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Conserved domains on  [gi|1778901291|ref|NP_001363847|]
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nischarin isoform 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 15-130 3.21e-62

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: 199.04  E-value: 3.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  15 EPAKEARVVGSELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTLLPPKKIIGKNSRSLVEKREKDLE 94
Cdd:cd06875     1 EPETKIRIPSAETVEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDLLPPKKLIGNKSPSFVEKRRKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1778901291  95 VYLQTLLKTFPDVAPRVLAHFLHFHLYEINGVTAAL 130
Cdd:cd06875    81 IYLQTLLSFFQKTMPRELAHFLDFHKYEIIGLTQNL 116
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
282-418 1.01e-22

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.39  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 282 AVIPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGVLVV-DNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKT 360
Cdd:COG4886   153 EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLET 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1778901291 361 LNLAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEvksIGNLPCLEHVALLNNPLSII 418
Cdd:COG4886   233 LDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPP---LANLTNLKTLDLSNNQLTDL 287
 
Name Accession Description Interval E-value
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 15-130 3.21e-62

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: 199.04  E-value: 3.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  15 EPAKEARVVGSELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTLLPPKKIIGKNSRSLVEKREKDLE 94
Cdd:cd06875     1 EPETKIRIPSAETVEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDLLPPKKLIGNKSPSFVEKRRKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1778901291  95 VYLQTLLKTFPDVAPRVLAHFLHFHLYEINGVTAAL 130
Cdd:cd06875    81 IYLQTLLSFFQKTMPRELAHFLDFHKYEIIGLTQNL 116
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
282-418 1.01e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.39  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 282 AVIPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGVLVV-DNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKT 360
Cdd:COG4886   153 EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLET 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1778901291 361 LNLAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEvksIGNLPCLEHVALLNNPLSII 418
Cdd:COG4886   233 LDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPP---LANLTNLKTLDLSNNQLTDL 287
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 290-425 2.92e-20

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 89.46  E-value: 2.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 290 LTTLDLSHNSISEIdESVKLIPKIEYLDLSHNGVLVVDNLQHLYNLVHLDLSYNKLSSLEG-------VHTKLGNVKTLN 362
Cdd:cd21340    48 LTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPPGEKltfdprsLAALSNSLRVLN 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778901291 363 LAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEVK-SIGNLPCLEHVALLNNPLSIIPDYRTKV 425
Cdd:cd21340   127 ISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLdLLSSWPSLRELDLTGNPVCKKPKYRDKI 190
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 25-117 6.40e-19

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: 82.01  E-value: 6.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291   25 SELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKiDKTL--LPPKKIIG---KNSRSLVEKREKDLEVYLQT 99
Cdd:smart00312   8 GDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFP-RSILppLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQS 86

                           90
                   ....*....|....*....
gi 1778901291  100 LLKTFPDVAP-RVLAHFLH 117
Cdd:smart00312  87 LLNHPELINHsEVVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 37-119 8.76e-16

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 72.27  E-value: 8.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  37 QVTDGNHEWTIKHRYSDFHDLHEKLvaERKIDKTL---LPPKKIIGKNSRSLVEKREKDLEVYLQTLLKTFPDVAPRVLA 113
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKL--LRKFPSVIippLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLL 78


                  ....*.
gi 1778901291 114 HFLHFH 119
Cdd:pfam00787  79 EFLESD 84
LRR_8 pfam13855
Leucine rich repeat;
311-366 4.62e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 4.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1778901291 311 PKIEYLDLSHNGVLVVD--NLQHLYNLVHLDLSYNKLSSLEGVH-TKLGNVKTLNLAGN 366
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDdgAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGN 59
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 290-388 2.46e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.07  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 290 LTTLDLSHNSISE-IDESVKLIPKIEYLDLSHNGV--LVVDNLQHLYNLVHLDLSYNKLS-SLEGVHTKLGNVKTLNLAG 365
Cdd:PLN00113  477 LENLDLSRNQFSGaVPRKLGSLSELMQLKLSENKLsgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQ 556

                          90       100
                  ....*....|....*....|....*...
gi 1778901291 366 NfleRLSG-----LHKLYSLVNLDLRDN 388
Cdd:PLN00113  557 N---QLSGeipknLGNVESLVQVNISHN 581
 
Name Accession Description Interval E-value
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 15-130 3.21e-62

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: 199.04  E-value: 3.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  15 EPAKEARVVGSELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTLLPPKKIIGKNSRSLVEKREKDLE 94
Cdd:cd06875     1 EPETKIRIPSAETVEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDLLPPKKLIGNKSPSFVEKRRKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1778901291  95 VYLQTLLKTFPDVAPRVLAHFLHFHLYEINGVTAAL 130
Cdd:cd06875    81 IYLQTLLSFFQKTMPRELAHFLDFHKYEIIGLTQNL 116
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
282-418 1.01e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.39  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 282 AVIPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGVLVV-DNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKT 360
Cdd:COG4886   153 EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLET 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1778901291 361 LNLAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEvksIGNLPCLEHVALLNNPLSII 418
Cdd:COG4886   233 LDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPP---LANLTNLKTLDLSNNQLTDL 287
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
284-420 1.27e-21

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 96.93  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 284 IPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGVLVVDN-LQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKTLN 362
Cdd:COG4886   132 LANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEeLGNLTNLKELDLSNNQITDLPEPLGNLTNLEELD 211

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1778901291 363 LAGNFLERLS-GLHKLYSLVNLDLRDNRIEQLDEvksIGNLPCLEHVALLNNPLSIIPD 420
Cdd:COG4886   212 LSGNQLTDLPePLANLTNLETLDLSNNQLTDLPE---LGNLTNLEELDLSNNQLTDLPP 267
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 26-116 5.96e-21

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


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 87.80  E-value: 5.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  26 ELVDTYTVYVIQVTD-GNHEWTIKHRYSDFHDLHEKLVaERKIDKTL--LPPKKIIGKNSRSLVEKREKDLEVYLQTLLK 102
Cdd:cd06093    12 DGGKKYVVYIIEVTTqGGEEWTVYRRYSDFEELHEKLK-KKFPGVILppLPPKKLFGNLDPEFIEERRKQLEQYLQSLLN 90

                          90
                  ....*....|....
gi 1778901291 103 TFPDVAPRVLAHFL 116
Cdd:cd06093    91 HPELRNSEELKEFL 104
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 290-425 2.92e-20

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 89.46  E-value: 2.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 290 LTTLDLSHNSISEIdESVKLIPKIEYLDLSHNGVLVVDNLQHLYNLVHLDLSYNKLSSLEG-------VHTKLGNVKTLN 362
Cdd:cd21340    48 LTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPPGEKltfdprsLAALSNSLRVLN 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778901291 363 LAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEVK-SIGNLPCLEHVALLNNPLSIIPDYRTKV 425
Cdd:cd21340   127 ISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLdLLSSWPSLRELDLTGNPVCKKPKYRDKI 190
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
284-420 1.00e-19

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.53  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 284 IPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGV-LVVDNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKTLN 362
Cdd:COG4886   109 LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLtDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELD 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1778901291 363 LAGNFLERLSG-LHKLYSLVNLDLRDNRIEQLDEvkSIGNLPCLEHVALLNNPLSIIPD 420
Cdd:COG4886   189 LSNNQITDLPEpLGNLTNLEELDLSGNQLTDLPE--PLANLTNLETLDLSNNQLTDLPE 245
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 25-117 6.40e-19

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: 82.01  E-value: 6.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291   25 SELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKiDKTL--LPPKKIIG---KNSRSLVEKREKDLEVYLQT 99
Cdd:smart00312   8 GDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFP-RSILppLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQS 86

                           90
                   ....*....|....*....
gi 1778901291  100 LLKTFPDVAP-RVLAHFLH 117
Cdd:smart00312  87 LLNHPELINHsEVVLEFLE 105
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 29-113 5.62e-16

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: 73.92  E-value: 5.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  29 DTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTL-LPPKKIIGKNSRSLVEKREKDLEVYLQTLLKTFPDV 107
Cdd:cd07277    16 DAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFdFPPKKAIGNKDAKFVEERRKRLQVYLRRVVNTLIQT 95


                  ....*.
gi 1778901291 108 APRVLA 113
Cdd:cd07277    96 SPELTA 101
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 37-119 8.76e-16

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 72.27  E-value: 8.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  37 QVTDGNHEWTIKHRYSDFHDLHEKLvaERKIDKTL---LPPKKIIGKNSRSLVEKREKDLEVYLQTLLKTFPDVAPRVLA 113
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKL--LRKFPSVIippLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLL 78


                  ....*.
gi 1778901291 114 HFLHFH 119
Cdd:pfam00787  79 EFLESD 84
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 21-119 2.17e-14

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: 69.23  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  21 RVVGSELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLvaeRKIDKTL-LPPKKIIGKNSRSLvEKREKDLEVYLQT 99
Cdd:cd06880     9 RLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKL---KKSIKTPdFPPKRVRNWNPKVL-EQRRQGLEAYLQG 84

                          90       100
                  ....*....|....*....|...
gi 1778901291 100 LLKtFPDVaPRVLAHFL---HFH 119
Cdd:cd06880    85 LLK-INEL-PKQLLDFLgvrHFP 105
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 30-116 2.23e-14

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: 69.60  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  30 TYTVYVIQVT----DGNHE-WTIKHRYSDFHDLHEKLVaER--KIDKTLLPPKKIIGKNSRSLVEKREKDLEVYLQTLL- 101
Cdd:cd06873    21 TYAVYAISVTriypNGQEEsWHVYRRYSDFHDLHMRLK-EKfpNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYLQSLLn 99

                          90
                  ....*....|....*....
gi 1778901291 102 ----KTFPDVAPrVLAHFL 116
Cdd:cd06873   100 pevlDANPGLQE-IVLDFL 117
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
290-420 4.09e-14

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.20  E-value: 4.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 290 LTTLDLSHNSISEIDESVKLIPKIEYLDLSHNgvlvvDNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKTLNLAGNFLE 369
Cdd:COG4886    75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLT 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1778901291 370 RL-SGLHKLYSLVNLDLRDNRIEQLDEvkSIGNLPCLEHVALLNNPLSIIPD 420
Cdd:COG4886   150 DLpEPLGNLTNLKSLDLSNNQLTDLPE--ELGNLTNLKELDLSNNQITDLPE 199
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 25-118 5.67e-13

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: 64.99  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  25 SELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLvaERKIDKTL---LPPKKII--GKNSRSLVEKREKDLEVYLQT 99
Cdd:cd06897     9 SVSPKPYTVYNIQVRLPLRSYTVSRRYSEFVALHKQL--ESEVGIEPpypLPPKSWFlsTSSNPKLVEERRVGLEAFLRA 86

                          90
                  ....*....|....*....
gi 1778901291 100 LLKTfPDVAPRVLAHFLHF 118
Cdd:cd06897    87 LLND-EDSRWRNSPAVKEF 104
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 24-101 2.50e-11

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: 60.84  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  24 GSELVDTYTVYVIQVTDG---NHEWTIKHRYSDFHDLHEKL-VAERKIdktLLPPKKIIGKNSRSLVEKREKDLEVYLQT 99
Cdd:cd06871    14 ASQNIQSHTEYIIRVQRGpspENSWQVIRRYNDFDLLNASLqISGISL---PLPPKKLIGNMDREFIAERQQGLQNYLNV 90


                  ..
gi 1778901291 100 LL 101
Cdd:cd06871    91 IL 92
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 31-107 4.64e-11

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: 60.40  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  31 YTVYVIQVT--DGNHE---WTIKHRYSDFHDLHEKLVAE-RKIDKTLLPPKKIIGKN--SRSLVEKREKDLEVYLQTLLK 102
Cdd:cd06876    38 FVVYLIEVQrlNNDDQssgWVVARRYSEFLELHKYLKKRyPGVLKLDFPQKRKISLKysKTLLVEERRKALEKYLQELLK 117


                  ....*
gi 1778901291 103 tFPDV 107
Cdd:cd06876   118 -IPEV 121
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
 20-101 7.39e-11

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 59.07  E-value: 7.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  20 ARVVGSELV----DTYTVYVIQVTD-GNHEWTIKHRYSDFHDLHEKLvaeRKIDKTLL--PPKKIIGKN-SRSLVEKREK 91
Cdd:cd06872     3 CRVLGAEIVksgsKSFAVYSVAVTDnENETWVVKRRFRNFETLHRRL---KEVPKYNLelPPKRFLSSSlDGAFIEERCK 79

                          90
                  ....*....|
gi 1778901291  92 DLEVYLQTLL 101
Cdd:cd06872    80 LLDKYLKDLL 89
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 31-107 1.03e-09

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: 55.88  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  31 YTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTLLPPKKIIGKN-SRSLVEKREKDLEVYLQTL-----LKTF 104
Cdd:cd06870    20 FTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPASNLKIPGKRLFGNNfDPDFIKQRRAGLDEFIQRLvsdpkLLNH 99


                  ...
gi 1778901291 105 PDV 107
Cdd:cd06870   100 PDV 102
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 29-103 2.09e-09

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: 55.47  E-value: 2.09e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778901291  29 DTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTL-LPPKKIIGKNSRSLVEKREKDLEVYLQTLLKT 103
Cdd:cd06874    16 DEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALeFPPKKLFGNKSERVAKERRRQLETYLRNFFSV 91
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
284-450 8.16e-09

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.64  E-value: 8.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 284 IPTWQALTTLDLSHNSISEIDESVKLiPKIEYLDLSHNGVLVVDNLQHLYNLVHLDLSYNKLSSLE-GVHTKLGNVKTLN 362
Cdd:COG4886   224 LANLTNLETLDLSNNQLTDLPELGNL-TNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKlKELELLLGLNSLL 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 363 LAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEVKSIGNLPCLEHVALLNNPLSIIPDYRTKVLSQFGERASEICLDDVA 442
Cdd:COG4886   303 LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTL 382


                  ....*...
gi 1778901291 443 TTEKELDT 450
Cdd:COG4886   383 ALLLLTLL 390
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 29-102 1.28e-08

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: 53.15  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  29 DTYTVYVIQV-----TDGNHE---WTIKHRYSDFHDLHEKLVaERKIDK--TLLPPKKIIGKNSRSLVEKREKDLEVYLQ 98
Cdd:cd06877    20 ERIYVFCIEVerndrRAKGHEpqhWSVLRRYNEFYVLESKLT-EFHGEFpdAPLPSRRIFGPKSYEFLESKREIFEEFLQ 98


                  ....
gi 1778901291  99 TLLK 102
Cdd:cd06877    99 KLLQ 102
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 15-114 1.46e-08

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: 52.58  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  15 EPAKearvVGsELVDTYTVY-VIQVTDGNH----EWTIKHRYSDFHDLHEKLVAERKidKTLLPP---KKIIG--KNSRS 84
Cdd:cd06859     7 DPVK----VG-DGMSAYVVYrVTTKTNLPDfkksEFSVLRRYSDFLWLYERLVEKYP--GRIVPPppeKQAVGrfKVKFE 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1778901291  85 LVEKREKDLEVYLQtllktfpdvapRVLAH 114
Cdd:cd06859    80 FIEKRRAALERFLR-----------RIAAH 98
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 26-100 3.31e-07

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: 48.48  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  26 ELVD----TYTVYVIQVtDGNHEWTIkhRYSDFHDLHEKLVAERKIDKT-LLPPKKIIGKNSRSLVEKREKdLEVYLQTL 100
Cdd:cd06885     9 ELSDeggsTYVAYNIHI-NGVLHCSV--RYSQLHGLNEQLKKEFGNRKLpPFPPKKLLPLTPAQLEERRLQ-LEKYLQAV 84
LRR_8 pfam13855
Leucine rich repeat;
311-366 4.62e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 4.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1778901291 311 PKIEYLDLSHNGVLVVD--NLQHLYNLVHLDLSYNKLSSLEGVH-TKLGNVKTLNLAGN 366
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDdgAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGN 59
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 290-390 4.85e-07

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 52.10  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 290 LTTLDLSHNSISE-----IDESVKLIPKIEYLDLSHN-----GVLV-VDNLQHLYNLVHLDLSYNKLSSLEGV----HTK 354
Cdd:COG5238   266 VETLYLSGNQIGAegaiaLAKALQGNTTLTSLDLSVNrigdeGAIAlAEGLQGNKTLHTLNLAYNGIGAQGAIalakALQ 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1778901291 355 LG-NVKTLNLAGNFL--ERLSGLHKLY----SLVNLDLRDNRI 390
Cdd:COG5238   346 ENtTLHSLDLSDNQIgdEGAIALAKYLegntTLRELNLGKNNI 388
LRR_8 pfam13855
Leucine rich repeat;
290-345 1.02e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.98  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1778901291 290 LTTLDLSHNSISEIDESV-KLIPKIEYLDLSHNGVLVVDN--LQHLYNLVHLDLSYNKL 345
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
PX_Bem1p cd06890
The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a ...
 18-107 1.10e-06

The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. 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 Bem1p specifically binds phosphatidylinositol-4-phosphate (PI4P).


Pssm-ID: 132800  Cd Length: 112  Bit Score: 47.28  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  18 KEARVVGSELVDTYTVYVIQVTDGNHEWTIKHR-YSDFHDLHEKLV------AERKIDKTLLP--PKKIIGKNSRSLVEK 88
Cdd:cd06890     1 VSASVESVLLEDNRYWYRVRATLSDGKTRYLCRyYQDFYKLHIALLdlfpaeAGRNSSKRILPylPGPVTDVVNDSISLK 80

                          90
                  ....*....|....*....
gi 1778901291  89 REKDLEVYLQTLLKTFPDV 107
Cdd:cd06890    81 RLNDLNEYLNELINLPAYI 99
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
 19-108 2.36e-06

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: 46.20  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  19 EARVVGSE---LVDTYTVYVIQVT-DGNHEWT-IKHRYSDFHDLHEKLvaeRKIDKTL----LPPKKIIGK-NSRSLVEK 88
Cdd:cd06883     1 EVSVFGFQkrySPEKYYIYVVKVTrENQTEPSfVFRTFEEFQELHNKL---SLLFPSLklpsFPARVVLGRsHIKQVAER 77

                          90       100
                  ....*....|....*....|
gi 1778901291  89 REKDLEVYLQTLLKTFPDVA 108
Cdd:cd06883    78 RKIELNSYLKSLFNASPEVA 97
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 289-390 2.36e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 49.79  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 289 ALTTLDLSHNSIS-----EIDESVKLIPKIEYLDLSHNGV------LVVDNLQHLYNLVHLDLSYNKLS---------SL 348
Cdd:COG5238   237 SLTTLDLSNNQIGdegviALAEALKNNTTVETLYLSGNQIgaegaiALAKALQGNTTLTSLDLSVNRIGdegaialaeGL 316

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1778901291 349 EGVHTklgnVKTLNLAGNFL-----ERL-SGLHKLYSLVNLDLRDNRI 390
Cdd:COG5238   317 QGNKT----LHTLNLAYNGIgaqgaIALaKALQENTTLHSLDLSDNQI 360
PX_PLD cd06895
The phosphoinositide binding Phox Homology domain of Phospholipase D; The PX domain is a ...
 20-102 2.49e-06

The phosphoinositide binding Phox Homology domain of Phospholipase D; 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. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. Members of this subfamily contain PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. Vertebrates contain two PLD isozymes, PLD1 and PLD2. PLD1 is located mainly in intracellular membranes while PLD2 is associated with plasma membranes. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132805  Cd Length: 140  Bit Score: 46.99  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  20 ARVVGSELVDTY------TVYVIQVTDGNHEWTIKHRYSDFHDLHEKL---------------------------VAERK 66
Cdd:cd06895     6 ARITDVERSGTTrhllnpNLYTIELQHGQFTWTIKRRYKHFQELHQALklyrallriplptrrhkeerlslkrsrKPERE 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1778901291  67 IDKTLLP--PKKIIGKNSRSLVEKREKDLEVYLQTLLK 102
Cdd:cd06895    86 KKNRRLPslPALPDILVSEEQLDSRKKQLENYLQNLLK 123
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 289-416 4.09e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 48.89  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 289 ALTTLDLSHNSISE----IDESVKLIPKIEYLDLSHNGV------LVVDNLQHLY-NLVHLDLSYNKLSS-----LEGVH 352
Cdd:cd00116    82 GLQELDLSDNALGPdgcgVLESLLRSSSLQELKLNNNGLgdrglrLLAKGLKDLPpALEKLVLGRNRLEGasceaLAKAL 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778901291 353 TKLGNVKTLNLAGNFLeRLSGLHKLY-------SLVNLDLRDNRIE-----QLDEVksIGNLPCLEHVALLNNPLS 416
Cdd:cd00116   162 RANRDLKELNLANNGI-GDAGIRALAeglkancNLEVLDLNNNGLTdegasALAET--LASLKSLEVLNLGDNNLT 234
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 31-101 4.12e-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: 45.89  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  31 YTVYVIQV-TDGNHEWTIKHRYSDFHDLHEKLVA----ERKI---DKTL--LPPKKIIGkNSRSLVEKREKDLEVYLQTL 100
Cdd:cd06882    20 YYVFVIEVkTKGGSKYLIYRRYRQFFALQSKLEErfgpEAGSsayDCTLptLPGKIYVG-RKAEIAERRIPLLNRYMKEL 98


                  .
gi 1778901291 101 L 101
Cdd:cd06882    99 L 99
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 44-107 1.73e-05

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: 44.28  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  44 EWTIKHRYSDFHDLHEKLVAERKIDKTLLPP---KKIIG----------KNSRSLVEKREKDLEVYLQ------TLLKTf 104
Cdd:cd07282    36 EFSVRRRFSDFLGLHSKLASKYLHVGYIVPPapeKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQrtvkhpTLLQD- 114


                  ...
gi 1778901291 105 PDV 107
Cdd:cd07282   115 PDL 117
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 28-107 2.62e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 43.89  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  28 VDTYTVYVIQVTDG-----NHEWTIKHRYSDFHDLHEKLVAERKIDKTLLPP---KKIIG----------KNSRSLVEKR 89
Cdd:cd07281    15 MNAYVVYKVTTQTSllmfrSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPppeKSLIGmtkvkvgkedSSSAEFLERR 94

                          90       100
                  ....*....|....*....|....
gi 1778901291  90 EKDLEVYLQ------TLLKTfPDV 107
Cdd:cd07281    95 RAALERYLQrivshpSLLQD-PDV 117
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 31-97 3.07e-05

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: 42.99  E-value: 3.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  31 YTVYviQVTDGNHEWTIKHRYSDFHDLHEKLVAE---RKIdkTLLPPKKIIGKNSRSLVEKREKDLEVYL 97
Cdd:cd06866    18 HVEY--EVSSKRFKSTVYRRYSDFVWLHEYLLKRypyRMV--PALPPKRIGGSADREFLEARRRGLSRFL 83
LRR_9 pfam14580
Leucine-rich repeat;
303-429 4.68e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 43.98  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 303 IDESVKLIPKIE--YLDLSHNGVLVVDNL-QHLYNLVHLDLSYNKLSSLEGVhTKLGNVKTLNLAGNFLERLS-GLHK-L 377
Cdd:pfam14580   9 IEQSAQYTNPVRerELDLRGYKIPIIENLgATLDQFDTIDFSDNEIRKLDGF-PLLRRLKTLLLNNNRICRIGeGLGEaL 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1778901291 378 YSLVNLDLRDNRIEQLDEVKSIGNLPCLEHVALLNNPLSIIPDYRTKVLSQF 429
Cdd:pfam14580  88 PNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKV 139
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 14-97 5.57e-05

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: 42.69  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  14 AEPAKEARVVGSElvdTYTVYviQVTDGNHEWTIKHRYSDFHDLHEKLVAerKIDKTLLPP---KKIIGKNSRSLVEKRE 90
Cdd:cd06862     6 TNPKKESKFKGLK---SFIAY--QITPTHTNVTVSRRYKHFDWLYERLVE--KYSCIAIPPlpeKQVTGRFEEDFIEKRR 78


                  ....*..
gi 1778901291  91 KDLEVYL 97
Cdd:cd06862    79 ERLELWM 85
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 22-101 5.78e-05

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: 42.40  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  22 VVGSELVDT---YTVYVIQVTDGNHE-WTIKHRYSDFHDLHEKLVAERKIDKTLLPPKKIIGKN-SRSLVEKREKDLEVY 96
Cdd:cd07276     8 ILGYEVMEErarFTVYKIRVENKVGDsWFVFRRYTDFVRLNDKLKQMFPGFRLSLPPKRWFKDNfDPDFLEERQLGLQAF 87


                  ....*
gi 1778901291  97 LQTLL 101
Cdd:cd07276    88 VNNIM 92
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 290-334 5.93e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 40.31  E-value: 5.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1778901291 290 LTTLDLSHNSISEIDESVKLiPKIEYLDLSHNGVLvvDNLQHLYN 334
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKL-PNLETLDLSGNNKI--TDLSDLAN 44
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 14-118 9.57e-05

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: 42.36  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  14 AEPAKEARVVGSELVDTYTVYVIQVTDGNHEWTIK---------HRYSDFHDLHEKLVAerKIDKTLLPP---KKI--IG 79
Cdd:cd06864     6 TEAEKRTGGSAMNLKETYTVYLIETKIVEHESEEGlskklsslwRRYSEFELLRNYLVV--TYPYVIVPPlpeKRAmfMW 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1778901291  80 KNSRS------LVEKREKDLEVYLQtllktfpdvapRVLAH--------FLHF 118
Cdd:cd06864    84 QKLSSdtfdpdFVERRRAGLENFLL-----------RVAGHpelcqdkiFLEF 125
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 30-102 1.04e-04

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: 41.85  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  30 TYTVYVIQVtdGNHEwtIKHRYSDFHDLHEKLVaerKIDKTL----LPPKKII-------GKNSR--SLVEKREKDLEVY 96
Cdd:cd06867    17 SYIVYVIRL--GGSE--VKRRYSEFESLRKNLT---RLYPTLiippIPEKHSLkdyakkpSKAKNdaKIIERRKRMLQRF 89


                  ....*.
gi 1778901291  97 LQTLLK 102
Cdd:cd06867    90 LNRCLQ 95
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 17-116 1.28e-04

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: 41.54  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  17 AKEARVVGSELVD------TYTVYVIQVTDGNHEWT---IKHRYSDFHDLHEKLVAERKIDKTL----LPPKKII----G 79
Cdd:cd07280     2 ATDVNVGDYTIVGgdtgggAYVVWKITIETKDLIGSsivAYKRYSEFVQLREALLDEFPRHKRNeipqLPPKVPWydsrV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1778901291  80 KNSRSLVEKREKDLEVYLQTLLKTfPD-VAPRVLAHFL 116
Cdd:cd07280    82 NLNKAWLEKRRRGLQYFLNCVLLN-PVfGGSPVVKEFL 118
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 13-108 1.41e-04

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: 41.76  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  13 EAEPAKEARVVGSElvdTYTVYVIQVTDGNH----------------EWTIKHRYSDFHDLHEKLVAE---RKIDKTLLP 73
Cdd:cd06893     6 KTITAKEYKGTGTH---PYTLYTVQYETILDvqseqnpnaaseqplaTHTVNRRFREFLTLQTRLEENpkfRKIMNVKGP 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1778901291  74 PKKI----IGKNSRSLVEKREKDLEVYLQTLLkTFPDVA 108
Cdd:cd06893    83 PKRLfdlpFGNMDKDKIEARRGLLETFLRQLC-SIPEIS 120
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 357-398 1.49e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 39.15  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1778901291 357 NVKTLNLAGNFLERLSGLHKLYSLVNLDLRDN-RIEQLDEVKS 398
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLAN 44
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
 19-102 2.14e-04

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: 41.21  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  19 EARVVGSELVDTYTVYVIQVTDGNHE-------WTIKHRYSDFHDLHEKL------VAERKIDKtllPPKKIIGKNSRSL 85
Cdd:cd06878    17 EVTVEDDKEVPLYVIVVHVSEVGLNEdesissgWVVTRKLSEFHDLHRKLkecsswLKKVELPS---LSKKWFKSIDKKF 93

                          90
                  ....*....|....*..
gi 1778901291  86 VEKREKDLEVYLQTLLK 102
Cdd:cd06878    94 LDKSKNQLQKYLQFILE 110
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 290-388 2.46e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.07  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 290 LTTLDLSHNSISE-IDESVKLIPKIEYLDLSHNGV--LVVDNLQHLYNLVHLDLSYNKLS-SLEGVHTKLGNVKTLNLAG 365
Cdd:PLN00113  477 LENLDLSRNQFSGaVPRKLGSLSELMQLKLSENKLsgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQ 556

                          90       100
                  ....*....|....*....|....*...
gi 1778901291 366 NfleRLSG-----LHKLYSLVNLDLRDN 388
Cdd:PLN00113  557 N---QLSGeipknLGNVESLVQVNISHN 581
PX_PI3K_C2_68D cd06884
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases ...
 29-117 2.74e-04

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases similar to the Drosophila PI3K_68D protein; 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. 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. PI3K_68D is a novel PI3K which is widely expressed throughout the Drosophila life cycle. In vitro, it has been shown to phosphorylate PI and PI4P. It is involved in signaling pathways that affect pattern formation of Drosophila wings.


Pssm-ID: 132794  Cd Length: 111  Bit Score: 40.48  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  29 DTYTVYVIQVT-DGNHEWTIKHR-YSDFHDLHEKLVAERKIDK-TLLPPKKIIGK-NSRSLVEKREKDLEVYLQTLLKTF 104
Cdd:cd06884    16 EKYYVYVVEVTrENQASPQHVFRtYKEFLELYQKLCRKFPLAKlHPLSTGSHVGRsNIKSVAEKRKQDIQQFLNSLFKMA 95

                          90
                  ....*....|....
gi 1778901291 105 PDVAPRVLAH-FLH 117
Cdd:cd06884    96 EEVSHSDLVYtFFH 109
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
275-420 3.72e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 275 TLGGPVTAVIPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGVLVVDNLQHLYNLVHLDLSYNKLSSLEGVHtK 354
Cdd:COG4886    16 LLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG-D 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778901291 355 LGNVKTLNLAGNflerlSGLHKLYSLVNLDLRDNRIEQLDEvkSIGNLPCLEHVALLNNPLSIIPD 420
Cdd:COG4886    95 LTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLPE--ELANLTNLKELDLSNNQLTDLPE 153
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 311-350 4.37e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.00  E-value: 4.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1778901291 311 PKIEYLDLSHNGVLVVDNLQHLYNLVHLDLSYN-KLSSLEG 350
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSD 41
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 293-416 6.05e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.53  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 293 LDLSHNSIS-EIDESVKLIPKIEYLDLSHNGVLvvDNLQHLY---NLVHLDLSYNKLSslEGVHTKLGN---VKTLNLAG 365
Cdd:PLN00113  433 LDISNNNLQgRINSRKWDMPSLQMLSLARNKFF--GGLPDSFgskRLENLDLSRNQFS--GAVPRKLGSlseLMQLKLSE 508

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1778901291 366 NFL-----ERLSGLHKlysLVNLDLRDNRIE-QLDEvkSIGNLPCLEHVALLNNPLS 416
Cdd:PLN00113  509 NKLsgeipDELSSCKK---LVSLDLSHNQLSgQIPA--SFSEMPVLSQLDLSQNQLS 560
PX_PI3K_C2_alpha cd07289
The phosphoinositide binding Phox Homology Domain of the Alpha Isoform of Class II ...
 29-108 7.75e-04

The phosphoinositide binding Phox Homology Domain of the Alpha Isoform 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. 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. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132822  Cd Length: 109  Bit Score: 39.14  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  29 DTYTVYVIQVT-DGNHEWTIKHR-YSDFHDLHEKLVAERKIDKTL-LPPKKIIGKNS-RSLVEKREKDLEVYLQTLLKTF 104
Cdd:cd07289    14 DKHYIYVVRILrEGQIEPSFVFRtFDEFQELHNKLSILFPLWKLPgFPNKMVLGRTHiKDVAAKRKVELNSYIQSLMNSS 93


                  ....
gi 1778901291 105 PDVA 108
Cdd:cd07289    94 TEVA 97
PX_FISH cd06888
The phosphoinositide binding Phox Homology domain of Five SH protein; The PX domain is a ...
 33-102 1.00e-03

The phosphoinositide binding Phox Homology domain of Five SH protein; 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. Five SH (FISH), also called Tks5, is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. FISH contains an N-terminal PX domain and five Src homology 3 (SH3) domains. FISH binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. This subfamily also includes proteins with a different number of SH3 domains than FISH, such as Tks4, which contains four SH3 domains instead of five. The Tks4 adaptor protein is required for the formation of functional podosomes. It has overlapping, but not identical, functions as FISH. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132798  Cd Length: 119  Bit Score: 38.94  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  33 VYVIQVT--DGNHEwTIKHRYSDFHDLHEKLV------------AERKIdkTLLPPKKIIGK-NSRSLVEKREKDLEVYL 97
Cdd:cd06888    20 VYIINVTwsDGSSN-VIYRRYSKFFDLQMQLLdkfpieggqkdpSQRII--PFLPGKILFRRsHIRDVAVKRLKPIDEYC 96


                  ....*
gi 1778901291  98 QTLLK 102
Cdd:cd06888    97 KALVR 101
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
 34-117 1.09e-03

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


Pssm-ID: 132779  Cd Length: 119  Bit Score: 38.80  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  34 YVIQVTDGNHEWT---IKHRYSDFHDLHEKLVAE---RKIDKtlLPPKKiigknsrSLVekREK---DLEVYLQTLLKTf 104
Cdd:cd06869    36 FIIRVRREGEEYRtiyVARRYSDFKKLHHDLKKEfpgKKLPK--LPHKD-------KLP--REKlrlSLRQYLRSLLKD- 103

                          90
                  ....*....|....
gi 1778901291 105 PDVA-PRVLAHFLH 117
Cdd:cd06869   104 PEVAhSSILQEFLT 117
PX_PI3K_C2_beta cd07290
The phosphoinositide binding Phox Homology Domain of the Beta Isoform of Class II ...
 33-117 1.42e-03

The phosphoinositide binding Phox Homology Domain of the Beta Isoform 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. 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. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132823  Cd Length: 109  Bit Score: 38.37  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  33 VYVIQVT-DGNHEWTIKHR-YSDFHDLHEKLvaERKIDKTLLP--PKK-IIGKNSRSLV-EKREKDLEVYLQTLLKTFPD 106
Cdd:cd07290    18 AYVVKVQrEGHKEATFVQRtFEEFQELHNKL--RLLFPSSKLPsfPSRfVIGRSRGEAVaERRKEELNGYIWHLIHAPPE 95

                          90
                  ....*....|..
gi 1778901291 107 VAPRVLAH-FLH 117
Cdd:cd07290    96 VAECDLVYtFFH 107
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 355-418 1.42e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 40.15  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778901291 355 LGNVKTLNLAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDevkSIGNLPCLEHVALLNNPLSII 418
Cdd:cd21340     1 LKRITHLYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIE---NLEFLTNLTHLYLQNNQIEKI 61
PX_PLD2 cd07297
The phosphoinositide binding Phox Homology domain of Phospholipase D2; The PX domain is a ...
 20-73 1.72e-03

The phosphoinositide binding Phox Homology domain of Phospholipase D2; 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. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. PLD2 contains PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. It mediates EGF-dependent insulin secretion and EGF-induced Ras activation by the guanine nucleotide-exchange factor Son of sevenless (Sos). It regulates mast cell activation by associating and promoting the activation of the protein tyrosine kinase Syk. PLD2 also participates in the sphingosine 1-phosphate-mediated pathway that stimulates the migration of endothelial cells, an important factor in angiogenesis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132830  Cd Length: 130  Bit Score: 38.75  E-value: 1.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  20 ARVVGSEL------VDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVaERKIDKTLLP 73
Cdd:cd07297     6 AKVENTERyttgskVHVCTLYTVRLTHGEFTWTVKKKFKHFQELHRDLY-RHKVMLSFLP 64
LRR_8 pfam13855
Leucine rich repeat;
357-415 2.16e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778901291 357 NVKTLNLAGNFLERLSG--LHKLYSLVNLDLRDNRIEQLDEvKSIGNLPCLEHVALLNNPL 415
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSP-GAFSGLPSLRYLDLSGNRL 61
PX_RICS_like cd07278
The phosphoinositide binding Phox Homology domain of PX-RICS-like proteins; The PX domain is a ...
 6-100 2.47e-03

The phosphoinositide binding Phox Homology domain of PX-RICS-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 family include PX-RICS, TCGAP (Tc10/Cdc42 GTPase-activating protein), and similar proteins. They contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. They act as Rho GTPase-activating proteins. PX-RICS is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P. TCGAP is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132811  Cd Length: 114  Bit Score: 37.86  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291   6 LSFGPEREAEPAKEArvvGSELVdtytvYVIQVTDGNHEWTIKHRYSDFHDLHEKL---VAERKIDK-TLLPPKKIIGKN 81
Cdd:cd07278     9 VVLSDDGSLKSYKNS---GKELV-----YLVQVQCQGKSWLVKRSYDDFRMLDKHLhqcIYDRKFSQlTELPEECIEKRE 80

                          90
                  ....*....|....*....
gi 1778901291  82 SRSLVekreKDLEVYLQTL 100
Cdd:cd07278    81 QQNLH----QVLSDYLKRL 95
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 276-416 2.58e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.60  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 276 LGGPVTAVIPTWQALTTLDLSHNSIS-EIDESVKLIPKIEYLDLSHNGVL--VVDNLQHLYNLVHLDLSYNKLSSleGVH 352
Cdd:PLN00113  272 LSGPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgkIPVALTSLPRLQVLQLWSNKFSG--EIP 349

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 353 TKLG---NVKTLNLAGNFL--ERLSGLHKLYSLVNLDLRDNRIEqlDEV-KSIGNLPCLEHVALLNNPLS 416
Cdd:PLN00113  350 KNLGkhnNLTVLDLSTNNLtgEIPEGLCSSGNLFKLILFSNSLE--GEIpKSLGACRSLRRVRLQDNSFS 417
LRR_8 pfam13855
Leucine rich repeat;
287-321 2.60e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 2.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1778901291 287 WQALTTLDLSHNSISEIDESV-KLIPKIEYLDLSHN 321
Cdd:pfam13855  24 LSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGN 59
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 23-98 2.97e-03

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: 37.72  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  23 VGsELVDTYTVYVIQVTDGNH-----EWTIKHRYSDFHDLHEKLVAERKidKTLLPP---KKIIGKNSRSLVEKREKDLE 94
Cdd:cd06861    11 VG-DLTSAHTVYTVRTRTTSPnfevsSFSVLRRYRDFRWLYRQLQNNHP--GVIVPPppeKQSVGRFDDNFVEQRRAALE 87


                  ....
gi 1778901291  95 VYLQ 98
Cdd:cd06861    88 KMLR 91
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 243-390 3.84e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 39.65  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 243 LATMSVRFSAASMKEvLVPEASEFDEW----EPEGTTlggPVTAVIPTWQALTTLDLSHNSISE-----IDESVKLIPKI 313
Cdd:cd00116   120 LGDRGLRLLAKGLKD-LPPALEKLVLGrnrlEGASCE---ALAKALRANRDLKELNLANNGIGDagiraLAEGLKANCNL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 314 EYLDLSHNG------VLVVDNLQHLYNLVHLDLSYNKLSS------LEGVHTKLGNVKTLNLAGNFLERLSG------LH 375
Cdd:cd00116   196 EVLDLNNNGltdegaSALAETLASLKSLEVLNLGDNNLTDagaaalASALLSPNISLLTLSLSCNDITDDGAkdlaevLA 275

                         170
                  ....*....|....*
gi 1778901291 376 KLYSLVNLDLRDNRI 390
Cdd:cd00116   276 EKESLLELDLRGNKF 290
PLN03150 PLN03150
hypothetical protein; Provisional
 276-346 4.54e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 39.80  E-value: 4.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778901291 276 LGGPVTAVIPTWQALTTLDLSHNSI-SEIDESVKLIPKIEYLDLSHNGV--LVVDNLQHLYNLVHLDLSYNKLS 346
Cdd:PLN03150  430 LRGFIPNDISKLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFngSIPESLGQLTSLRILNLNGNSLS 503
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 20-102 4.58e-03

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: 36.92  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  20 ARVVgSELVDTYTVYVIQV----TDGNHEWTIKHRYSDFHDLHEKLVAERK--IDKTLLPPKKIIGKNSRSLVEKREKDL 93
Cdd:cd07279     8 ARTV-KEGEKKYVVYQLAVvqtgDPDTQPAFIERRYSDFLKLYKALRKQHPqlMAKVSFPRKVLMGNFSSELIAERSRAF 86


                  ....*....
gi 1778901291  94 EVYLQTLLK 102
Cdd:cd07279    87 EQFLGHILS 95
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
 43-116 5.58e-03

The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer.


Pssm-ID: 132828  Cd Length: 116  Bit Score: 36.71  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  43 HEWTIKHRYSDFHDLHEKLvaERKIDKTLLPP---KKIIGKNSRSLVEKREKDLEVYLQT-----LLKTfpdvAPRVLAH 114
Cdd:cd07295    36 RVSSVRRRYSDFEYFRDIL--ERESPRVMIPPlpgKIFTNRFSDEVIEERRQGLETFLQSvaghpLLQT----GSKVLAA 109


                  ..
gi 1778901291 115 FL 116
Cdd:cd07295   110 FL 111
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
 20-100 6.05e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; 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. 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. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 36.72  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291  20 ARVVgSELVDTYTVY-VIQVTDG---NHEWTIKHRYSDFHDLHEKLVAE--RKIDKTLLPPKKIIGKNSRSLVEKREKDL 93
Cdd:cd07300     8 ARII-EQTISKHVVYqIIVIQTGsfdCNKVVIERRYSDFLKLHQELLSDfsEELEDVVFPKKKLTGNFSEEIIAERRVAL 86


                  ....*..
gi 1778901291  94 EVYLQTL 100
Cdd:cd07300    87 RDYLTLL 93
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 280-345 6.57e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.45  E-value: 6.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778901291 280 VTAVIP----TWQALTTLDLSHNSIS-EIDESVKLIPKIEYLDLSHNGVL--VVDNLQHLYNLVHLDLSYNKL 345
Cdd:PLN00113  511 LSGEIPdelsSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgeIPKNLGNVESLVQVNISHNHL 583
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 276-399 8.30e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 38.62  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778901291 276 LGGP-VTAVIPTWQ---ALTTLDLSHNSISE-----IDESVKLIPKIEYLDLSHN-----GVLVVDN-LQHLYNLVHLDL 340
Cdd:COG5238   304 IGDEgAIALAEGLQgnkTLHTLNLAYNGIGAqgaiaLAKALQENTTLHSLDLSDNqigdeGAIALAKyLEGNTTLRELNL 383

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778901291 341 SYNKLSSLEGV----HTKLGNVKTLNLAGNflerlsglhklysLVNLDLRDNRIEQLDEVKSI 399
Cdd:COG5238   384 GKNNIGKQGAEalidALQTNRLHTLILDGN-------------LIGAEAQQRLEQLLERIKSV 433
 
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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