)

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_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 279-507 3.44e-56

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: 187.18  E-value: 3.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTKFETEEAefesQRVRAADMKNVATAAVK 358
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVG----GELGEALSKLGKAAEEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYRELNTQTIKHLDKLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVASSrifggdkSRMRKIEE 438
Cdd:cd07596   77 SSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPG-------IKPAKVEE 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357492829 439 LKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:cd07596  150 LEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 92-206 6.30e-50

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.


The actual alignment was detected with superfamily member cd06865:

Pssm-ID: 470617  Cd Length: 120  Bit Score: 167.21  E-value: 6.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQEEQEvTNSLVPGGSSYHTYLITTRT-----GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKV 166
Cdd:cd06865    2 ITVSDPKKEQE-PSRVPLGGPPYISYKVTTRTnipsyTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 357492829 167 MQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd06865   81 MQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
 
Name Accession Description Interval E-value
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 279-507 3.44e-56

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: 187.18  E-value: 3.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTKFETEEAefesQRVRAADMKNVATAAVK 358
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVG----GELGEALSKLGKAAEEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYRELNTQTIKHLDKLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVASSrifggdkSRMRKIEE 438
Cdd:cd07596   77 SSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPG-------IKPAKVEE 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357492829 439 LKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:cd07596  150 LEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 92-206 6.30e-50

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: 167.21  E-value: 6.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQEEQEvTNSLVPGGSSYHTYLITTRT-----GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKV 166
Cdd:cd06865    2 ITVSDPKKEQE-PSRVPLGGPPYISYKVTTRTnipsyTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 357492829 167 MQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd06865   81 MQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 109-204 1.60e-18

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: 80.85  E-value: 1.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829   109 PGGSSYHTYLITTRTGKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKVMQKEEFVEQRRLALEKYLRKLG 188
Cdd:smart00312   9 DGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLNNFSEEFIEKRRRGLEKYLQSLL 88

                           90
                   ....*....|....*..
gi 357492829   189 LHPVIGK-SEELRVFLQ 204
Cdd:smart00312  89 NHPELINhSEVVLEFLE 105
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 277-507 2.16e-14

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 72.70  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  277 VVEEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLtkfeteeAEFESQRVRAADMKNVATAA 356
Cdd:pfam09325  19 FNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASL-------ASLELSTGLSRALSQLAEVE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  357 VKASRLYRELNTQTIKHL-DKLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVAssrifggDKSRMRK 435
Cdd:pfam09325  92 ERIKELLERQALQDVLTLgETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLLRA-------NKSQNDK 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357492829  436 IEELKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:pfam09325 165 LQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQKELIELWETFLPE 236
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 124-206 2.28e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 68.42  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  124 GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKvmqKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:pfam00787   5 SLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRY---NEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81


                  ...
gi 357492829  204 QVQ 206
Cdd:pfam00787  82 ESD 84
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 80-511 8.39e-10

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 60.97  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  80 GSGSGTESD-SIHISVSDPQEEqevtNSLVPGGSSYHTYLITTRT-----GKSEYG---VRRRFREVVTLSERLSEVYRG 150
Cdd:COG5391  120 LSTSHTILDyFISSTVSNPQSL----TLLVDSRDKHTSYEIITVTnlpsfQLRESRplvVRRRYSDFESLHSILIKLLPL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 151 YVIPVRPEKSSVERKVMQK--EEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQgklplmrtTDVASrmldgavrl 228
Cdd:COG5391  196 CAIPPLPSKKSNSEYYGDRfsDEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHS--------TLLSS--------- 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 229 PRQLFGAESGvvdlNDVAQPAKSGRDLLRIFKELKQSVS----------NDWGGAKPLVVEEDKEFMEKKDKLMEFEQQL 298
Cdd:COG5391  259 FIENRKSVPT----PLSLDLTSTTQELDMERKELNESTSkaihnilsifSLFEKILIQLESEEESLTRLLESLNNLLLLV 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 299 SNVSQQAESLVKFQQD------MGETMGELGLAFVKLTKFETEEAEFESqrvRAADMKNvataavkasrlYRELNTQTIK 372
Cdd:COG5391  335 LNFSGVFAKRLEQNQNsilnegVVQAETLRSSLKELLTQLQDEIKSRES---LILTDSN-----------LEKLTDQNLE 400

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 373 HLDKLHEYLGTMlainnafadrssallTVQTLSSELASLHSRIEKLEVASSRIFGGDKSRMRKIEELKEAVR-VTESAKI 451
Cdd:COG5391  401 DVEELSRSLRKN---------------SSQRAVVSQQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDKEkLEEQLAI 465

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 452 CaDREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEETSTY 511
Cdd:COG5391  466 A-EKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSVKEQLDRL 524
 
Name Accession Description Interval E-value
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 279-507 3.44e-56

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: 187.18  E-value: 3.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTKFETEEAefesQRVRAADMKNVATAAVK 358
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVG----GELGEALSKLGKAAEEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYRELNTQTIKHLDKLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVASSrifggdkSRMRKIEE 438
Cdd:cd07596   77 SSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPG-------IKPAKVEE 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357492829 439 LKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:cd07596  150 LEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 92-206 6.30e-50

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: 167.21  E-value: 6.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQEEQEvTNSLVPGGSSYHTYLITTRT-----GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKV 166
Cdd:cd06865    2 ITVSDPKKEQE-PSRVPLGGPPYISYKVTTRTnipsyTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 357492829 167 MQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd06865   81 MQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 90-204 5.92e-28

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: 107.66  E-value: 5.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQEEQEvtnslvpGGSSYHTYLITTRTG-----KSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVER 164
Cdd:cd06859    1 FEISVTDPVKVGD-------GMSAYVVYRVTTKTNlpdfkKSEFSVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGR 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 357492829 165 kVMQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06859   74 -FKVKFEFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLE 112
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 92-204 2.47e-22

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: 92.03  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQEEQEVTnslvpggSSYHTYLITTRTG-----KSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKv 166
Cdd:cd06861    3 ITVGDPHKVGDLT-------SAHTVYTVRTRTTspnfeVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRF- 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 357492829 167 mqKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06861   75 --DDNFVEQRRAALEKMLRKIANHPVLQKDPDFRLFLE 110
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 91-204 1.74e-19

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: 83.56  E-value: 1.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  91 HISVSDPQEEQEvtnslvpGGSSYHTYLITTRT-GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKvmqK 169
Cdd:cd06093    1 SVSIPDYEKVKD-------GGKKYVVYIIEVTTqGGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNL---D 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 357492829 170 EEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06093   71 PEFIEERRKQLEQYLQSLLNHPELRNSEELKEFLE 105
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 90-204 1.86e-19

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: 84.34  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQEEQEvtnslvpGGSSYHTYLITTRT-----GKSEYGVRRRFREVVTLSERLSEVYR--GYVIPVRPEKSSV 162
Cdd:cd07282    1 IEIGVSDPEKVGD-------GMNAYMAYRVTTKTslsmfSRSEFSVRRRFSDFLGLHSKLASKYLhvGYIVPPAPEKSIV 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 357492829 163 ---ERKVMQKE----EFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd07282   74 gmtKVKVGKEDssstEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLE 122
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 92-203 5.40e-19

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: 82.38  E-value: 5.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQeeqevtnSLVPGGSSYHTYLITTRTGKS-----EYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKV 166
Cdd:cd06860    3 ITVDNPE-------KHVTTLETYITYRVTTKTTRSefdssEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLL 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 357492829 167 MQ-KEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06860   76 DRfSPEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFL 113
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 109-204 1.60e-18

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: 80.85  E-value: 1.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829   109 PGGSSYHTYLITTRTGKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKVMQKEEFVEQRRLALEKYLRKLG 188
Cdd:smart00312   9 DGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLNNFSEEFIEKRRRGLEKYLQSLL 88

                           90
                   ....*....|....*..
gi 357492829   189 LHPVIGK-SEELRVFLQ 204
Cdd:smart00312  89 NHPELINhSEVVLEFLE 105
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 90-203 1.90e-15

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: 72.71  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQEEqevtnsLVPGGSSYHTYLITTRTG-----KSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVE- 163
Cdd:cd06863    1 LECLVSDPQKE------LDGSSDTYISYLITTKTNlpsfsRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKHRLEy 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 357492829 164 -RKVMQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06863   75 iTGDRFSPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFL 115
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 90-206 2.23e-15

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: 72.32  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQeeqevtnSLVPGGSSYHTYLITTRTGK-----SEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVER 164
Cdd:cd07284    1 IFITVDEPE-------SHVTAIETFITYRVMTKTSRsefdsSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKG 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 357492829 165 KVMQ-KEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd07284   74 MVERfNEDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 90-204 6.39e-15

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: 71.24  E-value: 6.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQEEQEvtnslvpGGSSYHTYLITTRTG-----KSEYGVRRRFREVVTLSERLSEVY--RGYVIPVRPEKS-- 160
Cdd:cd07281    1 LKVSITDPEKIGD-------GMNAYVVYKVTTQTSllmfrSKHFTVKRRFSDFLGLYEKLSEKHsqNGFIVPPPPEKSli 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 357492829 161 -----SVERKVMQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd07281   74 gmtkvKVGKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLE 122
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 277-507 2.16e-14

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 72.70  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  277 VVEEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLtkfeteeAEFESQRVRAADMKNVATAA 356
Cdd:pfam09325  19 FNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASL-------ASLELSTGLSRALSQLAEVE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  357 VKASRLYRELNTQTIKHL-DKLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVAssrifggDKSRMRK 435
Cdd:pfam09325  92 ERIKELLERQALQDVLTLgETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLLRA-------NKSQNDK 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357492829  436 IEELKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:pfam09325 165 LQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQKELIELWETFLPE 236
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 124-206 2.28e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 68.42  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  124 GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKvmqKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:pfam00787   5 SLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRY---NEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81


                  ...
gi 357492829  204 QVQ 206
Cdd:pfam00787  82 ESD 84
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 91-204 1.60e-13

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: 67.34  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  91 HISVSDPQEEqevtnSLVPGGSSYHTYLIT-TRTGKSeygVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERkvmQK 169
Cdd:cd06862    2 HCTVTNPKKE-----SKFKGLKSFIAYQITpTHTNVT---VSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGR---FE 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 357492829 170 EEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06862   71 EDFIEKRRERLELWMNRLARHPVLSQSEVFRHFLT 105
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 90-206 5.73e-13

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: 65.49  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQEEqevtnslVPGGSSYHTYLITTRTGKSE-----YGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVER 164
Cdd:cd07283    1 LFVTVDDPKKH-------VCTMETYITYRVTTKTTRTEfdlpeYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKG 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 357492829 165 KVMQ-KEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd07283   74 VVDRfSEEFVETRRKALDKFLKRIADHPVLSFNEHFNVFLTAK 116
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 114-203 4.57e-11

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: 59.55  E-value: 4.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 114 YHTYLITTRTGKSEygVRRRFREVVTLSERLSEVYRGYVIPVRPEKssverKVMQ--KEEFVEQRRLALEKYLRKLGLHP 191
Cdd:cd06866   18 HVEYEVSSKRFKST--VYRRYSDFVWLHEYLLKRYPYRMVPALPPK-----RIGGsaDREFLEARRRGLSRFLNLVARHP 90

                         90
                 ....*....|..
gi 357492829 192 VIGKSEELRVFL 203
Cdd:cd06866   91 VLSEDELVRTFL 102
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 92-204 1.08e-10

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: 59.30  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPqeEQEVTNSLVPGGSSYHTYLITTRTGKSE---------YGVRRRFREVVTLSERLSEVYRGYVIPVRPEKssv 162
Cdd:cd06864    3 ITVTEA--EKRTGGSAMNLKETYTVYLIETKIVEHEseeglskklSSLWRRYSEFELLRNYLVVTYPYVIVPPLPEK--- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357492829 163 erKVM---QK-------EEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06864   78 --RAMfmwQKlssdtfdPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLT 127
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 279-508 1.59e-10

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: 61.14  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTkfETEEAEFESQRvraadMKNVATAAVK 358
Cdd:cd07623    9 ETDQWFEEKQQQIENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLS--NCEEHTSLSRA-----LSQLAEVEEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYREL-NTQTIKHLDKLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVASsrifggdksRMRKIE 437
Cdd:cd07623   82 IEQLHGEQaDTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKREAKAKLELSG---------RTDKLD 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357492829 438 ELKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEET 508
Cdd:cd07623  153 QAQQEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQQLIKYWEAFLPEA 223
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 110-203 6.93e-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: 56.57  E-value: 6.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 110 GGSSYHTYLITTRTGKSEYG---VRRRFREVVTLSERLSEVY---RGYVIPVRPEKS--SVERKVMQKEeFVEQRRLALE 181
Cdd:cd07280   18 GGGAYVVWKITIETKDLIGSsivAYKRYSEFVQLREALLDEFprhKRNEIPQLPPKVpwYDSRVNLNKA-WLEKRRRGLQ 96

                         90       100
                 ....*....|....*....|..
gi 357492829 182 KYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd07280   97 YFLNCVLLNPVFGGSPVVKEFL 118
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 80-511 8.39e-10

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 60.97  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  80 GSGSGTESD-SIHISVSDPQEEqevtNSLVPGGSSYHTYLITTRT-----GKSEYG---VRRRFREVVTLSERLSEVYRG 150
Cdd:COG5391  120 LSTSHTILDyFISSTVSNPQSL----TLLVDSRDKHTSYEIITVTnlpsfQLRESRplvVRRRYSDFESLHSILIKLLPL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 151 YVIPVRPEKSSVERKVMQK--EEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQgklplmrtTDVASrmldgavrl 228
Cdd:COG5391  196 CAIPPLPSKKSNSEYYGDRfsDEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHS--------TLLSS--------- 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 229 PRQLFGAESGvvdlNDVAQPAKSGRDLLRIFKELKQSVS----------NDWGGAKPLVVEEDKEFMEKKDKLMEFEQQL 298
Cdd:COG5391  259 FIENRKSVPT----PLSLDLTSTTQELDMERKELNESTSkaihnilsifSLFEKILIQLESEEESLTRLLESLNNLLLLV 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 299 SNVSQQAESLVKFQQD------MGETMGELGLAFVKLTKFETEEAEFESqrvRAADMKNvataavkasrlYRELNTQTIK 372
Cdd:COG5391  335 LNFSGVFAKRLEQNQNsilnegVVQAETLRSSLKELLTQLQDEIKSRES---LILTDSN-----------LEKLTDQNLE 400

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 373 HLDKLHEYLGTMlainnafadrssallTVQTLSSELASLHSRIEKLEVASSRIFGGDKSRMRKIEELKEAVR-VTESAKI 451
Cdd:COG5391  401 DVEELSRSLRKN---------------SSQRAVVSQQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDKEkLEEQLAI 465

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 452 CaDREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEETSTY 511
Cdd:COG5391  466 A-EKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSVKEQLDRL 524
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 279-481 1.41e-09

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; 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. 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. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 58.08  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLtkfeteeAEFESQRVRAADMKNVATAAVK 358
Cdd:cd07627    1 EPDEWFIEKKQYLDSLESQLKQLYKSLELVSSQRKELASATEEFAETLEAL-------SSLELSKSLSDLLAALAEVQKR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYRELNTQTIKHLD-KLHEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVASsrifggdKSRMRKIE 437
Cdd:cd07627   74 IKESLERQALQDVLTLGvTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQLEKLKRQG-------KTQQEKLN 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 357492829 438 ELKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQN 481
Cdd:cd07627  147 SLLSELEEAERRASELKKEFEEVSELIKSELERFERERVEDFRN 190
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 130-203 5.19e-09

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: 54.62  E-value: 5.19e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357492829 130 VRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKVMQKEeFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06876   59 VARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKTL-LVEERRKALEKYLQELLKIPEVCEDEEFRKFL 131
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 111-206 1.44e-08

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: 52.66  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 111 GSSYHTYLITTRTGKSEYGVRRRFREVVTLSERL-SEVYRGYVIPVrPEKSSVeRKVMQKEEFVEQRRLALEKYLRKLGL 189
Cdd:cd06897   12 PKPYTVYNIQVRLPLRSYTVSRRYSEFVALHKQLeSEVGIEPPYPL-PPKSWF-LSTSSNPKLVEERRVGLEAFLRALLN 89

                         90
                 ....*....|....*....
gi 357492829 190 HPV--IGKSEELRVFLQVQ 206
Cdd:cd06897   90 DEDsrWRNSPAVKEFLNLP 108
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 105-203 4.17e-08

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: 51.48  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 105 NSLVPGGSSYHTYLIttRTGKSEygVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSV------ERKVMQKEEFVEQRRL 178
Cdd:cd06867    9 KSSEGGSGSYIVYVI--RLGGSE--VKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSLkdyakkPSKAKNDAKIIERRKR 84

                         90       100
                 ....*....|....*....|....*
gi 357492829 179 ALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06867   85 MLQRFLNRCLQHPILRNDIVFQKFL 109
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
 91-206 2.53e-07

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: 49.25  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  91 HISVSDPQEEQEvtnslvPGGSSYHTYLITTRT-----GKSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERk 165
Cdd:cd06898    1 SVEVRDPRTHKE------DDWGSYTDYEIFLHTnsmcfTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGR- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 357492829 166 vMQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd06898   74 -FNNEGFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFLQTQ 113
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 130-203 9.35e-07

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: 47.92  E-value: 9.35e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357492829 130 VRRRFREVVTLSERLSEV--YRGYVIPVRPEKSSVERKV--MQKEEfVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06893   53 VNRRFREFLTLQTRLEENpkFRKIMNVKGPPKRLFDLPFgnMDKDK-IEARRGLLETFLRQLCSIPEISNSEEVQEFL 129
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
 88-206 1.30e-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: 47.81  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  88 DSIHISVSDPQEEQEVTNSLVpggssyHTYLITTRTGKSEYGVRRRFREVVTLSERLSEV--YRGYVIPVRPEKSSVERK 165
Cdd:cd06892    1 SSLQVDISDALSERDKVKFTV------HTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENedYAGLIIPPAPPKPDFDAS 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357492829 166 ------------VMQKEEF------VEQRRLAL--------EKYLRKLGLHPVIGKSEELRVFLQVQ 206
Cdd:cd06892   75 reklqklgegegSMTKEEFekmkqeLEAEYLAIfkktvamhEVFLRRLASHPVLRNDANFRVFLEYE 141
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 91-204 1.78e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. 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. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 46.55  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  91 HISVSDPQEEQEvtnslvPGGSSYHTYLITTRtgkseyGV---RRRFREVVTLSERLSEVYRGYVIPVRPEKssverKV- 166
Cdd:cd06885    1 HFSIPDTQELSD------EGGSTYVAYNIHIN------GVlhcSVRYSQLHGLNEQLKKEFGNRKLPPFPPK-----KLl 63

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 357492829 167 -MQKEEfVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06885   64 pLTPAQ-LEERRLQLEKYLQAVVQDPRIANSDIFNSFLL 101
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
 93-203 8.10e-06

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: 45.43  E-value: 8.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  93 SVSDPQEEQEVTnslvpGGSSYHTY-LITTRTGKSeygVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKvmqKEE 171
Cdd:cd07286    4 TIDDPTKQTKFK-----GMKSYISYkLVPSHTGLQ---VHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRF---EED 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 357492829 172 FVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd07286   73 FISKRRKGLIWWMDHMCSHPVLARCDAFQHFL 104
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
 279-507 1.10e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 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. 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 effcient 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: 153348 [Multi-domain]  Cd Length: 234  Bit Score: 46.97  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTKFETEEAefesqRVRAadMKNVATAAVK 358
Cdd:cd07664   19 ESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTA-----LSRA--LSQLAEVEEK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYRELNTQTIKHLDKL-HEYLGTMLAINNAFADRSSALLTVQTLSSELASLHSRIEKLEVASsrifggdksRMRKIE 437
Cdd:cd07664   92 IDQLHQDQAFADFYLFSELlGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKREAEAKLQYAN---------KPDKLQ 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 438 ELKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:cd07664  163 QAKDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPE 232
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
 279-507 1.29e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; 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. 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 effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153349 [Multi-domain]  Cd Length: 234  Bit Score: 46.60  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 279 EEDKEFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTKFETEEAefesqRVRAadMKNVATAAVK 358
Cdd:cd07665   19 ESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSSEDNTA-----LSRA--LSQLAEVEEK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 359 ASRLYRE-LNTQTIKHLDKLHEYLGTMLAINNAFADRSSALLTVQTLSSELaslhsriEKLEVASSRIFGGDKSRmrKIE 437
Cdd:cd07665   92 IEQLHQEqANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAML-------QKKREAEARLLWANKPD--KLQ 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 438 ELKEAVRVTESAKICADREYERIKENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:cd07665  163 QAKDEIAEWESRVTQYERDFERISATVRKEVIRFEKEKSKDFKNHIIKYLETLLHSQQQLVKYWEAFLPE 232
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
 94-203 3.55e-05

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: 43.47  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  94 VSDPQEeqevtNSLVPGGSSYHTYLIT-TRTGKSeygVRRRFREVVTLSERLSEVYrGYVIPVR--PEKSSVERKvmqKE 170
Cdd:cd07285    5 VADPRK-----GSKMYGLKSYIEYQLTpTNTNRS---VNHRYKHFDWLYERLLVKF-GLAIPIPslPDKQVTGRF---EE 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 357492829 171 EFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd07285   73 EFIKMRMERLQAWMTRMCRHPVISESEVFQQFL 105
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
 92-203 8.29e-05

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: 42.27  E-value: 8.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQEEQEVTNSLVPGGSSYHT---YLITTRTGKSEYG---VRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERk 165
Cdd:cd06869    8 VAVRVTETAGRLSSKKAYFVNRSKHhyeFIIRVRREGEEYRtiyVARRYSDFKKLHHDLKKEFPGKKLPKLPHKDKLPR- 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 357492829 166 vmqkeefvEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06869   87 --------EKLRLSLRQYLRSLLKDPEVAHSSILQEFL 116
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 110-203 8.80e-05

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 42.04  E-value: 8.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 110 GGSSYHTYLITTRT-GKSEYGVRRRFREVVTLSERLSEVYRG--------YVIPVRPEKSSVERkvmqKEEFVEQRRLAL 180
Cdd:cd06882   16 GFTNYYVFVIEVKTkGGSKYLIYRRYRQFFALQSKLEERFGPeagssaydCTLPTLPGKIYVGR----KAEIAERRIPLL 91

                         90       100
                 ....*....|....*....|....
gi 357492829 181 EKYLRK-LGLHPVIGKSEELRVFL 203
Cdd:cd06882   92 NRYMKElLSLPVWVLMDEDVRLFF 115
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
 92-204 1.32e-04

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: 41.68  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  92 ISVSDPQeeqevtnSLVPGGSSYHTYLITTRTG-----KSEYGVRRRFREVVTLS---ERLSEVyrgyVIPVRPEKSSVE 163
Cdd:cd06894    4 IDVVNPQ-------THGVGKKRFTDYEVRMRTNlpvfkKKESSVRRRYSDFEWLRselERDSKI----VVPPLPGKALKR 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 357492829 164 RKVMQK------EEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd06894   73 QLPFRGddgifeEEFIEERRKGLETFINKVAGHPLAQNEKCLHMFLQ 119
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
 110-203 1.64e-04

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 40.97  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 110 GGSSYHTYLITTRTGKSE-YGVRRRFREVVTLSERLSEV--YRGYVIPVRPEKSSVErkvmqkEEFVEQRRLALEKYLRK 186
Cdd:cd06872   14 GSKSFAVYSVAVTDNENEtWVVKRRFRNFETLHRRLKEVpkYNLELPPKRFLSSSLD------GAFIEERCKLLDKYLKD 87

                         90
                 ....*....|....*..
gi 357492829 187 LGLHPVIGKSEELRVFL 203
Cdd:cd06872   88 LLVIEKVAESHEVWSFL 104
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
 90-204 2.57e-04

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: 40.75  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  90 IHISVSDPQeeqevtnSLVPGGSSYHTYLITTRTGK-----SEYGVRRRFREVVTLS---ERLSEVyrgyVIPVRPEKSS 161
Cdd:cd07293    2 LEIDVTNPQ-------TVGVGRGRFTTYEIRLKTNLpifklKESTVRRRYSDFEWLRselERESKV----VVPPLPGKAL 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 357492829 162 VERKVMQKEE------FVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd07293   71 FRQLPFRGDDgifddsFIEERKQGLEQFLNKVAGHPLAQNERCLHMFLQ 119
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 109-187 2.98e-04

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal 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. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 40.41  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 109 PGGSSYHTYLITTRTGKSEYGVRRRFREVVTLSERLSEVYrgyviPVR-----PEKSSVERKVMQkeeFVEQRRLALEKY 183
Cdd:cd07277   13 KGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKF-----PVVrsfdfPPKKAIGNKDAK---FVEERRKRLQVY 84


                 ....
gi 357492829 184 LRKL 187
Cdd:cd07277   85 LRRV 88
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
 87-204 3.10e-04

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: 40.79  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  87 SDSIHISVSDPQeeqevtnSLVPGGSSYHTYLITTRTGK-----SEYGVRRRFREVVTLSERLsEVYRGYVIPVRPEKSs 161
Cdd:cd07294    1 SNFLEIDIFNPQ-------TVGVGRNRFTTYEVRMRTNLpifklKESCVRRRYSDFEWLKNEL-ERDSKIVVPPLPGKA- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 357492829 162 VERKV-------MQKEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFLQ 204
Cdd:cd07294   72 LKRQLpfrgdegIFEESFIEERRQGLEQFINKIAGHPLAQNERCLHMFLQ 121
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 130-203 4.42e-04

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: 40.05  E-value: 4.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357492829 130 VRRRFREVVTLSERLSE---VYRGYVIPVRpeKSSVERKvmqkEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06877   46 VLRRYNEFYVLESKLTEfhgEFPDAPLPSR--RIFGPKS----YEFLESKREIFEEFLQKLLQKPELRGSELLYDFL 116
BAR_SNX7_30 cd07624
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ...
 283-507 5.81e-04

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: 41.21  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 283 EFMEKKDKLMEFEQQLSNVSQQAESLVKFQQDMGETMGELGLAFVKLTKFETEEAEFesqrvraadMKNVATAAVKASRL 362
Cdd:cd07624   15 EFDKMNEYLTLFGEKLGTIERISQRIHKERIEYFDELKEYSPIFQLWSASETELAPL---------LEGVSSAVERCTAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 363 YREL-NTQTIKHLDKLHEYLGTMLAINNAFADRSSalltVQtlsselASLHSRIEKLEvassrifggdksrmRKIEELKE 441
Cdd:cd07624   86 LEVLlSDHEFVFLPPLREYLLYSDAVKDVLKRRDQ----FQ------IEYELSVEELN--------------KKRLELLK 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357492829 442 AVRVTESAKICADreyerikENNRSELERIDKERQSDFQNMLRGFVVNQAGYAEKMAAVWEKLAEE 507
Cdd:cd07624  142 EVEKLQDKLECAN-------ADLKADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEEVLPA 200
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
 99-203 8.74e-04

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: 39.32  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829  99 EEQEVTNSLVPGGSSYHTYLIT------TRTGKSEYGVR----RRFREVVTLSERLSEVYRGYVIPVRPEKssverKVMQ 168
Cdd:cd06868    8 EYQEIRGKTSSGHVLYQIVVVTrlaafkSAKHKEEDVVQfmvsKKYSEFEELYKKLSEKYPGTILPPLPRK-----ALFV 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 357492829 169 KEEFVEQRRLALEKYLRKLGLHPVIGKSEELRVFL 203
Cdd:cd06868   83 SESDIRERRAAFNDFMRFISKDEKLANCPELLEFL 117
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
 100-207 4.64e-03

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: 37.09  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 100 EQEVTNSLV--PGGSSYHTYLITTRTG-----KSEYGVRRRFREVVTLSERLSEVYRGYVIPVRPEKSSVERKvmqKEEF 172
Cdd:cd07295    3 EIEVRNPKThgIGRGMFTDYEIVCRTNipafkLRVSSVRRRYSDFEYFRDILERESPRVMIPPLPGKIFTNRF---SDEV 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 357492829 173 VEQRRLALEKYLRKLGLHPVIGK-SEELRVFLQVQG 207
Cdd:cd07295   80 IEERRQGLETFLQSVAGHPLLQTgSKVLAAFLQDPK 115
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 113-203 5.45e-03

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: 36.87  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357492829 113 SYHTYLITTRTGKSEYGVRRRFREVVTLSERLseVYRGYVipvrpEKSSVERKVM---QKEEFVEQRRLALEKYLRKL-G 188
Cdd:cd06875   16 GYTVYIIEVKVGSVEWTVKHRYSDFAELHDKL--VAEHKV-----DKDLLPPKKLignKSPSFVEKRRKELEIYLQTLlS 88

                         90
                 ....*....|....*
gi 357492829 189 LHPViGKSEELRVFL 203
Cdd:cd06875   89 FFQK-TMPRELAHFL 102
 
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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