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Conserved domains on  [gi|661417113|gb|AIE13278|]
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SH3 and PX3 domain-containing 3-like protein, partial [Planiliza abu]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 36833)

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
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 18-142 6.07e-74

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 cd07286:

Pssm-ID: 470617  Cd Length: 127  Bit Score: 220.31  E-value: 6.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKFKGIKTYISYRVTPTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRR 97
Cdd:cd07286    1 FQCTIDDPTKQTKFKGMKSYISYKLVPSHTGLQVHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRFEEDFISKRRKG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 661417113  98 LILWMNHMTSHPVLSQYEGFEHFLMC--ADDKQWKLGKRRAEKDEMV 142
Cdd:cd07286   81 LIWWMDHMCSHPVLARCDAFQHFLTCpsTDEKAWKQGKRKAEKDEMV 127
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 125-233 2.73e-50

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


The actual alignment was detected with superfamily member pfam10456:

Pssm-ID: 472257  Cd Length: 236  Bit Score: 163.80  E-value: 2.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  125 DDKQWKLGKRRAEKDEMVGAHFMLTLQIPNEHQDLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQR 204
Cdd:pfam10456   1 DEKEWKTGKRKAEKDELVGAMFFLTIEIPEPPLDLQEVEQKVEGFKRFTKKMDDSVKQLLTVGNEFWKKCTGPFKKEYQK 80

                          90       100
                  ....*....|....*....|....*....
gi 661417113  205 LGNAFQSISQAFMLDPPHRSDTLNNAISH 233
Cdd:pfam10456  81 IGSAFQLLSQVFEMDGYVGSSALNEAIAH 109
 
Name Accession Description Interval E-value
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
 18-142 6.07e-74

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: 220.31  E-value: 6.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKFKGIKTYISYRVTPTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRR 97
Cdd:cd07286    1 FQCTIDDPTKQTKFKGMKSYISYKLVPSHTGLQVHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRFEEDFISKRRKG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 661417113  98 LILWMNHMTSHPVLSQYEGFEHFLMC--ADDKQWKLGKRRAEKDEMV 142
Cdd:cd07286   81 LIWWMDHMCSHPVLARCDAFQHFLTCpsTDEKAWKQGKRKAEKDEMV 127
BAR_3_WASP_bdg pfam10456
WASP-binding domain of Sorting nexin protein; The C-terminal region of the Sorting nexin group ...
 125-233 2.73e-50

WASP-binding domain of Sorting nexin protein; The C-terminal region of the Sorting nexin group of proteins appears to carry a BAR-like (Bin/amphiphysin/Rvs) domain. This domain is very diverse and the similarities with other BAR domains are few. In the Sorting nexins it is associated with family PX, pfam00787.13, and in combination with PX appears to be necessary to bind WASP along with p85 to form a multimeric signalling complex.


Pssm-ID: 313646  Cd Length: 236  Bit Score: 163.80  E-value: 2.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  125 DDKQWKLGKRRAEKDEMVGAHFMLTLQIPNEHQDLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQR 204
Cdd:pfam10456   1 DEKEWKTGKRKAEKDELVGAMFFLTIEIPEPPLDLQEVEQKVEGFKRFTKKMDDSVKQLLTVGNEFWKKCTGPFKKEYQK 80

                          90       100
                  ....*....|....*....|....*....
gi 661417113  205 LGNAFQSISQAFMLDPPHRSDTLNNAISH 233
Cdd:pfam10456  81 IGSAFQLLSQVFEMDGYVGSSALNEAIAH 109
BAR_SNX33 cd07669
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 33; BAR domains are dimerization, lipid ...
 153-233 5.34e-47

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 33; 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. SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153353  Cd Length: 207  Bit Score: 154.36  E-value: 5.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113 153 PNEHQDLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQRLGNAFQSISQAFMLDPPHRSDTLNNAIS 232
Cdd:cd07669    1 PTEHQDLQDVEERVDVFKAFSKKMDDSVLQLSNVASELVRKHLGGFRKEFQKLGNAFQAISHSFQLDPPYSSEALNNAIS 80


                 .
gi 661417113 233 H 233
Cdd:cd07669   81 H 81
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 51-121 2.41e-19

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 79.21  E-value: 2.41e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661417113   51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:pfam00787  11 VRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 28-113 1.26e-13

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: 64.67  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113    28 QTKFKGIKTYISYRVTPTHIGRP--VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGR---FEEDFIEKRKRRLILWM 102
Cdd:smart00312   5 EKIGDGKHYYYVIEIETKTGLEEwtVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRlnnFSEEFIEKRRRGLEKYL 84

                           90
                   ....*....|.
gi 661417113   103 NHMTSHPVLSQ 113
Cdd:smart00312  85 QSLLNHPELIN 95
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 51-114 1.37e-10

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 60.58  E-value: 1.37e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQ-----ATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQY 114
Cdd:COG5391  175 VRRRYSDFESLHSILIKLLPLCAIPPLPSKKsnseyYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNY 243
 
Name Accession Description Interval E-value
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
 18-142 6.07e-74

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: 220.31  E-value: 6.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKFKGIKTYISYRVTPTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRR 97
Cdd:cd07286    1 FQCTIDDPTKQTKFKGMKSYISYKLVPSHTGLQVHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRFEEDFISKRRKG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 661417113  98 LILWMNHMTSHPVLSQYEGFEHFLMC--ADDKQWKLGKRRAEKDEMV 142
Cdd:cd07286   81 LIWWMDHMCSHPVLARCDAFQHFLTCpsTDEKAWKQGKRKAEKDEMV 127
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 18-142 5.43e-70

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: 210.25  E-value: 5.43e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKFKGIKTYISYRVTPTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRR 97
Cdd:cd06862    1 YHCTVTNPKKESKFKGLKSFIAYQITPTHTNVTVSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGRFEEDFIEKRRER 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 661417113  98 LILWMNHMTSHPVLSQYEGFEHFLMCADDKQWKLGKRRAEKDEMV 142
Cdd:cd06862   81 LELWMNRLARHPVLSQSEVFRHFLTCTDEKDWKSGKRKAEKDELV 125
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
 18-142 1.35e-50

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: 160.96  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKFKGIKTYISYRVTPTHIGRPVYRRYKHFDWLYNRLLHKF-TVISVPHLPEKQATGRFEEDFIEKRKR 96
Cdd:cd07285    1 FDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFgLAIPIPSLPDKQVTGRFEEEFIKMRME 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 661417113  97 RLILWMNHMTSHPVLSQYEGFEHFLMCADDKQWKLGKRRAEKDEMV 142
Cdd:cd07285   81 RLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAEKDETV 126
BAR_3_WASP_bdg pfam10456
WASP-binding domain of Sorting nexin protein; The C-terminal region of the Sorting nexin group ...
 125-233 2.73e-50

WASP-binding domain of Sorting nexin protein; The C-terminal region of the Sorting nexin group of proteins appears to carry a BAR-like (Bin/amphiphysin/Rvs) domain. This domain is very diverse and the similarities with other BAR domains are few. In the Sorting nexins it is associated with family PX, pfam00787.13, and in combination with PX appears to be necessary to bind WASP along with p85 to form a multimeric signalling complex.


Pssm-ID: 313646  Cd Length: 236  Bit Score: 163.80  E-value: 2.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  125 DDKQWKLGKRRAEKDEMVGAHFMLTLQIPNEHQDLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQR 204
Cdd:pfam10456   1 DEKEWKTGKRKAEKDELVGAMFFLTIEIPEPPLDLQEVEQKVEGFKRFTKKMDDSVKQLLTVGNEFWKKCTGPFKKEYQK 80

                          90       100
                  ....*....|....*....|....*....
gi 661417113  205 LGNAFQSISQAFMLDPPHRSDTLNNAISH 233
Cdd:pfam10456  81 IGSAFQLLSQVFEMDGYVGSSALNEAIAH 109
BAR_SNX33 cd07669
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 33; BAR domains are dimerization, lipid ...
 153-233 5.34e-47

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 33; 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. SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153353  Cd Length: 207  Bit Score: 154.36  E-value: 5.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113 153 PNEHQDLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQRLGNAFQSISQAFMLDPPHRSDTLNNAIS 232
Cdd:cd07669    1 PTEHQDLQDVEERVDVFKAFSKKMDDSVLQLSNVASELVRKHLGGFRKEFQKLGNAFQAISHSFQLDPPYSSEALNNAIS 80


                 .
gi 661417113 233 H 233
Cdd:cd07669   81 H 81
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 18-121 2.45e-24

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: 93.03  E-value: 2.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKfkGIKTYISYRV---TPTHIGRP----VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEE-- 88
Cdd:cd06859    1 FEISVTDPVKVGD--GMSAYVVYRVttkTNLPDFKKsefsVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKVkf 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 661417113  89 DFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06859   79 EFIEKRRAALERFLRRIAAHPVLRKDPDFRLFL 111
BAR_SNX18 cd07670
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 18; BAR domains are dimerization, lipid ...
 158-232 4.44e-24

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 18; 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. SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153354  Cd Length: 207  Bit Score: 95.39  E-value: 4.44e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 661417113 158 DLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQRLGNAFQSISQAFMLDPPHRSDTLNNAIS 232
Cdd:cd07670    6 DLQDVESRIDGFKAFTKKMDESVLQLNHTANEFARKQVTGFKKEYQKVGQSFKGLSQAFELDQQAFSAGLNQAIA 80
BAR_SNX9_like cd07626
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9 and Similar Proteins; BAR domains are ...
 161-233 5.11e-22

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9 and Similar Proteins; 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 SNX9, SNX18, SNX33, and similar proteins. 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. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153310  Cd Length: 199  Bit Score: 89.63  E-value: 5.11e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 661417113 161 DVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQRLGNAFQSISQAFMLDPPHRSDTLNNAISH 233
Cdd:cd07626    1 DVEQQVDAFKKFVKSMDDSVKNLINIAQEQAKKHQGPYKKEYQKIGQAFTSLGTAFELDETPTSVPLTQAIKH 73
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 19-121 4.74e-21

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: 84.33  E-value: 4.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  19 TCSIEDPtkQTKFKGIKTYISYRVTPTHIGRP---VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRK 95
Cdd:cd06093    1 SVSIPDY--EKVKDGGKKYVVYIIEVTTQGGEewtVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERR 78

                         90       100
                 ....*....|....*....|....*.
gi 661417113  96 RRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06093   79 KQLEQYLQSLLNHPELRNSEELKEFL 104
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 51-121 2.41e-19

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 79.21  E-value: 2.41e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661417113   51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:pfam00787  11 VRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 18-121 4.52e-18

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: 76.62  E-value: 4.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKFkgIKTYISYRV---TPTHIGRP----VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDF 90
Cdd:cd06861    1 FEITVGDPHKVGDL--TSAHTVYTVrtrTTSPNFEVssfsVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRFDDNF 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 661417113  91 IEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06861   79 VEQRRAALEKMLRKIANHPVLQKDPDFRLFL 109
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 18-121 6.26e-16

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: 71.16  E-value: 6.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  18 FTCSIEDPTKQTKfKGIKTYISYRVTpTHIGRP--------VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQ-----ATG 84
Cdd:cd06863    1 LECLVSDPQKELD-GSSDTYISYLIT-TKTNLPsfsrkefkVRRRYSDFVFLHECLSNDFPACVVPPLPDKHrleyiTGD 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 661417113  85 RFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06863   79 RFSPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFL 115
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 21-121 3.40e-15

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: 69.29  E-value: 3.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  21 SIEDPTKQtkFKGIKTYISYRVTpTHIGRP--------VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQAT----GRFEE 88
Cdd:cd06860    4 TVDNPEKH--VTTLETYITYRVT-TKTTRSefdsseysVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVkgllDRFSP 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 661417113  89 DFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06860   81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFL 113
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 37-121 6.08e-15

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: 68.41  E-value: 6.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  37 YISYRVTPTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEG 116
Cdd:cd06866   18 HVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLNLVARHPVLSEDEL 97


                 ....*
gi 661417113 117 FEHFL 121
Cdd:cd06866   98 VRTFL 102
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 28-113 1.26e-13

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: 64.67  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113    28 QTKFKGIKTYISYRVTPTHIGRP--VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGR---FEEDFIEKRKRRLILWM 102
Cdd:smart00312   5 EKIGDGKHYYYVIEIETKTGLEEwtVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRlnnFSEEFIEKRRRGLEKYL 84

                           90
                   ....*....|.
gi 661417113   103 NHMTSHPVLSQ 113
Cdd:smart00312  85 QSLLNHPELIN 95
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 21-124 1.41e-13

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: 65.00  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  21 SIEDPtkQTKFKGIKTYISYRV-TPTHIGR------PVYRRYKHFDWLYNRLLHKFTVISVPHLPEK----QATGRFEED 89
Cdd:cd07284    4 TVDEP--ESHVTAIETFITYRVmTKTSRSEfdssefEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKfvmkGMVERFNED 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 661417113  90 FIEKRKRRLILWMNHMTSHPVLSQYEGFEHFLMCA 124
Cdd:cd07284   82 FIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 21-121 8.16e-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: 62.80  E-value: 8.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  21 SIEDPTKQTKfkGIKTYISYRV----TPTHIGRPVY---RRYKHFDWLYNRLLHKFTVISVPHLPEK----QATGRFEED 89
Cdd:cd07283    4 TVDDPKKHVC--TMETYITYRVttktTRTEFDLPEYsvrRRYQDFDWLRNKLEESQPTHLIPPLPEKfvvkGVVDRFSEE 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 661417113  90 FIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd07283   82 FVETRRKALDKFLKRIADHPVLSFNEHFNVFL 113
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 51-121 2.88e-12

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: 61.62  E-value: 2.88e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQA--------TGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06864   48 LWRRYSEFELLRNYLVVTYPYVIVPPLPEKRAmfmwqklsSDTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFL 126
BAR_SNX9 cd07668
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9; BAR domains are dimerization, lipid ...
 158-232 3.40e-11

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9; 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. 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 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. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153352  Cd Length: 210  Bit Score: 60.42  E-value: 3.40e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 661417113 158 DLQDVEERVDNFKSFAKKMDDSVMQLTHVASELVRKHLGGFRKEFQRLGNAFQSISQAFMLDPPHRSDTLNNAIS 232
Cdd:cd07668    6 DLVEIEQKCEAVGRFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSTSGYQGETDLNDAIT 80
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 51-114 1.37e-10

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 60.58  E-value: 1.37e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQ-----ATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQY 114
Cdd:COG5391  175 VRRRYSDFESLHSILIKLLPLCAIPPLPSKKsnseyYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNY 243
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
 51-126 4.90e-09

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: 52.85  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  51 VYRRYKHFDWLYNRLlHKFTVISVPHLPEK---------QATGRFEEDFIEKRKRRLILWMNHMTSHPvLSQYEGFEHFL 121
Cdd:cd06894   40 VRRRYSDFEWLRSEL-ERDSKIVVPPLPGKalkrqlpfrGDDGIFEEEFIEERRKGLETFINKVAGHP-LAQNEKCLHMF 117


                 ....*
gi 661417113 122 MCADD 126
Cdd:cd06894  118 LQEET 122
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 32-122 1.90e-08

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: 51.17  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  32 KGIKTYISYRVTPT---HIGRPV--YRRYKHFDWLYNRLLHKF---TVISVPHLPEK----QATGRFEEDFIEKRKRRLI 99
Cdd:cd07280   17 TGGGAYVVWKITIEtkdLIGSSIvaYKRYSEFVQLREALLDEFprhKRNEIPQLPPKvpwyDSRVNLNKAWLEKRRRGLQ 96

                         90       100
                 ....*....|....*....|...
gi 661417113 100 LWMNHMTSHPVLSQYEGFEHFLM 122
Cdd:cd07280   97 YFLNCVLLNPVFGGSPVVKEFLL 119
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 51-121 3.33e-08

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


Pssm-ID: 132781  Cd Length: 120  Bit Score: 50.44  E-value: 3.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661417113  51 VYRRYKHFDWLYNRLlhKFTVISVPhLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06871   40 VIRRYNDFDLLNASL--QISGISLP-LPPKKLIGNMDREFIAERQQGLQNYLNVILMNPILASCLPVKKFL 107
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 24-121 3.39e-08

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: 50.50  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  24 DPTKQ----TKFKGIKTYISYRVT-------PTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEK---QATGRFEED 89
Cdd:cd06865    6 DPKKEqepsRVPLGGPPYISYKVTtrtnipsYTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKsvvESQVMQSAE 85

                         90       100       110
                 ....*....|....*....|....*....|..
gi 661417113  90 FIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06865   86 FIEQRRVALEKYLNRLAAHPVIGLSDELRVFL 117
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
 51-111 1.05e-07

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: 49.03  E-value: 1.05e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVL 111
Cdd:cd07295   40 VRRRYSDFEYFRDILERESPRVMIPPLPGKIFTNRFSDEVIEERRQGLETFLQSVAGHPLL 100
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 26-121 1.53e-07

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: 48.40  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  26 TKQTKFKGIKTYISYrvTPTHIGRPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRF---------EEDFIEKRKR 96
Cdd:cd06867    7 AGKSSEGGSGSYIVY--VIRLGGSEVKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSLKDYakkpskaknDAKIIERRKR 84

                         90       100
                 ....*....|....*....|....*
gi 661417113  97 RLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06867   85 MLQRFLNRCLQHPILRNDIVFQKFL 109
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
 51-121 2.69e-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: 47.71  E-value: 2.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFE-EDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd06898   39 VRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRFNnEGFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFL 110
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 33-121 9.00e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 46.17  E-value: 9.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  33 GIKTYISYRVTPTHIGRP------VYRRYKHFDWLYNRLLHKFtvisvPHL------PEKQATGRFEEDFIEKRKRRLIL 100
Cdd:cd07279   14 GEKKYVVYQLAVVQTGDPdtqpafIERRYSDFLKLYKALRKQH-----PQLmakvsfPRKVLMGNFSSELIAERSRAFEQ 88

                         90       100
                 ....*....|....*....|.
gi 661417113 101 WMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd07279   89 FLGHILSIPNLRDSKAFLDFL 109
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 21-121 1.52e-06

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: 45.82  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  21 SIEDPTKQTKfkGIKTYISYRVTP----THIGRP---VYRRYKHFDWLYNRLLHKFTVIS--VPHLPEKQATGRFE---- 87
Cdd:cd07282    4 GVSDPEKVGD--GMNAYMAYRVTTktslSMFSRSefsVRRRFSDFLGLHSKLASKYLHVGyiVPPAPEKSIVGMTKvkvg 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 661417113  88 -ED-----FIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd07282   82 kEDsssteFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 121
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 35-122 2.44e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 45.34  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  35 KTYISYRVTPTHIGRP-------VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMNHMTS 107
Cdd:cd06873   20 KTYAVYAISVTRIYPNgqeeswhVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYLQSLLN 99

                         90
                 ....*....|....*
gi 661417113 108 HPVLSQYEGFEHFLM 122
Cdd:cd06873  100 PEVLDANPGLQEIVL 114
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 51-105 3.12e-06

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: 45.03  E-value: 3.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMNHM 105
Cdd:cd07277   34 VYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKRLQVYLRRV 88
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
 51-122 4.68e-06

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: 44.65  E-value: 4.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVP--------HLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPvLSQYEGFEHFLM 122
Cdd:cd07294   42 VRRRYSDFEWLKNELERDSKIVVPPlpgkalkrQLPFRGDEGIFEESFIEERRQGLEQFINKIAGHP-LAQNERCLHMFL 120
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
 51-122 5.96e-06

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: 44.21  E-value: 5.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVISVP--------HLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPvLSQYEGFEHFLM 122
Cdd:cd07293   40 VRRRYSDFEWLRSELERESKVVVPPlpgkalfrQLPFRGDDGIFDDSFIEERKQGLEQFLNKVAGHP-LAQNERCLHMFL 118
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 19-121 8.75e-06

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: 43.89  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  19 TCSIEDPTKQTKfkGIKTYISYRVTpTHIGRPVY--------RRYKHFDWLYNRLLHKFTV--ISVPHLPEKQATGRFE- 87
Cdd:cd07281    2 KVSITDPEKIGD--GMNAYVVYKVT-TQTSLLMFrskhftvkRRFSDFLGLYEKLSEKHSQngFIVPPPPEKSLIGMTKv 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 661417113  88 ----ED-----FIEKRKRRLILWMNHMTSHPVLSQYEGFEHFL 121
Cdd:cd07281   79 kvgkEDsssaeFLERRRAALERYLQRIVSHPSLLQDPDVREFL 121
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 20-122 7.28e-05

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


Pssm-ID: 132780  Cd Length: 109  Bit Score: 40.85  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661417113  20 CSIEDPTKQTKFKGIKTYISYRVTPTHigrpVYRRYKHFDWLYNRLLHKFTVISVpHLPEKQATGR-FEEDFIEKRKRRL 98
Cdd:cd06870    9 SSDEDREKKKRFTVYKVVVSVGRSSWF----VFRRYAEFDKLYESLKKQFPASNL-KIPGKRLFGNnFDPDFIKQRRAGL 83

                         90       100
                 ....*....|....*....|....
gi 661417113  99 ILWMNHMTSHPVLSQYEGFEHFLM 122
Cdd:cd06870   84 DEFIQRLVSDPKLLNHPDVRAFLQ 107
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
 51-122 1.67e-04

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


Pssm-ID: 132791  Cd Length: 117  Bit Score: 40.00  E-value: 1.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 661417113  51 VYRRYKHFDWLYNRLLHKFTVI----SVPHLPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFLM 122
Cdd:cd06881   40 VWKRYSDFKKLHRELSRLHKQLylsgSFPPFPKGKYFGRFDAAVIEERRQAILELLDFVGNHPALYQSSAFQQFFE 115
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 51-125 1.22e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 37.39  E-value: 1.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 661417113  51 VYRRYKHFDWLYNRLLHKFT--VISVPhlPEKQATGRFEEDFIEKRKRRLILWMNHMTSHPVLSQYEGFEHFLmCAD 125
Cdd:cd07276   37 VFRRYTDFVRLNDKLKQMFPgfRLSLP--PKRWFKDNFDPDFLEERQLGLQAFVNNIMAHKDIAKCKLVREFF-CLD 110
 
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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