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Conserved domains on  [gi|1182918148|ref|NP_001337472|]
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sorting nexin-14 isoform p [Homo sapiens]

Protein Classification

RGS_SNX14 and PX_SNX14 domain-containing protein( domain architecture ID 10490382)

protein containing domains PXA, RGS_SNX14, PX_SNX14, and Nexin_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RGS_SNX14 cd08722
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; ...
243-369 1.35e-68

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX14 (Sorting Nexin14) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX14 is believed to regulates membrane trafficking in motor neurons.


:

Pssm-ID: 188677  Cd Length: 127  Bit Score: 222.99  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 243 IREQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDEMLSLHEELQKIYKTYCLDESIDKIRFDPFIVEEI 322
Cdd:cd08722     1 ILDDQRLLFPFMQFLKEEGAVHLLQFCLTVEDFNRRILNPDLTDEEKQSLHKEAQEIYKTYFLPEAPDRIHFPPDIVEEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1182918148 323 QRIAEGPYIDVVKLQTMRCLFEAYEHVLSLLENVFTPMFCHSDEYFR 369
Cdd:cd08722    81 KQILEGGPEKIVKLRTSRPLFEAYEHVYSLLESVFCPLFCHSDEYFI 127
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
467-589 5.40e-62

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: 204.53  E-value: 5.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 467 AWKISIPYVDFFEDPSSERKekkerIPVFCIDVERNDRRAVGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKR 546
Cdd:cd06877     2 AWRVSIPYVEMRRDPSNGER-----IYVFCIEVERNDRRAKGHEPQHWSVLRRYNEFYVLESKLTEFHGEFPDAPLPSRR 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1182918148 547 IIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLSPN 589
Cdd:cd06877    77 IFGPKSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSPN 119
PXA pfam02194
PXA domain; This domain is associated with PX domains pfam00787.
84-202 4.40e-28

PXA domain; This domain is associated with PX domains pfam00787.


:

Pssm-ID: 460484  Cd Length: 181  Bit Score: 111.56  E-value: 4.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  84 LSEVDIPSIITKKLLKAAMKHIEVIVKARQKVKN---TEFLQQAALEEYGPELHVALR--------SRRDELHYLRKLTE 152
Cdd:pfam02194  52 LRKVDLASLLLSRLLPLLTSHLEDYRKAEEAVRGkklNELDLALASKYLALKPHPALSpvllsssqSREAEQKYLRLLVD 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1182918148 153 LLFPYILPPKATDCRSLTLLIREILSGSVFLPSLDFLADPDTVNHLLIIF 202
Cdd:pfam02194 132 GLLPLLLPPEDLESRPVRVLVREILACLVLLPVINKLSDPDFINELIVKL 181
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
710-814 3.03e-24

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


:

Pssm-ID: 462541  Cd Length: 111  Bit Score: 98.07  E-value: 3.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 710 WLHH-LLMGTRILFKNTLEMYTDYYLQCKLEQLFQEHRLVSLITLLRDAIFC-----ENTEPRSLQDKQKGAKQTFEEMM 783
Cdd:pfam08628   1 WLRRrALNALKQVLQQLLGDTIERKLRESVEWLTSEEQVASYIRLLRDALWPggllaEPPPERTEEEKLRTRKEARKLLL 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1182918148 784 NYIPDLLVKCIGEETKYESIRLLFDGLQQPV 814
Cdd:pfam08628  81 SLIPDALGSVVGRENAREAARRVFDMLQNPR 111
 
Name Accession Description Interval E-value
RGS_SNX14 cd08722
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; ...
243-369 1.35e-68

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX14 (Sorting Nexin14) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX14 is believed to regulates membrane trafficking in motor neurons.


Pssm-ID: 188677  Cd Length: 127  Bit Score: 222.99  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 243 IREQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDEMLSLHEELQKIYKTYCLDESIDKIRFDPFIVEEI 322
Cdd:cd08722     1 ILDDQRLLFPFMQFLKEEGAVHLLQFCLTVEDFNRRILNPDLTDEEKQSLHKEAQEIYKTYFLPEAPDRIHFPPDIVEEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1182918148 323 QRIAEGPYIDVVKLQTMRCLFEAYEHVLSLLENVFTPMFCHSDEYFR 369
Cdd:cd08722    81 KQILEGGPEKIVKLRTSRPLFEAYEHVYSLLESVFCPLFCHSDEYFI 127
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
467-589 5.40e-62

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: 204.53  E-value: 5.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 467 AWKISIPYVDFFEDPSSERKekkerIPVFCIDVERNDRRAVGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKR 546
Cdd:cd06877     2 AWRVSIPYVEMRRDPSNGER-----IYVFCIEVERNDRRAKGHEPQHWSVLRRYNEFYVLESKLTEFHGEFPDAPLPSRR 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1182918148 547 IIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLSPN 589
Cdd:cd06877    77 IFGPKSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSPN 119
PXA pfam02194
PXA domain; This domain is associated with PX domains pfam00787.
84-202 4.40e-28

PXA domain; This domain is associated with PX domains pfam00787.


Pssm-ID: 460484  Cd Length: 181  Bit Score: 111.56  E-value: 4.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  84 LSEVDIPSIITKKLLKAAMKHIEVIVKARQKVKN---TEFLQQAALEEYGPELHVALR--------SRRDELHYLRKLTE 152
Cdd:pfam02194  52 LRKVDLASLLLSRLLPLLTSHLEDYRKAEEAVRGkklNELDLALASKYLALKPHPALSpvllsssqSREAEQKYLRLLVD 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1182918148 153 LLFPYILPPKATDCRSLTLLIREILSGSVFLPSLDFLADPDTVNHLLIIF 202
Cdd:pfam02194 132 GLLPLLLPPEDLESRPVRVLVREILACLVLLPVINKLSDPDFINELIVKL 181
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
710-814 3.03e-24

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


Pssm-ID: 462541  Cd Length: 111  Bit Score: 98.07  E-value: 3.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 710 WLHH-LLMGTRILFKNTLEMYTDYYLQCKLEQLFQEHRLVSLITLLRDAIFC-----ENTEPRSLQDKQKGAKQTFEEMM 783
Cdd:pfam08628   1 WLRRrALNALKQVLQQLLGDTIERKLRESVEWLTSEEQVASYIRLLRDALWPggllaEPPPERTEEEKLRTRKEARKLLL 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1182918148 784 NYIPDLLVKCIGEETKYESIRLLFDGLQQPV 814
Cdd:pfam08628  81 SLIPDALGSVVGRENAREAARRVFDMLQNPR 111
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
507-589 4.99e-22

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 90.76  E-value: 4.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 507 VGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:pfam00787   2 PTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81

                  ...
gi 1182918148 587 SPN 589
Cdd:pfam00787  82 ESD 84
PXA smart00313
Domain associated with PX domains; unpubl. observations
76-206 4.92e-15

Domain associated with PX domains; unpubl. observations


Pssm-ID: 214611  Cd Length: 176  Bit Score: 73.99  E-value: 4.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148   76 ISSKVDASLSEVDIPSIITKKLLKAAMKHIEVIVKARQKvKNTEFLQQAALEEYGPE--LHVALRSRRDELHYLRKLTEL 153
Cdd:smart00313  44 ILRQLYRRLSRQDSAHLILYEILKNLISTITNALEAVLR-FASPQIPSTEIDLQYAEtaIHKALSSPSNELTYRRQLVEM 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1182918148  154 LFPYILPPKATDCRSLTLLIREILSGSVFLPSLDFLADPDTVNHLLIIFIDDS 206
Cdd:smart00313 123 LLKFLLPEDSLCSRLHRCLLREVLAMQVILPLITHLSDPDTINLCIILLFSSS 175
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
507-587 3.08e-11

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: 60.82  E-value: 3.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  507 VGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNY---EFLKSKREEFQEYLQKLLQHPELSN-SQLL 582
Cdd:smart00312  21 TKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLNNfseEFIEKRRRGLEKYLQSLLNHPELINhSEVV 100

                   ....*
gi 1182918148  583 ADFLS 587
Cdd:smart00312 101 LEFLE 105
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
240-367 3.00e-09

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 55.35  E-value: 3.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  240 LKQIREQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDrilrpELSNDEMLSLheeLQKIYKTYCLDESIDKIRFDPFIV 319
Cdd:smart00315   2 LESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKK-----AEDDEERIAK---AREIYDKFLSPNAPKEVNLDSDLR 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1182918148  320 EEIQRIAEGPYIDVvklqtmRCLFEAYEHVLSLLENVFTPMFCHSDEY 367
Cdd:smart00315  74 EKIEENLESEEPPP------DLFDEAQREVYELLEKDSFPRFLESDYY 115
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
249-371 6.50e-06

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 459870  Cd Length: 117  Bit Score: 46.07  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 249 LLFRfmNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDemlslheeLQKIYKTYCLDESIDKIRFDPFIVEEIQriaeg 328
Cdd:pfam00615  13 RLFR--QFLESEFSEENLEFWLACEEFKKADPDEERLKK--------AKEIYNEFLAPGSPKEINLDSDLREEIR----- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1182918148 329 pyiDVVKLQTMRCLFEAY-EHVLSLLENVFTPMFCHSDeYFRQL 371
Cdd:pfam00615  78 ---ENLEKEPTRDLFDEAqAEVYELMEKDSYPRFLKSP-LYLRL 117
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
456-598 4.25e-04

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 43.63  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 456 VSTPNTPRNLAAWKISIpyvdfFEDPSSERKEKKERIPVFCIDVER--NDRRAVGHEPEHWSVYRRYLEFYVLESKLTEF 533
Cdd:COG5391   118 PPLSTSHTILDYFISST-----VSNPQSLTLLVDSRDKHTSYEIITvtNLPSFQLRESRPLVVRRRYSDFESLHSILIKL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 534 HGAFPDAQLPSKRIIGPKNY-----EFLKSKREEFQEYLQKLLQHPELSNSQ----------LLADFLSPNG--GETQFL 596
Cdd:COG5391   193 LPLCAIPPLPSKKSNSEYYGdrfsdEFIEERRQSLQNFLRRVSTHPLLSNYKnsksweshstLLSSFIENRKsvPTPLSL 272

                  ..
gi 1182918148 597 DK 598
Cdd:COG5391   273 DL 274
 
Name Accession Description Interval E-value
RGS_SNX14 cd08722
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; ...
243-369 1.35e-68

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX14 (Sorting Nexin14) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX14 is believed to regulates membrane trafficking in motor neurons.


Pssm-ID: 188677  Cd Length: 127  Bit Score: 222.99  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 243 IREQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDEMLSLHEELQKIYKTYCLDESIDKIRFDPFIVEEI 322
Cdd:cd08722     1 ILDDQRLLFPFMQFLKEEGAVHLLQFCLTVEDFNRRILNPDLTDEEKQSLHKEAQEIYKTYFLPEAPDRIHFPPDIVEEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1182918148 323 QRIAEGPYIDVVKLQTMRCLFEAYEHVLSLLENVFTPMFCHSDEYFR 369
Cdd:cd08722    81 KQILEGGPEKIVKLRTSRPLFEAYEHVYSLLESVFCPLFCHSDEYFI 127
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
467-589 5.40e-62

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: 204.53  E-value: 5.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 467 AWKISIPYVDFFEDPSSERKekkerIPVFCIDVERNDRRAVGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKR 546
Cdd:cd06877     2 AWRVSIPYVEMRRDPSNGER-----IYVFCIEVERNDRRAKGHEPQHWSVLRRYNEFYVLESKLTEFHGEFPDAPLPSRR 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1182918148 547 IIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLSPN 589
Cdd:cd06877    77 IFGPKSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSPN 119
PXA pfam02194
PXA domain; This domain is associated with PX domains pfam00787.
84-202 4.40e-28

PXA domain; This domain is associated with PX domains pfam00787.


Pssm-ID: 460484  Cd Length: 181  Bit Score: 111.56  E-value: 4.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  84 LSEVDIPSIITKKLLKAAMKHIEVIVKARQKVKN---TEFLQQAALEEYGPELHVALR--------SRRDELHYLRKLTE 152
Cdd:pfam02194  52 LRKVDLASLLLSRLLPLLTSHLEDYRKAEEAVRGkklNELDLALASKYLALKPHPALSpvllsssqSREAEQKYLRLLVD 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1182918148 153 LLFPYILPPKATDCRSLTLLIREILSGSVFLPSLDFLADPDTVNHLLIIF 202
Cdd:pfam02194 132 GLLPLLLPPEDLESRPVRVLVREILACLVLLPVINKLSDPDFINELIVKL 181
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
710-814 3.03e-24

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


Pssm-ID: 462541  Cd Length: 111  Bit Score: 98.07  E-value: 3.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 710 WLHH-LLMGTRILFKNTLEMYTDYYLQCKLEQLFQEHRLVSLITLLRDAIFC-----ENTEPRSLQDKQKGAKQTFEEMM 783
Cdd:pfam08628   1 WLRRrALNALKQVLQQLLGDTIERKLRESVEWLTSEEQVASYIRLLRDALWPggllaEPPPERTEEEKLRTRKEARKLLL 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1182918148 784 NYIPDLLVKCIGEETKYESIRLLFDGLQQPV 814
Cdd:pfam08628  81 SLIPDALGSVVGRENAREAARRVFDMLQNPR 111
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
507-589 4.99e-22

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 90.76  E-value: 4.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 507 VGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:pfam00787   2 PTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81

                  ...
gi 1182918148 587 SPN 589
Cdd:pfam00787  82 ESD 84
RGS cd07440
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ...
245-369 1.95e-19

Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.


Pssm-ID: 188659 [Multi-domain]  Cd Length: 113  Bit Score: 84.36  E-value: 1.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 245 EQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDrilrpelSNDEMLSLHEELQKIYKTYCLDESIDKIRFDPFIVEEIQR 324
Cdd:cd07440     2 RDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKK-------TTSSDEELKSKAKEIYDKYISKDAPKEINIPESIREEIEE 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1182918148 325 IAEGPYIDvvklqtMRCLFEAYEHVLSLLENVFTPMFCHSDEYFR 369
Cdd:cd07440    75 NLEEPYPD------PDCFDEAQEHILNLLEKDSYPRFLKSDLYLK 113
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
484-587 1.72e-17

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: 78.55  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 484 ERKEKKERIPVFCIDVERNDrravghePEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEF 563
Cdd:cd06093     9 KVKDGGKKYVVYIIEVTTQG-------GEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQL 81
                          90       100
                  ....*....|....*....|....
gi 1182918148 564 QEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd06093    82 EQYLQSLLNHPELRNSEELKEFLE 105
PXA smart00313
Domain associated with PX domains; unpubl. observations
76-206 4.92e-15

Domain associated with PX domains; unpubl. observations


Pssm-ID: 214611  Cd Length: 176  Bit Score: 73.99  E-value: 4.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148   76 ISSKVDASLSEVDIPSIITKKLLKAAMKHIEVIVKARQKvKNTEFLQQAALEEYGPE--LHVALRSRRDELHYLRKLTEL 153
Cdd:smart00313  44 ILRQLYRRLSRQDSAHLILYEILKNLISTITNALEAVLR-FASPQIPSTEIDLQYAEtaIHKALSSPSNELTYRRQLVEM 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1182918148  154 LFPYILPPKATDCRSLTLLIREILSGSVFLPSLDFLADPDTVNHLLIIFIDDS 206
Cdd:smart00313 123 LLKFLLPEDSLCSRLHRCLLREVLAMQVILPLITHLSDPDTINLCIILLFSSS 175
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
469-587 1.94e-12

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: 65.02  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 469 KISIpyVDFFEDPSSERKEkkerIPVFCIDVER--NDRRAVGhepehWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKR 546
Cdd:cd06876    21 RVSI--QSYISDVEEEGKE----FVVYLIEVQRlnNDDQSSG-----WVVARRYSEFLELHKYLKKRYPGVLKLDFPQKR 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1182918148 547 IIGPKNYE--FLKSKREEFQEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd06876    90 KISLKYSKtlLVEERRKALEKYLQELLKIPEVCEDEEFRKFLS 132
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
507-587 3.08e-11

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: 60.82  E-value: 3.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  507 VGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNY---EFLKSKREEFQEYLQKLLQHPELSN-SQLL 582
Cdd:smart00312  21 TKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLNNfseEFIEKRRRGLEKYLQSLLNHPELINhSEVV 100

                   ....*
gi 1182918148  583 ADFLS 587
Cdd:smart00312 101 LEFLE 105
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
484-586 4.57e-11

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: 60.50  E-value: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 484 ERKEKKERIPVFCIDVERNdrravghEPEHWSVYRRYLEFYVLESKLTEfhgAFPDAQ--LPSKRIIGPK-NYEFLKSKR 560
Cdd:cd07276    12 EVMEERARFTVYKIRVENK-------VGDSWFVFRRYTDFVRLNDKLKQ---MFPGFRlsLPPKRWFKDNfDPDFLEERQ 81
                          90       100
                  ....*....|....*....|....*.
gi 1182918148 561 EEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:cd07276    82 LGLQAFVNNIMAHKDIAKCKLVREFF 107
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
511-601 4.67e-10

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: 57.74  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 511 PEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPelsnSQLLADFLSPNG 590
Cdd:cd07277    29 DDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKRLQVYLRRVVNTL----IQTSPELTACPS 104
                          90
                  ....*....|.
gi 1182918148 591 GETqfLDKILP 601
Cdd:cd07277   105 KET--LIKLLP 113
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
495-597 6.44e-10

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: 57.37  E-value: 6.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 495 FCIDVERndrravGHEPEH-WSVYRRYLEFYVLESKLtEFHGAfpDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQH 573
Cdd:cd06871    24 YIIRVQR------GPSPENsWQVIRRYNDFDLLNASL-QISGI--SLPLPPKKLIGNMDREFIAERQQGLQNYLNVILMN 94
                          90       100
                  ....*....|....*....|....
gi 1182918148 574 PELSNSQLLADFLSPNGGETQFLD 597
Cdd:cd06871    95 PILASCLPVKKFLDPNNYSANFTE 118
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
480-586 8.32e-10

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: 57.03  E-value: 8.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 480 DPSSERKEKKERIPVFCIDVerndrrAVGHEpeHWSVYRRYLEFYVLESKLTEfhgAFPDAQL--PSKRIIGpKNY--EF 555
Cdd:cd06870     8 PSSDEDREKKKRFTVYKVVV------SVGRS--SWFVFRRYAEFDKLYESLKK---QFPASNLkiPGKRLFG-NNFdpDF 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1182918148 556 LKSKREEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:cd06870    76 IKQRRAGLDEFIQRLVSDPKLLNHPDVRAFL 106
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
464-588 9.64e-10

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: 57.38  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 464 NLAAWKISIPYVDFFEdpsserkEKKERIPVFCIDVER--NDRRAVGHEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQ 541
Cdd:cd06878     5 HLGKWRANIQSAEVTV-------EDDKEVPLYVIVVHVseVGLNEDESISSGWVVTRKLSEFHDLHRKLKECSSWLKKVE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1182918148 542 LP--SKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLSP 588
Cdd:cd06878    78 LPslSKKWFKSIDKKFLDKSKNQLQKYLQFILEDETLCQSEALYSFLSP 126
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
240-367 3.00e-09

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 55.35  E-value: 3.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148  240 LKQIREQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDrilrpELSNDEMLSLheeLQKIYKTYCLDESIDKIRFDPFIV 319
Cdd:smart00315   2 LESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKK-----AEDDEERIAK---AREIYDKFLSPNAPKEVNLDSDLR 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1182918148  320 EEIQRIAEGPYIDVvklqtmRCLFEAYEHVLSLLENVFTPMFCHSDEY 367
Cdd:smart00315  74 EKIEENLESEEPPP------DLFDEAQREVYELLEKDSFPRFLESDYY 115
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
486-588 1.10e-08

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: 53.81  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 486 KEKKERIPVFCIDVERNDRRAvghEPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQE 565
Cdd:cd06873    16 KEHGKTYAVYAISVTRIYPNG---QEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQ 92
                          90       100
                  ....*....|....*....|....*..
gi 1182918148 566 YLQKLLQHPELSNS----QLLADFLSP 588
Cdd:cd06873    93 YLQSLLNPEVLDANpglqEIVLDFLEP 119
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
516-581 9.32e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 51.18  E-value: 9.32e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918148 516 VYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGP-KNYEFLKSKREEFQEYLQKLLQHPE-LSNSQL 581
Cdd:cd06898    39 VRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRfNNEGFIEERQQGLQDFLEKVLQTPLlLSDSRL 106
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
514-587 1.17e-07

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: 50.73  E-value: 1.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918148 514 WSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRII--GPKNYEFLKSKREEFQEYLQKLLQHPE--LSNSQLLADFLS 587
Cdd:cd06897    29 YTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFlsTSSNPKLVEERRVGLEAFLRALLNDEDsrWRNSPAVKEFLN 106
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
515-589 1.45e-07

The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX41 and SNX42 (also called Atg20p) form dimers with SNX4, and are required in protein recycling from the sorting endosome (post-Golgi endosome) back to the late Golgi in yeast.


Pssm-ID: 132777  Cd Length: 112  Bit Score: 50.71  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 515 SVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIgpKNY--EFLKSKREE---------FQEYLQKLLQHPELSNSQLLA 583
Cdd:cd06867    29 EVKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSL--KDYakKPSKAKNDAkiierrkrmLQRFLNRCLQHPILRNDIVFQ 106

                  ....*.
gi 1182918148 584 DFLSPN 589
Cdd:cd06867   107 KFLDPN 112
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
515-587 2.82e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization.


Pssm-ID: 132818  Cd Length: 126  Bit Score: 50.02  E-value: 2.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1182918148 515 SVYRRYLEF-YVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd07285    33 SVNHRYKHFdWLYERLLVKFGLAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLN 106
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
487-596 3.52e-07

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: 49.59  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 487 EKKERIPVFCIDVERNDRRavghepehWSVYRRYLEFYVLESKLTEFHGAFPDAqLPSKRIIGPKNYEFLKSKREEFQEY 566
Cdd:cd06875    12 ETVEGYTVYIIEVKVGSVE--------WTVKHRYSDFAELHDKLVAEHKVDKDL-LPPKKLIGNKSPSFVEKRRKELEIY 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1182918148 567 LQKLLQHPELSNSQLLADFLSPNGGETQFL 596
Cdd:cd06875    83 LQTLLSFFQKTMPRELAHFLDFHKYEIIGL 112
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
515-587 7.10e-07

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: 48.85  E-value: 7.10e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182918148 515 SVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd06862    33 TVSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGRFEEDFIEKRRERLELWMNRLARHPVLSQSEVFRHFLT 105
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
512-586 9.35e-07

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: 48.52  E-value: 9.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 512 EHWSVYRRYLEFYVLESKLTEFHG--AFPDAQLPSKRIIG----------PKNYEFLKSKREEFQEYLQKLLQHPELSNS 579
Cdd:cd07281    35 KHFTVKRRFSDFLGLYEKLSEKHSqnGFIVPPPPEKSLIGmtkvkvgkedSSSAEFLERRRAALERYLQRIVSHPSLLQD 114

                  ....*..
gi 1182918148 580 QLLADFL 586
Cdd:cd07281   115 PDVREFL 121
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
515-587 1.07e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 47.99  E-value: 1.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1182918148 515 SVYRRYLEFYVLESKLTEfhgAFPD---AQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd06866    31 TVYRRYSDFVWLHEYLLK---RYPYrmvPALPPKRIGGSADREFLEARRRGLSRFLNLVARHPVLSEDELVRTFLT 103
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
504-587 1.15e-06

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


Pssm-ID: 132775  Cd Length: 120  Bit Score: 48.19  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 504 RRAVGHEPEHWSVYRRYLEFYVLESKL-TEFHGAFPDAQlPSKRI---IGPKNYEFLKSKREEFQEYLQKLLQHPELSNS 579
Cdd:cd06865    32 TNIPSYTHGEFTVRRRFRDVVALADRLaEAYRGAFVPPR-PDKSVvesQVMQSAEFIEQRRVALEKYLNRLAAHPVIGLS 110

                  ....*...
gi 1182918148 580 QLLADFLS 587
Cdd:cd06865   111 DELRVFLT 118
RGS_AKAP2_2 cd08721
Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, ...
247-369 2.05e-06

Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, D-AKAP2; The RGS (Regulator of G-protein Signaling) domain is an essential part of the D-AKAP2 (A-kinase anchoring protein), a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. D-AKAP2 contains two RGS domains which play an important role in spatiotemporal localization of cAMP-dependent PKA (cyclic AMP-dependent protein kinase) that regulates many different signaling pathways by phosphorylation of target proteins. This cd contains the second RGS domain.


Pssm-ID: 188676  Cd Length: 121  Bit Score: 47.34  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 247 QDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDEMLSLHEELqKIYKTYCLDESI------DKIRFDpfIVE 320
Cdd:cd08721     5 ESALFYFMEYMEQEGARNLLQFWLAADNFQSQLAAKEGQYDGQQAQNDAM-IIYDKYFSLQATeplgfdDKTRLE--VES 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1182918148 321 EIQRiAEGPYIDvvklqtmrCLFEAYEHVLSLLENVFTPMFCHSDEYFR 369
Cdd:cd08721    82 NICR-EGGPLPS--------CFEAPLLQALTTLEQHYLPGFLSSQLYYK 121
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
494-586 4.75e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 46.11  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 494 VFCIDVERNDRRAVghepehwsVYRRYLEFYVLESKLTEFHGAfPDaqLPSKRIIGpKNYEFLKSKREEFQEYLQKLLQH 573
Cdd:cd06880    21 VFTIEVLVNGRRHT--------VEKRYSEFHALHKKLKKSIKT-PD--FPPKRVRN-WNPKVLEQRRQGLEAYLQGLLKI 88
                          90
                  ....*....|...
gi 1182918148 574 PELsnSQLLADFL 586
Cdd:cd06880    89 NEL--PKQLLDFL 99
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
249-371 6.50e-06

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 459870  Cd Length: 117  Bit Score: 46.07  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 249 LLFRfmNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDemlslheeLQKIYKTYCLDESIDKIRFDPFIVEEIQriaeg 328
Cdd:pfam00615  13 RLFR--QFLESEFSEENLEFWLACEEFKKADPDEERLKK--------AKEIYNEFLAPGSPKEINLDSDLREEIR----- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1182918148 329 pyiDVVKLQTMRCLFEAY-EHVLSLLENVFTPMFCHSDeYFRQL 371
Cdd:pfam00615  78 ---ENLEKEPTRDLFDEAqAEVYELMEKDSYPRFLKSP-LYLRL 117
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
510-586 3.54e-05

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: 43.72  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 510 EPEHWSVYRRYLEFYVLESKLTEFH-GAF--PdaqLPSKRIIG-PK-NYEFLKSKREEFQEYLQKLLQHPELSNSQLLAD 584
Cdd:cd06859    33 KKSEFSVLRRYSDFLWLYERLVEKYpGRIvpP---PPEKQAVGrFKvKFEFIEKRRAALERFLRRIAAHPVLRKDPDFRL 109

                  ..
gi 1182918148 585 FL 586
Cdd:cd06859   110 FL 111
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
484-588 7.18e-05

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: 42.73  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 484 ERKEKKERIPVFCIDVERNDRravgHEPEHwsVYRRYLEFYVLESKLTEfhgAFPDAQLPS---KRIIGPKNYEFLKSKR 560
Cdd:cd06883     8 QKRYSPEKYYIYVVKVTRENQ----TEPSF--VFRTFEEFQELHNKLSL---LFPSLKLPSfpaRVVLGRSHIKQVAERR 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1182918148 561 -EEFQEYLQKLLQHP-ELSNSQLLADFLSP 588
Cdd:cd06883    79 kIELNSYLKSLFNASpEVAESDLVYTFFHP 108
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
510-587 7.70e-05

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: 42.72  E-value: 7.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918148 510 EPEHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd06861    33 EVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRFDDNFVEQRRAALEKMLRKIANHPVLQKDPDFRLFLE 110
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
512-571 1.29e-04

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 42.37  E-value: 1.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 512 EHWSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLL 571
Cdd:cd06874    30 ETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQLETYLRNFF 89
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
514-586 2.24e-04

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: 41.96  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 514 WSVYRRYLEFYVLESKLTE--FHGAFPDAQLPSKRIIG----------PKNYEFLKSKREEFQEYLQKLLQHPELSNSQL 581
Cdd:cd07282    37 FSVRRRFSDFLGLHSKLASkyLHVGYIVPPAPEKSIVGmtkvkvgkedSSSTEFVEKRRAALERYLQRTVKHPTLLQDPD 116

                  ....*
gi 1182918148 582 LADFL 586
Cdd:cd07282   117 LRQFL 121
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
514-586 3.07e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 41.17  E-value: 3.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182918148 514 WSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPK----NYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:cd06860    37 YSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLldrfSPEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFL 113
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
514-587 3.39e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 41.12  E-value: 3.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918148 514 WSVYRRYLEFYVLESKLTEFHGAFPDAQLPSKRIIGPK----NYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLS 587
Cdd:cd07284    37 FEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMverfNEDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLT 114
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
456-598 4.25e-04

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 43.63  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 456 VSTPNTPRNLAAWKISIpyvdfFEDPSSERKEKKERIPVFCIDVER--NDRRAVGHEPEHWSVYRRYLEFYVLESKLTEF 533
Cdd:COG5391   118 PPLSTSHTILDYFISST-----VSNPQSLTLLVDSRDKHTSYEIITvtNLPSFQLRESRPLVVRRRYSDFESLHSILIKL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 534 HGAFPDAQLPSKRIIGPKNY-----EFLKSKREEFQEYLQKLLQHPELSNSQ----------LLADFLSPNG--GETQFL 596
Cdd:COG5391   193 LPLCAIPPLPSKKSNSEYYGdrfsdEFIEERRQSLQNFLRRVSTHPLLSNYKnsksweshstLLSSFIENRKsvPTPLSL 272

                  ..
gi 1182918148 597 DK 598
Cdd:COG5391   273 DL 274
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
513-586 5.24e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 40.01  E-value: 5.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1182918148 513 HWSVyrRYLEFYVLESKLTEFHGAFPDAQLPSKRIIgPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:cd06885    30 HCSV--RYSQLHGLNEQLKKEFGNRKLPPFPPKKLL-PLTPAQLEERRLQLEKYLQAVVQDPRIANSDIFNSFL 100
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
497-589 8.24e-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: 40.22  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 497 IDVERNDRRAVGHEP--EHWSVYRRYLEFYVLESKLTEFHG--AFPDAQLPSKRI----IGPKNYEFLKSKREEFQEYLQ 568
Cdd:cd06893    32 LDVQSEQNPNAASEQplATHTVNRRFREFLTLQTRLEENPKfrKIMNVKGPPKRLfdlpFGNMDKDKIEARRGLLETFLR 111
                          90       100
                  ....*....|....*....|.
gi 1182918148 569 KLLQHPELSNSQLLADFLSPN 589
Cdd:cd06893   112 QLCSIPEISNSEEVQEFLAYG 132
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
516-586 1.51e-03

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


Pssm-ID: 132789  Cd Length: 138  Bit Score: 39.62  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1182918148 516 VYRRYLEFYVLeskLTEFHGAFPDAQLPS---KRIIGPKNYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFL 586
Cdd:cd06879    65 VLRRFNDFLKL---HTDLKKLFPKKKLPAappKGLLRMKNRALLEERRHSLEEWMGKLLSDIDLSRSVPVASFL 135
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
516-588 1.59e-03

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: 39.23  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 516 VYRRYLEFYVLESKLTEfhgAFPDA------QLPSKRIIGPK----NYEFLKSKREEFQEYLQKLLQHPELSNSQLLADF 585
Cdd:cd07280    41 AYKRYSEFVQLREALLD---EFPRHkrneipQLPPKVPWYDSrvnlNKAWLEKRRRGLQYFLNCVLLNPVFGGSPVVKEF 117

                  ...
gi 1182918148 586 LSP 588
Cdd:cd07280   118 LLP 120
PX_Bem1p cd06890
The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a ...
512-588 1.75e-03

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: 38.81  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 512 EHWSVYRRYLEFYVLESKLTEfhgAFPD--AQLPSKRIIGP-------KNYEFLKSKR-EEFQEYLQKLLQHPE-LSNSQ 580
Cdd:cd06890    27 KTRYLCRYYQDFYKLHIALLD---LFPAeaGRNSSKRILPYlpgpvtdVVNDSISLKRlNDLNEYLNELINLPAyIQTSE 103

                  ....*...
gi 1182918148 581 LLADFLSP 588
Cdd:cd06890   104 VVRDFFAN 111
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
515-587 3.53e-03

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 38.04  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 515 SVYRRYLEFYVLESKLTEFHGAFPDAQLPSKriigpKNYEFLKSKR--EEF--------QEYLQKLLQHPELSNSQLLAD 584
Cdd:cd06863    39 KVRRRYSDFVFLHECLSNDFPACVVPPLPDK-----HRLEYITGDRfsPEFitrraqslQRFLRRISLHPVLSQSKILHQ 113

                  ...
gi 1182918148 585 FLS 587
Cdd:cd06863   114 FLE 116
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
510-589 7.35e-03

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: 37.11  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918148 510 EPEHWSVYRRYLEFYVLESKLTEFhgAFPDAQLPSKRIIGPK-NYEFLKSKREEFQEYLQKLLQHPELSNSQLLADFLSP 588
Cdd:cd06872    29 ENETWVVKRRFRNFETLHRRLKEV--PKYNLELPPKRFLSSSlDGAFIEERCKLLDKYLKDLLVIEKVAESHEVWSFLSA 106

                  .
gi 1182918148 589 N 589
Cdd:cd06872   107 R 107
 
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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