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Conserved domains on  [gi|386781089|ref|NP_001247826|]
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sorting nexin-2 [Macaca mulatta]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10508661)

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; also contains a sorting nexin N-terminal domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
283-516 1.75e-163

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: 462.60  E-value: 1.75e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 283 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 362
Cdd:cd07664    1 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 363 ALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDK 442
Cdd:cd07664   81 ALSQLAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKREAEAKLQYANKPDK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 443 IQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 516
Cdd:cd07664  161 LQQAKDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 234
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
142-265 6.86e-93

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: 278.48  E-value: 6.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 221
Cdd:cd07282    1 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd07282   81 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 124
Sorting_nexin pfam03700
Sorting nexin, N-terminal domain; These proteins bins to the cytoplasmic domain of plasma ...
3-75 2.33e-19

Sorting nexin, N-terminal domain; These proteins bins to the cytoplasmic domain of plasma membrane receptors. and are involved in endocytic protein trafficking. The N-terminal domain appears to be specific to sorting nexins 1 and 2.


:

Pssm-ID: 461016  Cd Length: 75  Bit Score: 82.27  E-value: 2.33e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089    3 AEREPPPLGDGKPTDFEDLE------DGEDLFTSTVSTlessPSSPEPASLPAEDISANSNGPKPTEVGLDDDREDLFA 75
Cdd:pfam03700   1 SEREPPPFPDSEDPEPEDAAgdgdsdEGEDIFTGTVST----LGSSPSSPEPASLPFTNSNGPKTNGVHSDDDQQDLFA 75
 
Name Accession Description Interval E-value
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
283-516 1.75e-163

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: 462.60  E-value: 1.75e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 283 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 362
Cdd:cd07664    1 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 363 ALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDK 442
Cdd:cd07664   81 ALSQLAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKREAEAKLQYANKPDK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 443 IQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 516
Cdd:cd07664  161 LQQAKDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 234
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
281-514 4.00e-106

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: 316.53  E-value: 4.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  281 ILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTAL 360
Cdd:pfam09325   1 LSSLFGKFFSSVSKSSYKFNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  361 SRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANK- 439
Cdd:pfam09325  81 SRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLLRANKs 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386781089  440 -PDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPE 514
Cdd:pfam09325 161 qNDKLQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQKELIELWETFLPE 236
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
142-265 6.86e-93

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: 278.48  E-value: 6.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 221
Cdd:cd07282    1 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd07282   81 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 124
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
146-263 2.78e-28

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: 108.20  E-value: 2.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089   146 VSDPEKVGDGMNAYMAYRVTTKTSLSMFSksefsVKRRFSDFLGLHSKLasKYLHVGYIVPPAPEKsivgmtkVKVGKED 225
Cdd:smart00312   1 VVEPEKIGDGKHYYYVIEIETKTGLEEWT-----VSRRYSDFLELHSKL--KKHFPRSILPPLPGK-------KLFGRLN 66
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 386781089   226 SSSTEFVEKRRAALERYLQRTVKHPTLLQ-DPDLRQFLE 263
Cdd:smart00312  67 NFSEEFIEKRRRGLEKYLQSLLNHPELINhSEVVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
170-265 3.44e-24

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 96.16  E-value: 3.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  170 LSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVgyIVPPAPEKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQRTVKH 249
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSV--IIPPLPPKRWLG----------RYNEEFIEKRRKGLEQYLQRLLQH 68
                          90
                  ....*....|....*.
gi 386781089  250 PTLLQDPDLRQFLESS 265
Cdd:pfam00787  69 PELRNSEVLLEFLESD 84
Sorting_nexin pfam03700
Sorting nexin, N-terminal domain; These proteins bins to the cytoplasmic domain of plasma ...
3-75 2.33e-19

Sorting nexin, N-terminal domain; These proteins bins to the cytoplasmic domain of plasma membrane receptors. and are involved in endocytic protein trafficking. The N-terminal domain appears to be specific to sorting nexins 1 and 2.


Pssm-ID: 461016  Cd Length: 75  Bit Score: 82.27  E-value: 2.33e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089    3 AEREPPPLGDGKPTDFEDLE------DGEDLFTSTVSTlessPSSPEPASLPAEDISANSNGPKPTEVGLDDDREDLFA 75
Cdd:pfam03700   1 SEREPPPFPDSEDPEPEDAAgdgdsdEGEDIFTGTVST----LGSSPSSPEPASLPFTNSNGPKTNGVHSDDDQQDLFA 75
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
141-509 1.43e-18

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 88.70  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 141 DIEIGVSDPEKVGDGM---NAYMAYRVTTKTSLSMFSKSEF---SVKRRFSDFLGLHSKLASKYLhvGYIVPPAPEKSIV 214
Cdd:COG5391  130 FISSTVSNPQSLTLLVdsrDKHTSYEIITVTNLPSFQLRESrplVVRRRYSDFESLHSILIKLLP--LCAIPPLPSKKSN 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 215 GMTkvkvgKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDP----------DLRQFLE------SSELPRAVNTQALSG 278
Cdd:COG5391  208 SEY-----YGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNYKnsksweshstLLSSFIEnrksvpTPLSLDLTSTTQELD 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 279 AGILRMVNKAADAVNKMTIKMNEsdawFEEKQQQFENLDQQL-RKLHASVEALVCHRKELSANTAAFAK---SAAMLGNS 354
Cdd:COG5391  283 MERKELNESTSKAIHNILSIFSL----FEKILIQLESEEESLtRLLESLNNLLLLVLNFSGVFAKRLEQnqnSILNEGVV 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 355 EDHTALS---RALSQLAEVEEKIDQL-----HQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITL-L 425
Cdd:COG5391  359 QAETLRSslkELLTQLQDEIKSRESLiltdsNLEKLTDQNLEDVEELSRSLRKNSSQRAVVSQQPEGLTSFSKLSYKLrD 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 426 KKREAEAKmmvaNKPDKIQQAKNEIREweaKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLI 505
Cdd:COG5391  439 FVQEKSRS----KSIESLQQDKEKLEE---QLAIAEKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENL 511

                 ....
gi 386781089 506 KYWE 509
Cdd:COG5391  512 EIWK 515
 
Name Accession Description Interval E-value
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
283-516 1.75e-163

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: 462.60  E-value: 1.75e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 283 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 362
Cdd:cd07664    1 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 363 ALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDK 442
Cdd:cd07664   81 ALSQLAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKREAEAKLQYANKPDK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 443 IQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 516
Cdd:cd07664  161 LQQAKDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 234
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
293-516 7.01e-135

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: 389.71  E-value: 7.01e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 293 NKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEE 372
Cdd:cd07623    1 SKITIKMDETDQWFEEKQQQIENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLSNCEEHTSLSRALSQLAEVEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 373 KIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDKIQQAKNEIRE 452
Cdd:cd07623   81 KIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKREAKAKLELSGRTDKLDQAQQEIKE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 453 WEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 516
Cdd:cd07623  161 WEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQQLIKYWEAFLPEAK 224
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
283-516 2.61e-128

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: 373.25  E-value: 2.61e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 283 RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSR 362
Cdd:cd07665    1 KMFNKATDAVSKMTIKMNESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSSEDNTALSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 363 ALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDK 442
Cdd:cd07665   81 ALSQLAEVEEKIEQLHQEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAMLQKKREAEARLLWANKPDK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 443 IQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAK 516
Cdd:cd07665  161 LQQAKDEIAEWESRVTQYERDFERISATVRKEVIRFEKEKSKDFKNHIIKYLETLLHSQQQLVKYWEAFLPEAK 234
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
281-514 4.00e-106

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: 316.53  E-value: 4.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  281 ILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTAL 360
Cdd:pfam09325   1 LSSLFGKFFSSVSKSSYKFNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  361 SRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANK- 439
Cdd:pfam09325  81 SRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLLRANKs 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386781089  440 -PDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPE 514
Cdd:pfam09325 161 qNDKLQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQKELIELWETFLPE 236
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
142-265 6.86e-93

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: 278.48  E-value: 6.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 221
Cdd:cd07282    1 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd07282   81 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 124
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
142-263 1.68e-68

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: 215.69  E-value: 1.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 221
Cdd:cd07281    1 LKVSITDPEKIGDGMNAYVVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd07281   81 GKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLE 122
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
142-265 8.36e-63

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: 200.50  E-value: 8.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLhvGYIVPPAPEKSIVGMTKVKV 221
Cdd:cd06859    1 FEISVTDPVKVGDGMSAYVVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVEKYP--GRIVPPPPEKQAVGRFKVKF 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 222 gkedssstEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd06859   79 --------EFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLESD 114
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
301-514 2.65e-49

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: 169.07  E-value: 2.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 301 ESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDH--TALSRALSQLAEVEEKIDQLH 378
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEvgGELGEALSKLGKAAEELSSLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 379 QEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVAN--KPDKIQQAKNEIREWEAK 456
Cdd:cd07596   81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPgiKPAKVEELEEELEEAESA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386781089 457 VQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPE 514
Cdd:cd07596  161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
301-512 1.33e-47

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: 164.40  E-value: 1.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 301 ESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEEKIDQLHQE 380
Cdd:cd07627    1 EPDEWFIEKKQYLDSLESQLKQLYKSLELVSSQRKELASATEEFAETLEALSSLELSKSLSDLLAALAEVQKRIKESLER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 381 QAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANK--PDKIQQAKNEIREWEAKVQ 458
Cdd:cd07627   81 QALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQLEKLKRQGKtqQEKLNSLLSELEEAERRAS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 386781089 459 QGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFL 512
Cdd:cd07627  161 ELKKEFEEVSELIKSELERFERERVEDFRNSVEIYLESAIESQKELIELWETFY 214
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
143-265 6.21e-37

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: 132.09  E-value: 6.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 143 EIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylHVGYIVPPAPEKSIVGmtkvkvg 222
Cdd:cd06861    2 EITVGDPHKVGDLTSAHTVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNN--HPGVIVPPPPEKQSVG------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 386781089 223 kedSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd06861   73 ---RFDDNFVEQRRAALEKMLRKIANHPVLQKDPDFRLFLESE 112
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
144-262 1.44e-31

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: 117.82  E-value: 1.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 144 IGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylHVGYIVPPAPEKSIVgmtkvkVGK 223
Cdd:cd06860    3 ITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEES--HPTHIIPPLPEKHSV------KGL 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 386781089 224 EDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd06860   75 LDRFSPEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFL 113
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
142-265 9.74e-30

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: 112.77  E-value: 9.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEK-VGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYlhVGYIVPPAPEKSivgmtKVK 220
Cdd:cd06863    1 LECLVSDPQKeLDGSSDTYISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSNDF--PACVVPPLPDKH-----RLE 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 386781089 221 VGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd06863   74 YITGDRFSPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLESS 118
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
146-263 2.78e-28

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: 108.20  E-value: 2.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089   146 VSDPEKVGDGMNAYMAYRVTTKTSLSMFSksefsVKRRFSDFLGLHSKLasKYLHVGYIVPPAPEKsivgmtkVKVGKED 225
Cdd:smart00312   1 VVEPEKIGDGKHYYYVIEIETKTGLEEWT-----VSRRYSDFLELHSKL--KKHFPRSILPPLPGK-------KLFGRLN 66
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 386781089   226 SSSTEFVEKRRAALERYLQRTVKHPTLLQ-DPDLRQFLE 263
Cdd:smart00312  67 NFSEEFIEKRRRGLEKYLQSLLNHPELINhSEVVLEFLE 105
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
144-264 6.19e-26

The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 102.11  E-value: 6.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 144 IGVSDPEKVGD------GMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASkyLHVGYIVPPAPEKSIVGMT 217
Cdd:cd06865    2 ITVSDPKKEQEpsrvplGGPPYISYKVTTRTNIPSYTHGEFTVRRRFRDVVALADRLAE--AYRGAFVPPRPDKSVVESQ 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386781089 218 KVKvgkedssSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLES 264
Cdd:cd06865   80 VMQ-------SAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTL 119
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
143-264 1.37e-24

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: 98.20  E-value: 1.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 143 EIGVSDPEKVGDGMNAYMAYRVTTKTSlsmfSKSEFSVKRRFSDFLGLHSKLASKYLhvGYIVPPAPEKSIVGMTkvkvg 222
Cdd:cd06093    1 SVSIPDYEKVKDGGKKYVVYIIEVTTQ----GGEEWTVYRRYSDFEELHEKLKKKFP--GVILPPLPPKKLFGNL----- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 386781089 223 kedssSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLES 264
Cdd:cd06093   70 -----DPEFIEERRKQLEQYLQSLLNHPELRNSEELKEFLEL 106
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
170-265 3.44e-24

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 96.16  E-value: 3.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  170 LSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVgyIVPPAPEKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQRTVKH 249
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSV--IIPPLPPKRWLG----------RYNEEFIEKRRKGLEQYLQRLLQH 68
                          90
                  ....*....|....*.
gi 386781089  250 PTLLQDPDLRQFLESS 265
Cdd:pfam00787  69 PELRNSEVLLEFLESD 84
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
142-262 1.81e-22

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: 92.35  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylHVGYIVPPAPEKSIVGmtkvkv 221
Cdd:cd07284    1 IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEA--HPTLIIPPLPEKFVMK------ 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd07284   73 GMVERFNEDFIETRRKALHKFLNRIADHPTLTFNEDFKIFL 113
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
142-262 1.47e-21

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: 90.12  E-value: 1.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEK--VGDGMN---AYMAYRVTTK----TSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVgyIVPPAPEKS 212
Cdd:cd06864    1 MEITVTEAEKrtGGSAMNlkeTYTVYLIETKivehESEEGLSKKLSSLWRRYSEFELLRNYLVVTYPYV--IVPPLPEKR 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 386781089 213 IVGMTKVKVGkeDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd06864   79 AMFMWQKLSS--DTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFL 126
Sorting_nexin pfam03700
Sorting nexin, N-terminal domain; These proteins bins to the cytoplasmic domain of plasma ...
3-75 2.33e-19

Sorting nexin, N-terminal domain; These proteins bins to the cytoplasmic domain of plasma membrane receptors. and are involved in endocytic protein trafficking. The N-terminal domain appears to be specific to sorting nexins 1 and 2.


Pssm-ID: 461016  Cd Length: 75  Bit Score: 82.27  E-value: 2.33e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089    3 AEREPPPLGDGKPTDFEDLE------DGEDLFTSTVSTlessPSSPEPASLPAEDISANSNGPKPTEVGLDDDREDLFA 75
Cdd:pfam03700   1 SEREPPPFPDSEDPEPEDAAgdgdsdEGEDIFTGTVST----LGSSPSSPEPASLPFTNSNGPKTNGVHSDDDQQDLFA 75
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
141-509 1.43e-18

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 88.70  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 141 DIEIGVSDPEKVGDGM---NAYMAYRVTTKTSLSMFSKSEF---SVKRRFSDFLGLHSKLASKYLhvGYIVPPAPEKSIV 214
Cdd:COG5391  130 FISSTVSNPQSLTLLVdsrDKHTSYEIITVTNLPSFQLRESrplVVRRRYSDFESLHSILIKLLP--LCAIPPLPSKKSN 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 215 GMTkvkvgKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDP----------DLRQFLE------SSELPRAVNTQALSG 278
Cdd:COG5391  208 SEY-----YGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNYKnsksweshstLLSSFIEnrksvpTPLSLDLTSTTQELD 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 279 AGILRMVNKAADAVNKMTIKMNEsdawFEEKQQQFENLDQQL-RKLHASVEALVCHRKELSANTAAFAK---SAAMLGNS 354
Cdd:COG5391  283 MERKELNESTSKAIHNILSIFSL----FEKILIQLESEEESLtRLLESLNNLLLLVLNFSGVFAKRLEQnqnSILNEGVV 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 355 EDHTALS---RALSQLAEVEEKIDQL-----HQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITL-L 425
Cdd:COG5391  359 QAETLRSslkELLTQLQDEIKSRESLiltdsNLEKLTDQNLEDVEELSRSLRKNSSQRAVVSQQPEGLTSFSKLSYKLrD 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 426 KKREAEAKmmvaNKPDKIQQAKNEIREweaKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLI 505
Cdd:COG5391  439 FVQEKSRS----KSIESLQQDKEKLEE---QLAIAEKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENL 511

                 ....
gi 386781089 506 KYWE 509
Cdd:COG5391  512 EIWK 515
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
144-264 1.12e-17

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: 78.97  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 144 IGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylHVGYIVPPAPEKSIVGmtkvkvGK 223
Cdd:cd07283    3 VTVDDPKKHVCTMETYITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEES--QPTHLIPPLPEKFVVK------GV 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 386781089 224 EDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLES 264
Cdd:cd07283   75 VDRFSEEFVETRRKALDKFLKRIADHPVLSFNEHFNVFLTA 115
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
142-263 6.27e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX3 associates with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P). It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume.


Pssm-ID: 132826  Cd Length: 123  Bit Score: 74.26  E-value: 6.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylhVGYIVPPAPEKSIVGMTKVKv 221
Cdd:cd07293    2 LEIDVTNPQTVGVGRGRFTTYEIRLKTNLPIFKLKESTVRRRYSDFEWLRSELERE---SKVVVPPLPGKALFRQLPFR- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd07293   78 GDDGIFDDSFIEERKQGLEQFLNKVAGHPLAQNERCLHMFLQ 119
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
142-263 3.15e-15

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: 72.11  E-value: 3.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLA--SKylhvgYIVPPAPEKSIVGMTKV 219
Cdd:cd06894    2 LEIDVVNPQTHGVGKKRFTDYEVRMRTNLPVFKKKESSVRRRYSDFEWLRSELErdSK-----IVVPPLPGKALKRQLPF 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 220 KvGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd06894   77 R-GDDGIFEEEFIEERRKGLETFINKVAGHPLAQNEKCLHMFLQ 119
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
142-269 1.26e-14

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: 70.84  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylhVGYIVPPAPEKSIVGMTKVKv 221
Cdd:cd07294    4 LEIDIFNPQTVGVGRNRFTTYEVRMRTNLPIFKLKESCVRRRYSDFEWLKNELERD---SKIVVPPLPGKALKRQLPFR- 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386781089 222 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESSELPR 269
Cdd:cd07294   80 GDEGIFEESFIEERRQGLEQFINKIAGHPLAQNERCLHMFLQDETIDR 127
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
180-264 2.34e-13

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: 66.95  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 180 VKRRFSDFLGLHSKLASKYLHVGYIvpPAPEKSIVGmtkvkvgkEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLR 259
Cdd:cd06876   59 VARRYSEFLELHKYLKKRYPGVLKL--DFPQKRKIS--------LKYSKTLLVEERRKALEKYLQELLKIPEVCEDEEFR 128

                 ....*
gi 386781089 260 QFLES 264
Cdd:cd06876  129 KFLSQ 133
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
138-265 3.32e-13

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: 65.71  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 138 DIFDIEIgvsDPEKvgDGM-NAYMAYRVTTKtslsmfsKSEFSVKRRFSDFLGLHSKLASKYLHvgYIVPPAPEKSIVGm 216
Cdd:cd06866    1 DTVTVEL---VPEK--KGLfLKHVEYEVSSK-------RFKSTVYRRYSDFVWLHEYLLKRYPY--RMVPALPPKRIGG- 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 386781089 217 tkvkvgkedSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 265
Cdd:cd06866   66 ---------SADREFLEARRRGLSRFLNLVARHPVLSEDELVRTFLTEP 105
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
141-263 3.85e-13

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 66.62  E-value: 3.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 141 DIEIGVSDPEKVgdgmnaymAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIV-----G 215
Cdd:cd07291    6 DIPDALSERDKV--------KFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFdgpreK 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386781089 216 MTKVKVGKEDSSSTEFVEKRR--------------AALERYLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd07291   78 MQKLGEGEGSMTKEEFAKMKQeleaeylavfkktvQVHEVFLQRLSSHPSLSKDRNFHIFLE 139
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
146-264 8.93e-13

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: 64.66  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDPE-KVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKylHVGYIVPPAPEKSIVGMTKVKvgke 224
Cdd:cd06898    4 VRDPRtHKEDDWGSYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKN--ALLIQLPSLPPKNLFGRFNNE---- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 386781089 225 dssstEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLES 264
Cdd:cd06898   78 -----GFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFLQT 112
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
141-263 6.97e-12

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: 63.22  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 141 DIEIGVSDPEKVgdgmnaymAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKS--IVGMTK 218
Cdd:cd06892    6 DISDALSERDKV--------KFTVHTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENEDYAGLIIPPAPPKPdfDASREK 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386781089 219 V-KVGKEDSSST-EFVEKRRAALERY---------------LQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd06892   78 LqKLGEGEGSMTkEEFEKMKQELEAEylaifkktvamhevfLRRLASHPVLRNDANFRVFLE 139
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
155-266 9.81e-12

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: 62.33  E-value: 9.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 155 GMNAYMAYRVTTktslsmfSKSEFSVKRRFSDFLGLHSKLASKYLHVgyIVPPAPEKSIVGmtkvkvgkedSSSTEFVEK 234
Cdd:cd06862   16 GLKSFIAYQITP-------THTNVTVSRRYKHFDWLYERLVEKYSCI--AIPPLPEKQVTG----------RFEEDFIEK 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 386781089 235 RRAALERYLQRTVKHPTLLQDPDLRQFLESSE 266
Cdd:cd06862   77 RRERLELWMNRLARHPVLSQSEVFRHFLTCTD 108
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
142-266 3.98e-11

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: 60.20  E-value: 3.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVgyIVPPAPEKSIVgmtkvkv 221
Cdd:cd07295    2 LEIEVRNPKTHGIGRGMFTDYEIVCRTNIPAFKLRVSSVRRRYSDFEYFRDILERESPRV--MIPPLPGKIFT------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386781089 222 gkeDSSSTEFVEKRRAALERYLQRTVKHPtLLQDPD--LRQFLESSE 266
Cdd:cd07295   73 ---NRFSDEVIEERRQGLETFLQSVAGHP-LLQTGSkvLAAFLQDPK 115
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
157-263 1.05e-10

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


Pssm-ID: 132807  Cd Length: 108  Bit Score: 58.82  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 157 NAYMAYRVTTKTSLSmfsksEFSVKRRFSDFLGLHSKLASkylHVGYIVP-PAPEKSIVgmtkvkvgKEDSSSTEFVEKR 235
Cdd:cd06897   13 KPYTVYNIQVRLPLR-----SYTVSRRYSEFVALHKQLES---EVGIEPPyPLPPKSWF--------LSTSSNPKLVEER 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 386781089 236 RAALERYLQRTVKHP-TLLQD-PDLRQFLE 263
Cdd:cd06897   77 RVGLEAFLRALLNDEdSRWRNsPAVKEFLN 106
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
143-263 2.74e-10

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: 57.65  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 143 EIGVSDPEKVGDGMN-AYMAYRVTTKTSlsmfsksefSVKRRFSDFLGLHSKLASkyLHVGYIVPPAPEK-SIVG-MTKV 219
Cdd:cd06867    1 PIQIVDAGKSSEGGSgSYIVYVIRLGGS---------EVKRRYSEFESLRKNLTR--LYPTLIIPPIPEKhSLKDyAKKP 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 220 KVGKEDSsstEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd06867   70 SKAKNDA---KIIERRKRMLQRFLNRCLQHPILRNDIVFQKFLD 110
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
158-264 1.13e-09

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: 56.18  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 158 AYMAYRVTTKTSLSmfSKSEFSVKRRFSDFLGLHSKLASKY-LHVGYIVPPAPEKSIVGMTKVKVGKEdsssteFVEKRR 236
Cdd:cd07280   21 AYVVWKITIETKDL--IGSSIVAYKRYSEFVQLREALLDEFpRHKRNEIPQLPPKVPWYDSRVNLNKA------WLEKRR 92
                         90       100
                 ....*....|....*....|....*...
gi 386781089 237 AALERYLQRTVKHPTLLQDPDLRQFLES 264
Cdd:cd07280   93 RGLQYFLNCVLLNPVFGGSPVVKEFLLP 120
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
146-263 2.37e-09

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: 55.02  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDPEKVGDGmnaYMAYRVTTKtslsMFSK------SEFSVKRRFSDFLGLHSKLASKY--LHVGYIVPPAPEKSIVGmt 217
Cdd:cd06881    7 VTDTRRHKKG---YTEYKITSK----VFSRsvpedvSEVVVWKRYSDFKKLHRELSRLHkqLYLSGSFPPFPKGKYFG-- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 386781089 218 kvkvgkedSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd06881   78 --------RFDAAVIEERRQAILELLDFVGNHPALYQSSAFQQFFE 115
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
141-263 4.89e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 55.11  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 141 DIEIGVSDPEKVgdgmnaymAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVK 220
Cdd:cd07292    6 DISDALSERDKV--------KFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREK 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386781089 221 VGK----EDSSSTEFVEKRRAALER---------------YLQRTVKHPTLLQDPDLRQFLE 263
Cdd:cd07292   78 LQKlgegEGSMTKEEFTKMKQELEAeylaifkktvamhevFLCRVAAHPILRKDLNFHVFLE 139
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
142-262 8.69e-09

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: 53.57  E-value: 8.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKV-GDGMNAYMAYRVTTKTSLSMFSKS--------EFSVKRRFSDFLGLHSKLASKYLHVgyIVPPAPEK- 211
Cdd:cd06868    2 LDLTVPEYQEIrGKTSSGHVLYQIVVVTRLAAFKSAkhkeedvvQFMVSKKYSEFEELYKKLSEKYPGT--ILPPLPRKa 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386781089 212 SIVGMTKVKvgkedssstefveKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd06868   80 LFVSESDIR-------------ERRAAFNDFMRFISKDEKLANCPELLEFL 117
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
177-263 3.90e-08

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: 51.51  E-value: 3.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 177 EFSVKRRFSDFLGLHSKLASKYLHVGYIVPPapeKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQRTV-KHPTLLQD 255
Cdd:cd06875   30 EWTVKHRYSDFAELHDKLVAEHKVDKDLLPP---KKLIG----------NKSPSFVEKRRKELEIYLQTLLsFFQKTMPR 96

                 ....*...
gi 386781089 256 PdLRQFLE 263
Cdd:cd06875   97 E-LAHFLD 103
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
280-495 2.13e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; 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. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153347  Cd Length: 218  Bit Score: 51.86  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 280 GILRMVNKAADAVNKMTIKmnESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSAN---TAAFAKSAAmlgnSED 356
Cdd:cd07663    1 GFFKNMVKSADEVLFSGVK--EVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDyihISAALNSVA----AEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 357 HTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLlkkreaeakmmv 436
Cdd:cd07663   75 PTVIKKYLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKAL------------ 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089 437 ankpDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLE 495
Cdd:cd07663  143 ----DKARLKSKDVKQAEAHQQECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTE 197
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
150-262 3.76e-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: 49.08  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 150 EKVGDGMNAYMAYRVTTKTSL-----------SMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSivgMTK 218
Cdd:cd06893   12 EYKGTGTHPYTLYTVQYETILdvqseqnpnaaSEQPLATHTVNRRFREFLTLQTRLEENPKFRKIMNVKGPPKR---LFD 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 386781089 219 VKVGKEDSSStefVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd06893   89 LPFGNMDKDK---IEARRGLLETFLRQLCSIPEISNSEEVQEFL 129
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
177-249 6.48e-07

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: 48.11  E-value: 6.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 177 EFSVKRRFSDFLGLHSKLASKYLHVG-YIVPPapeksivgmtKVKVGKEDsssTEFVEKRRAALERYLQRTVKH 249
Cdd:cd07277   31 EWNVYRRYSEFYELHKKLKKKFPVVRsFDFPP----------KKAIGNKD---AKFVEERRKRLQVYLRRVVNT 91
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
142-263 6.55e-07

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: 48.03  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVsdpekVGDGMNAYMAYRVT-TKTSLSMFSKSeFSVKRRFSDFLGLHSKLASKYLHVGYIVPPApEKSIVGMTKvk 220
Cdd:cd06873   10 INTGI-----VKEHGKTYAVYAISvTRIYPNGQEES-WHVYRRYSDFHDLHMRLKEKFPNLSKLSFPG-KKTFNNLDR-- 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386781089 221 vgkedssstEFVEKRRAALERYLQRTVKHPTLLQDPDLR----QFLE 263
Cdd:cd06873   81 ---------AFLEKRRKMLNQYLQSLLNPEVLDANPGLQeivlDFLE 118
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
184-474 7.22e-07

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 52.26  E-value: 7.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  184 FSDFLGLHsklaskyLHVGYIVPPAPEKSIVGMTKVKVGKE----DSSSTEFVEKRRAALERY--LQRTVKHPTLLQDPD 257
Cdd:COG3096   818 FSQFVGGH-------LAVAFAPDPEAELAALRQRRSELERElaqhRAQEQQLRQQLDQLKEQLqlLNKLLPQANLLADET 890
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  258 LRQFLESSelpRAVNTQALSGAGILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALvchrKEL 337
Cdd:COG3096   891 LADRLEEL---REELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEV 963
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  338 SANTAAFA--KSAAMLGNSedhTALSRAL-SQLAEVEEKI----DQLHQEQAfadfymfseLLSDYIRLIAAVKGVFDHR 410
Cdd:COG3096   964 VQRRPHFSyeDAVGLLGEN---SDLNEKLrARLEQAEEARrearEQLRQAQA---------QYSQYNQVLASLKSSRDAK 1031
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089  411 MKCWQKWED--AQITLLKKREAEAKmmVANKPDKIQQA----KNEIREWEAKVQQGERDFEQISKTIRKE 474
Cdd:COG3096  1032 QQTLQELEQelEELGVQADAEAEER--ARIRRDELHEElsqnRSRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
146-262 9.29e-07

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: 48.13  E-value: 9.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDPEKVGD--GMNAYMAYRVTTktslsmfSKSEFSVKRRFSDFLGLHSKLASKYLHVGyiVPPAPEKSIVGMTKvkvgk 223
Cdd:cd07286    5 IDDPTKQTKfkGMKSYISYKLVP-------SHTGLQVHRRYKHFDWLYARLAEKFPVIS--VPHIPEKQATGRFE----- 70
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 386781089 224 EDsssteFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd07286   71 ED-----FISKRRKGLIWWMDHMCSHPVLARCDAFQHFL 104
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
146-262 1.26e-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: 46.94  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDP---EKVGDGMNAYMAYRVTTKTSLsmfsksEFSVkrRFSDFLGLHSKLASKYlhVGYIVPPAPEKSIVGMTKVKVg 222
Cdd:cd06885    2 FSIPdtqELSDEGGSTYVAYNIHINGVL------HCSV--RYSQLHGLNEQLKKEF--GNRKLPPFPPKKLLPLTPAQL- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 386781089 223 kedssstefvEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd06885   71 ----------EERRLQLEKYLQAVVQDPRIANSDIFNSFL 100
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
146-266 1.34e-06

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: 47.43  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDPEKVgDGMNAYMAYRVTTKTSlsmfSKSEFSVKRRFSDFLGLHSKLASKY-LHVGY-----IVPPAPEKSIVGmtkv 219
Cdd:cd06882    8 IADIEEK-RGFTNYYVFVIEVKTK----GGSKYLIYRRYRQFFALQSKLEERFgPEAGSsaydcTLPTLPGKIYVG---- 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386781089 220 kvgkedsSSTEFVEKRRAALERYLQRTVK-HPTLLQDPDLRQFLESSE 266
Cdd:cd06882   79 -------RKAEIAERRIPLLNRYMKELLSlPVWVLMDEDVRLFFYQTE 119
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
146-262 2.76e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 46.50  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDPEKVGDGmnaYMAYRVTTKtslsMFSKS------EFSVKRRFSDFLGLHSKLAskYLHVGYI-----VPPAPEKSIV 214
Cdd:cd07288    7 VTDPRTHPKG---YTEYKVTAQ----FISKKqpedvkEVVVWKRYSDLKKLHGELA--YTHRNLFrrqeeFPPFPRAQVF 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386781089 215 GMTKVKVgkedssstefVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd07288   78 GRFEAAV----------IEERRNAAEAMLLFTVNIPALYNSPQLKEFF 115
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
142-263 7.62e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; 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. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 44.96  E-value: 7.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 142 IEIGVSDPEKVGDGMN-AYMAYRVTTKtslsmFSKSEFSVKRRFSDFLGLHSKLASKYLhvgyiVPPAPEKSIvgmtkvk 220
Cdd:cd06880    1 IEVSIPSYRLEVDESEkPYTVFTIEVL-----VNGRRHTVEKRYSEFHALHKKLKKSIK-----TPDFPPKRV------- 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 386781089 221 vgkeDSSSTEFVEKRRAALERYLQRTVKHPTLLQdpDLRQFLE 263
Cdd:cd06880   64 ----RNWNPKVLEQRRQGLEAYLQGLLKINELPK--QLLDFLG 100
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
179-262 1.57e-05

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


Pssm-ID: 132812  Cd Length: 112  Bit Score: 44.24  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 179 SVKRRFSDFLGLHSKLASKYlhvgyivpPAPEKSIVGMTKVKVGkedSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDL 258
Cdd:cd07279   37 FIERRYSDFLKLYKALRKQH--------PQLMAKVSFPRKVLMG---NFSSELIAERSRAFEQFLGHILSIPNLRDSKAF 105

                 ....
gi 386781089 259 RQFL 262
Cdd:cd07279  106 LDFL 109
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
175-267 1.68e-05

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: 44.29  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 175 KSEFSVKRRFSDFLGLHSKLASkyLHVGYIVPPAPEKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQrtvkhpTLLQ 254
Cdd:cd06877   41 PQHWSVLRRYNEFYVLESKLTE--FHGEFPDAPLPSRRIFG----------PKSYEFLESKREIFEEFLQ------KLLQ 102
                         90
                 ....*....|...
gi 386781089 255 DPDLRqfleSSEL 267
Cdd:cd06877  103 KPELR----GSEL 111
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
306-514 1.92e-05

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


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 45.51  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 306 FEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEEKIDQLHQ--EQAF 383
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTDLGEALEKFGKIQKELEEFRDQLEQklENKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 384 ADFymFSELLSDYIRLIAAVKGVFDHRMkcwQKWEDAQITLLKKREAeakmmvANKPDKIQQAkneirewEAKVQQGERD 463
Cdd:cd07307   82 IEP--LKEYLKKDLKEIKKRRKKLDKAR---LDYDAAREKLKKLRKK------KKDSSKLAEA-------EEELQEAKEK 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386781089 464 FEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPE 514
Cdd:cd07307  144 YEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
351-506 5.41e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; 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. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. 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. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 44.63  E-value: 5.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 351 LGNSEdHTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKRea 430
Cdd:cd07621   71 LATSE-PTPLDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKAR-- 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089 431 eAKMMVANKPDKIQQAKNEireweakvqqgerDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLV---QTQQQLIK 506
Cdd:cd07621  148 -AKNKDVHAAEAAQQEACE-------------KFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIkhaKAQIQLLK 212
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
153-245 5.46e-05

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; 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. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. 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: 132784  Cd Length: 127  Bit Score: 42.75  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 153 GDGMNAYMAYRVTTKTSlsmfsKSEFSVKRRFSDFLGLHSKLASKYLHVGYIvpPAPEKSIVGmtkvkvgkedSSSTEFV 232
Cdd:cd06874   12 GQGKDEHFEFEVKITVL-----DETWTVFRRYSRFRELHKTMKLKYPEVAAL--EFPPKKLFG----------NKSERVA 74
                         90
                 ....*....|...
gi 386781089 233 EKRRAALERYLQR 245
Cdd:cd06874   75 KERRRQLETYLRN 87
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
176-262 7.78e-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: 42.01  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 176 SEFSVKRRFSDFLGLHSKLASKYlhvgyivpPA-----PEKSIVGmtkvkvgkeDSSSTEFVEKRRAALERYLQRTVKHP 250
Cdd:cd06870   32 SSWFVFRRYAEFDKLYESLKKQF--------PAsnlkiPGKRLFG---------NNFDPDFIKQRRAGLDEFIQRLVSDP 94
                         90
                 ....*....|..
gi 386781089 251 TLLQDPDLRQFL 262
Cdd:cd06870   95 KLLNHPDVRAFL 106
BAR_SNX_like cd07630
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are ...
360-500 1.48e-04

The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of uncharacterized proteins with similarity to sorting nexins (SNXs), which 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: 153314  Cd Length: 198  Bit Score: 42.88  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 360 LSRALSQLAEVEEKIDQlhqeqAFAD-FYMFSELLSDYIRLIAAVKGVFDHRM----KCWQKWEDAQITLLKKR------ 428
Cdd:cd07630   44 LSSSLQLCVGLDEASVV-----ALNRlCTKLSEALEEAKENIEVVAGNNENTLgltlDLYSRYSESEKDMLFRRtcklie 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386781089 429 -EAEAKMMVANKPDKIQQAkneirewEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQT 500
Cdd:cd07630  119 fENASKALEKAKPQKKEQA-------EEAKKKAETEFEEISSLAKKELERFHRQRVLELQSALVCYAESQIKN 184
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
146-262 1.50e-04

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: 41.55  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 146 VSDPEKVGD--GMNAYMAYRVTTKTSlsmfsksEFSVKRRFSDFLGLHSKLASKYlHVGYIVPPAPEKSIVGMTKvkvgk 223
Cdd:cd07285    5 VADPRKGSKmyGLKSYIEYQLTPTNT-------NRSVNHRYKHFDWLYERLLVKF-GLAIPIPSLPDKQVTGRFE----- 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 386781089 224 edsssTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 262
Cdd:cd07285   72 -----EEFIKMRMERLQAWMTRMCRHPVISESEVFQQFL 105
BAR_SNX9_like cd07626
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9 and Similar Proteins; BAR domains are ...
351-506 2.79e-04

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: 42.25  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 351 LGNSEDHTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQitllkKREA 430
Cdd:cd07626   58 LDETPTSVPLTQAIKHTGQAYEEIGELFAEQPKHDLIPLLDGLHEYKGLLSTFPDIIGVHKGAVQKVKECE-----RLVD 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386781089 431 EAKMMVAnkpdkiqqaknEIREWEAKVqqgerdfEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIK 506
Cdd:cd07626  133 EGKMSSA-----------ELEEVKRRT-------DVISYALLAEINHFHRERVRDFKSMMRNYLQQQIEFYQKIAA 190
PX_Vps17p cd06891
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain ...
115-264 7.03e-04

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; 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. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. Similar to Vps5p and SNX1, Vps17p harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit helps determine specific membrane localization.


Pssm-ID: 132801  Cd Length: 140  Bit Score: 40.03  E-value: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 115 SKSMSAPVIFDRSREEIEEEANGDIFDIEIGVSDPEKVGDGmNAYMAYRVTTKtsLSMFSKSEF-SVKRRFSDFlglhSK 193
Cdd:cd06891    3 PSQPESRKILTSNRRELEPERKKPKYFLRVRVTGIERNKSK-DPIIRFDVTTN--LPTFRSSTYkDVRRTYEEF----QK 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781089 194 LAsKYLHVGY---IVPPAPEKSivgmtkvkvGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLES 264
Cdd:cd06891   76 LF-KYLNGANpetFVPALPLPS---------TSYGSNNEEDARKLKANLQRWFNRVCSDPILIRDEELRFFIES 139
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
180-258 7.30e-04

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


Pssm-ID: 132793  Cd Length: 109  Bit Score: 39.26  E-value: 7.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089 180 VKRRFSDFLGLHSKLASKYLHVGyiVPPAPEKSIVGMTKVKvgkedssstEFVEKRRAALERYLQRTVKHPTLLQDPDL 258
Cdd:cd06883   34 VFRTFEEFQELHNKLSLLFPSLK--LPSFPARVVLGRSHIK---------QVAERRKIELNSYLKSLFNASPEVAESDL 101
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
180-263 9.85e-04

The phosphoinositide binding Phox Homology domain of uncharacterized 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 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: 132789  Cd Length: 138  Bit Score: 39.62  E-value: 9.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 180 VKRRFSDFLGLHSKLASKYLHVGyiVPPAPEKSIVGMtkvkvgkedsSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLR 259
Cdd:cd06879   65 VLRRFNDFLKLHTDLKKLFPKKK--LPAAPPKGLLRM----------KNRALLEERRHSLEEWMGKLLSDIDLSRSVPVA 132

                 ....
gi 386781089 260 QFLE 263
Cdd:cd06879  133 SFLE 136
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
173-264 1.74e-03

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: 38.50  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 173 FSKSEFSVKRRFSDFLGLHsklasKYLHVGYIVPPAPEKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQRTVKHPTL 252
Cdd:cd06871   33 SPENSWQVIRRYNDFDLLN-----ASLQISGISLPLPPKKLIG----------NMDREFIAERQQGLQNYLNVILMNPIL 97
                         90
                 ....*....|..
gi 386781089 253 LQDPDLRQFLES 264
Cdd:cd06871   98 ASCLPVKKFLDP 109
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
282-495 2.39e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; 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. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 39.64  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 282 LRMVNKAADAVNKMTIKmnESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGnSEDHTALS 361
Cdd:cd07662    3 FKNVVKSADGVIVSGVK--DVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLG-TQDSTDIC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 362 RALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLlkkreaeakmmvankpD 441
Cdd:cd07662   80 KFFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKAL----------------D 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 386781089 442 KIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLE 495
Cdd:cd07662  144 KARAKNKDVLQAETTQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAE 197
BAR_Atg20p cd07629
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg20p; BAR domains are ...
301-510 4.90e-03

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


Pssm-ID: 153313  Cd Length: 187  Bit Score: 38.14  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 301 ESDAWFEEKQQQFENLDQQL--------RKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEE 372
Cdd:cd07629    1 EPDDEFTDIEAETKKYEQLLhggmekvnRRITKRLGDLAEDMADLGGRFNAFSLEEQKSELAEALEKVGQAVDSTYLATE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 373 KIDQ-LHqeqafadfYMFSELLSDYIRLIAAVKGVFDHRmkcwqKWEDAQITLLKKREAEAKMMVANKPDKIQqakneir 451
Cdd:cd07629   81 ALVGsLY--------YNINEPLSESAQFAGVVRELLKYR-----KLKHVQYEMTKDSLLESALVAASDDLVIS------- 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386781089 452 eweakvqqgerdfeqiSKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEA 510
Cdd:cd07629  141 ----------------STIKQKDLPRFQREREADLREILKNYSKYHKDWAKQNLEAWKE 183
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
180-262 5.55e-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: 36.62  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 180 VKRRFSDFLGLHSKLASKYLHVGYIVPPapeKSIVGmtkvkvgkeDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLR 259
Cdd:cd07276   37 VFRRYTDFVRLNDKLKQMFPGFRLSLPP---KRWFK---------DNFDPDFLEERQLGLQAFVNNIMAHKDIAKCKLVR 104

                 ...
gi 386781089 260 QFL 262
Cdd:cd07276  105 EFF 107
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
180-265 9.33e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; 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. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, 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: 132788  Cd Length: 127  Bit Score: 36.58  E-value: 9.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781089 180 VKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLR 259
Cdd:cd06878   52 VTRKLSEFHDLHRKLKECSSWLKKVELPSLSKKWFK----------SIDKKFLDKSKNQLQKYLQFILEDETLCQSEALY 121

                 ....*.
gi 386781089 260 QFLESS 265
Cdd:cd06878  122 SFLSPS 127
 
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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