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Conserved domains on  [gi|17550150|ref|NP_508216|]
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PX domain-containing protein [Caenorhabditis elegans]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10246351)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein similar to Saccoglossus kowalevskii sorting nexin 2

Gene Ontology:  GO:0035091|GO:0006612|GO:0140090
PubMed:  15649145|16782399|11884510

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 243-468 6.42e-101

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: 301.50  E-value: 6.42e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 243 SKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSRALSSLTDVTE 322
Cdd:cd07623   1 SKITIKMDETDQWFEEKQQQIENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLSNCEEHTSLSRALSQLAEVEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 323 NVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSagGRNERSDQLKGEI 402
Cdd:cd07623  81 KIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKREAKAKLELS--GRTDKLDQAQQEI 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17550150 403 EDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPEAN 468
Cdd:cd07623 159 KEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQQLIKYWEAFLPEAK 224
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 91-214 3.13e-32

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


The actual alignment was detected with superfamily member cd07281:

Pssm-ID: 470617  Cd Length: 124  Bit Score: 119.39  E-value: 3.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  91 KVTMREFEKRGDGMNAYIVYKLETEVSgVVGYTKQHYETWRRFSDFLGLHGKIVEKYLAKGIVIPQPPEKSISALTKTKT 170
Cdd:cd07281   2 KVSITDPEKIGDGMNAYVVYKVTTQTS-LLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17550150 171 NSDPAMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd07281  81 GKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLEKE 124
 
Name Accession Description Interval E-value
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 243-468 6.42e-101

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: 301.50  E-value: 6.42e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 243 SKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSRALSSLTDVTE 322
Cdd:cd07623   1 SKITIKMDETDQWFEEKQQQIENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLSNCEEHTSLSRALSQLAEVEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 323 NVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSagGRNERSDQLKGEI 402
Cdd:cd07623  81 KIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKREAKAKLELS--GRTDKLDQAQQEI 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17550150 403 EDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPEAN 468
Cdd:cd07623 159 KEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQQLIKYWEAFLPEAK 224
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 231-466 1.56e-80

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: 249.51  E-value: 1.56e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150   231 VKKIFKNFQVVFSKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSL 310
Cdd:pfam09325   1 LSSLFGKFFSSVSKSSYKFNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150   311 SRALSSLTDVTENVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSAGG 390
Cdd:pfam09325  81 SRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLLRANKS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17550150   391 RNERSDQLKGEIEDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPE 466
Cdd:pfam09325 161 QNDKLQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQKELIELWETFLPE 236
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 91-214 3.13e-32

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: 119.39  E-value: 3.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  91 KVTMREFEKRGDGMNAYIVYKLETEVSgVVGYTKQHYETWRRFSDFLGLHGKIVEKYLAKGIVIPQPPEKSISALTKTKT 170
Cdd:cd07281   2 KVSITDPEKIGDGMNAYVVYKVTTQTS-LLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17550150 171 NSDPAMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd07281  81 GKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLEKE 124
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 96-212 1.47e-20

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: 86.24  E-value: 1.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150     96 EFEKRGDGMNAYIVYKLETEVSgvvgytKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALtktktnsDPA 175
Cdd:smart00312   3 EPEKIGDGKHYYYVIEIETKTG------LEEWTVSRRYSDFLELHSKLKKHF--PRSILPPLPGKKLFGR-------LNN 67

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17550150    176 MSREVGIQRARQLERYICRLIQHPRMRNDCD-VRDFLT 212
Cdd:smart00312  68 FSEEFIEKRRRGLEKYLQSLLNHPELINHSEvVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 119-214 7.92e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 66.50  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150   119 VVGYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISaltktkTNSDPAMSREvgiqRARQLERYICRLIQH 198
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKF--PSVIIPPLPPKRWL------GRYNEEFIEK----RRKGLEQYLQRLLQH 68

                          90
                  ....*....|....*.
gi 17550150   199 PRMRNDCDVRDFLTIE 214
Cdd:pfam00787  69 PELRNSEVLLEFLESD 84
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 37-464 9.55e-11

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 63.66  E-value: 9.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  37 NEDTPPSKLRLHTTEEPKESSSPAVINSIEDHDQYVGNDNHYAQISPEPALSNFKVTMREFEKRgdgMNAYIVYKLETEV 116
Cdd:COG5391  96 SRASEFRSLRDMLSLLLPTSLQPPLSTSHTILDYFISSTVSNPQSLTLLVDSRDKHTSYEIITV---TNLPSFQLRESRP 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 117 SGVVgytkqhyetwRRFSDFLGLHGKIVEKYLakGIVIPQPPEK-SISALTKTKtnsdpaMSREVGIQRARQLERYICRL 195
Cdd:COG5391 173 LVVR----------RRYSDFESLHSILIKLLP--LCAIPPLPSKkSNSEYYGDR------FSDEFIEERRQSLQNFLRRV 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 196 IQHPRMRNDCDVRDFLTIESDL----------PKAVQTAALSSF-GVKKIFKNFQVVFSKMAFHMEEGDRWFEQVQSQVD 264
Cdd:COG5391 235 STHPLLSNYKNSKSWESHSTLLssfienrksvPTPLSLDLTSTTqELDMERKELNESTSKAIHNILSIFSLFEKILIQLE 314

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 265 ELDEALRKLytVTETLVASRRDMATSGEQLGK---------ALSMLAACEESTSLSRALSSLTDVTENVSAVYGKQAEV- 334
Cdd:COG5391 315 SEEESLTRL--LESLNNLLLLVLNFSGVFAKRleqnqnsilNEGVVQAETLRSSLKELLTQLQDEIKSRESLILTDSNLe 392

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 335 ----DNSKFSESIYEYIMLISALKDVFGERvrawqqwqDAQQTLARKRDQKTKIDLSAGGRNERSDQLKGEIEDTVQKMD 410
Cdd:COG5391 393 kltdQNLEDVEELSRSLRKNSSQRAVVSQQ--------PEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDKEKLEEQLA 464

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 17550150 411 QLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFE 464
Cdd:COG5391 465 IAEKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSVK 518
 
Name Accession Description Interval E-value
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 243-468 6.42e-101

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: 301.50  E-value: 6.42e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 243 SKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSRALSSLTDVTE 322
Cdd:cd07623   1 SKITIKMDETDQWFEEKQQQIENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLSNCEEHTSLSRALSQLAEVEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 323 NVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSagGRNERSDQLKGEI 402
Cdd:cd07623  81 KIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKREAKAKLELS--GRTDKLDQAQQEI 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17550150 403 EDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPEAN 468
Cdd:cd07623 159 KEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQQLIKYWEAFLPEAK 224
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 231-466 1.56e-80

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: 249.51  E-value: 1.56e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150   231 VKKIFKNFQVVFSKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSL 310
Cdd:pfam09325   1 LSSLFGKFFSSVSKSSYKFNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150   311 SRALSSLTDVTENVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSAGG 390
Cdd:pfam09325  81 SRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLLRANKS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17550150   391 RNERSDQLKGEIEDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPE 466
Cdd:pfam09325 161 QNDKLQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQKELIELWETFLPE 236
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
 243-467 5.64e-50

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: 170.23  E-value: 5.64e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 243 SKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSRALSSLTDVTE 322
Cdd:cd07664  11 NKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 323 NVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSagGRNERSDQLKGEI 402
Cdd:cd07664  91 KIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKREAEAKLQYA--NKPDKLQQAKDEI 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17550150 403 EDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPEA 467
Cdd:cd07664 169 KEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEA 233
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
 233-467 1.35e-44

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: 156.00  E-value: 1.35e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 233 KIFKNFQVVFSKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSR 312
Cdd:cd07665   1 KMFNKATDAVSKMTIKMNESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSSEDNTALSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 313 ALSSLTDVTENVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKidLSAGGRN 392
Cdd:cd07665  81 ALSQLAEVEEKIEQLHQEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAMLQKKREAEAR--LLWANKP 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17550150 393 ERSDQLKGEIEDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPEA 467
Cdd:cd07665 159 DKLQQAKDEIAEWESRVTQYERDFERISATVRKEVIRFEKEKSKDFKNHIIKYLETLLHSQQQLVKYWEAFLPEA 233
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 251-466 6.51e-34

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: 127.09  E-value: 6.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 251 EGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEE--STSLSRALSSLTDVTENVSAVY 328
Cdd:cd07596   1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEevGGELGEALSKLGKAAEELSSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 329 GKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSAGGRNERSDQLKGEIEDTVQK 408
Cdd:cd07596  81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17550150 409 MDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPE 466
Cdd:cd07596 161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 91-214 3.13e-32

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: 119.39  E-value: 3.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  91 KVTMREFEKRGDGMNAYIVYKLETEVSgVVGYTKQHYETWRRFSDFLGLHGKIVEKYLAKGIVIPQPPEKSISALTKTKT 170
Cdd:cd07281   2 KVSITDPEKIGDGMNAYVVYKVTTQTS-LLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17550150 171 NSDPAMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd07281  81 GKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLEKE 124
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 91-211 1.53e-31

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: 117.46  E-value: 1.53e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  91 KVTMREFEKRGDGMNAYIVYKLETEVSGVVgYTKQHYETWRRFSDFLGLHGKIVEKYLAKGIVIPQPPEKSISALTKTKT 170
Cdd:cd07282   2 EIGVSDPEKVGDGMNAYMAYRVTTKTSLSM-FSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17550150 171 NSDPAMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFL 211
Cdd:cd07282  81 GKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 121
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 251-464 2.16e-29

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: 114.71  E-value: 2.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 251 EGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSRALSSLTDVTENVSAVYGK 330
Cdd:cd07627   1 EPDEWFIEKKQYLDSLESQLKQLYKSLELVSSQRKELASATEEFAETLEALSSLELSKSLSDLLAALAEVQKRIKESLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 331 QAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSAGGRNERSDQLKGEIEDTVQKMD 410
Cdd:cd07627  81 QALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRAS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17550150 411 QLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFE 464
Cdd:cd07627 161 ELKKEFEEVSELIKSELERFERERVEDFRNSVEIYLESAIESQKELIELWETFY 214
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 90-212 4.79e-28

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 107.66  E-value: 4.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  90 FKVTMREFEKRGDGMNAYIVYKLETEVSGVvGYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSIsaLTKTK 169
Cdd:cd06859   1 FEISVTDPVKVGDGMSAYVVYRVTTKTNLP-DFKKSEFSVLRRYSDFLWLYERLVEKY--PGRIVPPPPEKQA--VGRFK 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17550150 170 TNSDpamsrevGI-QRARQLERYICRLIQHPRMRNDCDVRDFLT 212
Cdd:cd06859  76 VKFE-------FIeKRRAALERFLRRIAAHPVLRKDPDFRLFLE 112
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 91-213 1.22e-20

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: 86.64  E-value: 1.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  91 KVTMREFEKRGDGMNAYIVYKLETEVSGvvgytKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALtktkt 170
Cdd:cd06093   1 SVSIPDYEKVKDGGKKYVVYIIEVTTQG-----GEEWTVYRRYSDFEELHEKLKKKF--PGVILPPLPPKKLFGN----- 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17550150 171 nsdpaMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTI 213
Cdd:cd06093  69 -----LDPEFIEERRKQLEQYLQSLLNHPELRNSEELKEFLEL 106
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 96-212 1.47e-20

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: 86.24  E-value: 1.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150     96 EFEKRGDGMNAYIVYKLETEVSgvvgytKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALtktktnsDPA 175
Cdd:smart00312   3 EPEKIGDGKHYYYVIEIETKTG------LEEWTVSRRYSDFLELHSKLKKHF--PRSILPPLPGKKLFGR-------LNN 67

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17550150    176 MSREVGIQRARQLERYICRLIQHPRMRNDCD-VRDFLT 212
Cdd:smart00312  68 FSEEFIEKRRRGLEKYLQSLLNHPELINHSEvVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 119-214 7.92e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 66.50  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150   119 VVGYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISaltktkTNSDPAMSREvgiqRARQLERYICRLIQH 198
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKF--PSVIIPPLPPKRWL------GRYNEEFIEK----RRKGLEQYLQRLLQH 68

                          90
                  ....*....|....*.
gi 17550150   199 PRMRNDCDVRDFLTIE 214
Cdd:pfam00787  69 PELRNSEVLLEFLESD 84
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 103-214 1.31e-13

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: 67.06  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 103 GMNAYIVYKLETEvSGVVGYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSIsaltktkTNSDPAMSREVGI 182
Cdd:cd06865  19 GGPPYISYKVTTR-TNIPSYTHGEFTVRRRFRDVVALADRLAEAY--RGAFVPPRPDKSV-------VESQVMQSAEFIE 88

                        90       100       110
                ....*....|....*....|....*....|..
gi 17550150 183 QRARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd06865  89 QRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 90-214 1.58e-11

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: 61.21  E-value: 1.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  90 FKVTMREFEKRGDGMNAYIVYKLETEVSgVVGYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALTKTk 169
Cdd:cd06861   1 FEITVGDPHKVGDLTSAHTVYTVRTRTT-SPNFEVSSFSVLRRYRDFRWLYRQLQNNH--PGVIVPPPPEKQSVGRFDD- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17550150 170 tnsdpamsrEVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd06861  77 ---------NFVEQRRAALEKMLRKIANHPVLQKDPDFRLFLESE 112
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 37-464 9.55e-11

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 63.66  E-value: 9.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  37 NEDTPPSKLRLHTTEEPKESSSPAVINSIEDHDQYVGNDNHYAQISPEPALSNFKVTMREFEKRgdgMNAYIVYKLETEV 116
Cdd:COG5391  96 SRASEFRSLRDMLSLLLPTSLQPPLSTSHTILDYFISSTVSNPQSLTLLVDSRDKHTSYEIITV---TNLPSFQLRESRP 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 117 SGVVgytkqhyetwRRFSDFLGLHGKIVEKYLakGIVIPQPPEK-SISALTKTKtnsdpaMSREVGIQRARQLERYICRL 195
Cdd:COG5391 173 LVVR----------RRYSDFESLHSILIKLLP--LCAIPPLPSKkSNSEYYGDR------FSDEFIEERRQSLQNFLRRV 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 196 IQHPRMRNDCDVRDFLTIESDL----------PKAVQTAALSSF-GVKKIFKNFQVVFSKMAFHMEEGDRWFEQVQSQVD 264
Cdd:COG5391 235 STHPLLSNYKNSKSWESHSTLLssfienrksvPTPLSLDLTSTTqELDMERKELNESTSKAIHNILSIFSLFEKILIQLE 314

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 265 ELDEALRKLytVTETLVASRRDMATSGEQLGK---------ALSMLAACEESTSLSRALSSLTDVTENVSAVYGKQAEV- 334
Cdd:COG5391 315 SEEESLTRL--LESLNNLLLLVLNFSGVFAKRleqnqnsilNEGVVQAETLRSSLKELLTQLQDEIKSRESLILTDSNLe 392

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 335 ----DNSKFSESIYEYIMLISALKDVFGERvrawqqwqDAQQTLARKRDQKTKIDLSAGGRNERSDQLKGEIEDTVQKMD 410
Cdd:COG5391 393 kltdQNLEDVEELSRSLRKNSSQRAVVSQQ--------PEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDKEKLEEQLA 464

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 17550150 411 QLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFE 464
Cdd:COG5391 465 IAEKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSVK 518
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 92-212 4.27e-10

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: 56.96  E-value: 4.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  92 VTMREFEKRGDGMNAYIVYKLETEVSGVVgYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALTKTKtn 171
Cdd:cd06860   3 ITVDNPEKHVTTLETYITYRVTTKTTRSE-FDSSEYSVRRRYQDFLWLRQKLEESH--PTHIIPPLPEKHSVKGLLDR-- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17550150 172 sdpaMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLT 212
Cdd:cd06860  78 ----FSPEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLT 114
BAR_SNX7_30 cd07624
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ...
 256-466 6.16e-10

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


Pssm-ID: 153308  Cd Length: 200  Bit Score: 58.55  E-value: 6.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 256 FEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEesTSLSRALSSLTDVTENVSAVYGKQAEVD 335
Cdd:cd07624  16 FDKMNEYLTLFGEKLGTIERISQRIHKERIEYFDELKEYSPIFQLWSASE--TELAPLLEGVSSAVERCTAALEVLLSDH 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 336 NSKFSESIYEYIMLISALKDVFgervrawqqwqdaqqtlaRKRDQ-KTKIDLSAGGRNERSDQLKGEIEDTvqkMDQLEQ 414
Cdd:cd07624  94 EFVFLPPLREYLLYSDAVKDVL------------------KRRDQfQIEYELSVEELNKKRLELLKEVEKL---QDKLEC 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17550150 415 hfieLSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPE 466
Cdd:cd07624 153 ----ANADLKADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEEVLPA 200
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 113-211 1.87e-09

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: 54.95  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 113 ETEVSGVVGYTKQH--YETWRRFSDFLGLHGKIVEKYLAkgIVIPQPPEK-SI--SALTKTKTNSDPAMSRevgiQRARQ 187
Cdd:cd06867  12 EGGSGSYIVYVIRLggSEVKRRYSEFESLRKNLTRLYPT--LIIPPIPEKhSLkdYAKKPSKAKNDAKIIE----RRKRM 85

                        90       100
                ....*....|....*....|....
gi 17550150 188 LERYICRLIQHPRMRNDCDVRDFL 211
Cdd:cd06867  86 LQRFLNRCLQHPILRNDIVFQKFL 109
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 90-214 3.45e-09

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: 54.68  E-value: 3.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  90 FKVTMREFEKR--GDGMN---AYIVYKLET---EVSGVVGYTKQHYETWRRFSDFLGLHGKIVEKYLAkgIVIPQPPEKS 161
Cdd:cd06864   1 MEITVTEAEKRtgGSAMNlkeTYTVYLIETkivEHESEEGLSKKLSSLWRRYSEFELLRNYLVVTYPY--VIVPPLPEKR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17550150 162 ISALTK--TKTNSDPAMsrevgIQRARQ-LERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd06864  79 AMFMWQklSSDTFDPDF-----VERRRAgLENFLLRVAGHPELCQDKIFLEFLTHE 129
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 103-216 7.61e-08

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: 50.78  E-value: 7.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 103 GMNAYIVYKLETEVSGVvgytkqhyETWRRFSDFLGLHGKIVEKYLAkgIVIPQPPEKSISAltktKTNSDPAMSREVgi 182
Cdd:cd06862  16 GLKSFIAYQITPTHTNV--------TVSRRYKHFDWLYERLVEKYSC--IAIPPLPEKQVTG----RFEEDFIEKRRE-- 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17550150 183 qrarQLERYICRLIQHPRMRnDCDV-RDFLTIESD 216
Cdd:cd06862  80 ----RLELWMNRLARHPVLS-QSEVfRHFLTCTDE 109
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 106-211 2.55e-07

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: 49.25  E-value: 2.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 106 AYIVYKLETEVSGVVGYTKQHYetwRRFSDFLGLHGKIVEKY-LAKGIVIPQPPEKSISALTKTKtnsdpaMSREVGIQR 184
Cdd:cd07280  21 AYVVWKITIETKDLIGSSIVAY---KRYSEFVQLREALLDEFpRHKRNEIPQLPPKVPWYDSRVN------LNKAWLEKR 91

                        90       100
                ....*....|....*....|....*..
gi 17550150 185 ARQLERYICRLIQHPRMRNDCDVRDFL 211
Cdd:cd07280  92 RRGLQYFLNCVLLNPVFGGSPVVKEFL 118
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 92-212 2.73e-06

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: 46.12  E-value: 2.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  92 VTMREFEKRGDGMNAYIVYKLETEVSGVvGYTKQHYETWRRFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALTKTKTN 171
Cdd:cd07284   3 ITVDEPESHVTAIETFITYRVMTKTSRS-EFDSSEFEVRRRYQDFLWLKGRLEEAH--PTLIIPPLPEKFVMKGMVERFN 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17550150 172 SDPAMSREvgiqraRQLERYICRLIQHPRMRNDCDVRDFLT 212
Cdd:cd07284  80 EDFIETRR------KALHKFLNRIADHPTLTFNEDFKIFLT 114
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 263-466 4.73e-06

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


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 47.05  E-value: 4.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 263 VDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAAC---EESTSLSRALSSLTDVTENVSAVYGKQAEVDNSKF 339
Cdd:cd07307   2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKElpdLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 340 SESIYEYIMliSALKDVfgervrawqqwqdaqqTLARKRDQKTKID----LSAGGRNERSDQLKGEIEDTVQKMDQLEQH 415
Cdd:cd07307  82 IEPLKEYLK--KDLKEI----------------KKRRKKLDKARLDydaaREKLKKLRKKKKDSSKLAEAEEELQEAKEK 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17550150 416 FIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPE 466
Cdd:cd07307 144 YEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 131-212 5.16e-06

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: 44.91  E-value: 5.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 131 RRFSDFLGLHGKIVEKYLAKgiVIPQPPEKSISALtktktnsdpaMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDF 210
Cdd:cd06866  34 RRYSDFVWLHEYLLKRYPYR--MVPALPPKRIGGS----------ADREFLEARRRGLSRFLNLVARHPVLSEDELVRTF 101


                ..
gi 17550150 211 LT 212
Cdd:cd06866 102 LT 103
BAR_Atg24p cd07628
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg24p; BAR domains are ...
 251-466 4.01e-05

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


Pssm-ID: 153312  Cd Length: 185  Bit Score: 44.18  E-value: 4.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 251 EGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEEStslsralssltDVTENVSavygk 330
Cdd:cd07628   1 KPDKEFLEIREKSDKLDENLTKIDKIFAKVVKRQSDLSVDYADLATQFQKLGSLESG-----------EITEPFK----- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 331 qaevdnsKFSESIYEYIMLISALKDVFGE----RVRAWQQWQDAQQTLARKRDQKtKIDLSaggrnERSDQLKGEIEDTV 406
Cdd:cd07628  65 -------IFSESLSQFSTSLRVLNKYTDEnyltSLKDLLHYILSLKNLIKLRDQK-QLDYE-----ELSDYLLTDEVENA 131

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 407 QKMDQLeqhfieLSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPE 466
Cdd:cd07628 132 KETSDA------FNKEVLKEYPNFERIKKQEIKDSLGALADGHIDFYQGLVEDWEKVEPK 185
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 91-196 9.80e-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: 41.98  E-value: 9.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  91 KVTMREFEKRGDGMNAYIVYKLETEVSGvvgytkqhyETW---RRFSDFLGLHGKIVEKYLAKGiVIPQPPEKSISAltk 167
Cdd:cd06874   2 KITIPRYVLRGQGKDEHFEFEVKITVLD---------ETWtvfRRYSRFRELHKTMKLKYPEVA-ALEFPPKKLFGN--- 68

                        90       100
                ....*....|....*....|....*....
gi 17550150 168 tktnsdpaMSREVGIQRARQLERYICRLI 196
Cdd:cd06874  69 --------KSERVAKERRRQLETYLRNFF 89
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 132-211 1.81e-04

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: 40.78  E-value: 1.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 132 RFSDFLGLHGKIVEKYlaKGIVIPQPPEKSISALTKTKTNsdpamsrevgiQRARQLERYICRLIQHPRMRNDCDVRDFL 211
Cdd:cd06885  34 RYSQLHGLNEQLKKEF--GNRKLPPFPPKKLLPLTPAQLE-----------ERRLQLEKYLQAVVQDPRIANSDIFNSFL 100
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
 249-447 2.75e-04

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: 42.23  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 249 MEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAAcEESTSLSRALSSLTDVTENVSAVY 328
Cdd:cd07663  18 VKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAA-EEPTVIKKYLLKVAELFEKLRKVE 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 329 GKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSAGGRnersdqlkgeiEDTVQK 408
Cdd:cd07663  97 DRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQ-----------QECCQK 165

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17550150 409 MDQleqhfieLSKAIREEVARFDADRKQDMKKMLVEYME 447
Cdd:cd07663 166 FEK-------LSESAKQELISFKRRRVAAFRKNLIEMTE 197
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 105-211 4.15e-04

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: 39.56  E-value: 4.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 105 NAYIVYKLETEVSGVVgytkqhYETWRRFSDFLGLHgKIVEKYLakGIVIPQP-PEKSISaltkTKTNSDPAMSREvgiq 183
Cdd:cd06897  13 KPYTVYNIQVRLPLRS------YTVSRRYSEFVALH-KQLESEV--GIEPPYPlPPKSWF----LSTSSNPKLVEE---- 75

                        90       100       110
                ....*....|....*....|....*....|
gi 17550150 184 RARQLERYICRLIQHP--RMRNDCDVRDFL 211
Cdd:cd06897  76 RRVGLEAFLRALLNDEdsRWRNSPAVKEFL 105
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 101-212 5.57e-04

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: 39.58  E-value: 5.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 101 GDGMNAYIVYKLETEVSGVVgYTKQHYETWRRFSDFLGLHGKIVEKYLAkgIVIPQPPEKSisaltKTKTNSDPAMSREV 180
Cdd:cd06863  13 DGSSDTYISYLITTKTNLPS-FSRKEFKVRRRYSDFVFLHECLSNDFPA--CVVPPLPDKH-----RLEYITGDRFSPEF 84

                        90       100       110
                ....*....|....*....|....*....|..
gi 17550150 181 GIQRARQLERYICRLIQHPRMRNDCDVRDFLT 212
Cdd:cd06863  85 ITRRAQSLQRFLRRISLHPVLSQSKILHQFLE 116
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 98-211 1.16e-03

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: 38.96  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  98 EKRGdgMNAYIVYKLETEVSGvvgytKQHYETWRRFSDFLGLHGKIVEKYlakgivipqPPEKSISALTKTKTNSDPAM- 176
Cdd:cd06882  13 EKRG--FTNYYVFVIEVKTKG-----GSKYLIYRRYRQFFALQSKLEERF---------GPEAGSSAYDCTLPTLPGKIy 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17550150 177 ---SREVGIQRARQLERYICRLIQ-HPRMRNDCDVRDFL 211
Cdd:cd06882  77 vgrKAEIAERRIPLLNRYMKELLSlPVWVLMDEDVRLFF 115
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 128-211 1.38e-03

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: 38.40  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 128 ETW---RRFSDFLGLHGKIVEKYlakgivipqpPEKSISALTKTKTNSDpaMSREVGIQRARQLERYICRLIQ------H 198
Cdd:cd06873  39 ESWhvyRRYSDFHDLHMRLKEKF----------PNLSKLSFPGKKTFNN--LDRAFLEKRRKMLNQYLQSLLNpevldaN 106

                        90
                ....*....|...
gi 17550150 199 PRMRNdcDVRDFL 211
Cdd:cd06873 107 PGLQE--IVLDFL 117
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 129-212 1.69e-03

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 38.44  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 129 TW---RRFSDFLGLHGKIVEKYLAKGIVIpqPPEKSISALTKTKTNsdpamsreVGIQRARQLERYICRLIQHPRMRNDC 205
Cdd:cd06876  56 GWvvaRRYSEFLELHKYLKKRYPGVLKLD--FPQKRKISLKYSKTL--------LVEERRKALEKYLQELLKIPEVCEDE 125


                ....*..
gi 17550150 206 DVRDFLT 212
Cdd:cd06876 126 EFRKFLS 132
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 107-214 2.13e-03

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


Pssm-ID: 132809  Cd Length: 110  Bit Score: 37.77  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150 107 YIVYKLETEvsgvvgytKQHYETW---RRFSDFLGLHGKIveKYLAKGIVIPQPPEKSIsaltktKTNSDPAMSREvgiq 183
Cdd:cd07276  20 FTVYKIRVE--------NKVGDSWfvfRRYTDFVRLNDKL--KQMFPGFRLSLPPKRWF------KDNFDPDFLEE---- 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 17550150 184 RARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd07276  80 RQLGLQAFVNNIMAHKDIAKCKLVREFFCLD 110
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 92-214 7.58e-03

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: 36.59  E-value: 7.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  92 VTMREFEKRGDGMNAYIVyKLETEVSGVVGYTKQHYETWRRFSDFLGLHGKIVEkYLAKGIVIPQPPEKSISAltktktn 171
Cdd:cd06877  10 VEMRRDPSNGERIYVFCI-EVERNDRRAKGHEPQHWSVLRRYNEFYVLESKLTE-FHGEFPDAPLPSRRIFGP------- 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17550150 172 sdpaMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTIE 214
Cdd:cd06877  81 ----KSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSPN 119
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 98-211 8.46e-03

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: 36.75  E-value: 8.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550150  98 EKRGDGMNAYIVYKLETEVSGVVGYTKQHYETW----------RRFSDFLGLHGKIVEKYLAKGIVIPQPPEKSISALTK 167
Cdd:cd06893  12 EYKGTGTHPYTLYTVQYETILDVQSEQNPNAASeqplathtvnRRFREFLTLQTRLEENPKFRKIMNVKGPPKRLFDLPF 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17550150 168 TKTNSDPAMSREvgiqraRQLERYICRLIQHPRMRNDCDVRDFL 211
Cdd:cd06893  92 GNMDKDKIEARR------GLLETFLRQLCSIPEISNSEEVQEFL 129
 
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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