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Conserved domains on  [gi|133901974|ref|NP_001076763|]
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PX domain-containing protein [Caenorhabditis elegans]

Protein Classification

SNX17 family PH domain-containing protein( domain architecture ID 12951902)

SNX17 family PH (pleckstrin homology) domain-containing protein similar to PH region of sorting nexin 17 (SNX17), a critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM-like_C_SNX17 cd13337
Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding ...
 292-395 4.10e-51

Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding protein that interacts with the free kindlin-binding site in endosomes to stabilize beta1 integrins, resulting in their recycling to the cell surface where they can be reused. SNX17 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. SNX17 binds Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270145  Cd Length: 113  Bit Score: 169.06  E-value: 4.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 292 YSYEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRITQVM---------DKISFQFEYLMA 362
Cdd:cd13337    1 YGYIQFEPCICDYPKPGTRVLVSIGNRELNFRLKDEEGKVKEGSFRVTRMRCWRITASHieedskkdeKKLELSFEYLMS 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 133901974 363 KDTFEWITLDTDQSILMSLLLQSIGSEILYEHN 395
Cdd:cd13337   81 KDKLQWITIRSDQAILMSLCLQSMVDELLRKKN 113
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 3-109 8.02e-49

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: 162.88  E-value: 8.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   3 HVDVPDTKTLVERsdGITKYTAYNIHINGWYHGSVRFSHLYEFAELIKQKFSQRyKGPEFPAKKLFKLDPKAIDERRQKI 82
Cdd:cd06885    1 HFSIPDTQELSDE--GGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNR-KLPPFPPKKLLPLTPAQLEERRLQL 77

                         90       100
                 ....*....|....*....|....*..
gi 133901974  83 TKYFQALVQHPEVARHYLVEKKLLGFQ 109
Cdd:cd06885   78 EKYLQAVVQDPRIANSDIFNSFLLNAQ 104
FERM_F1_SNX17 cd16121
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 118-229 2.71e-32

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 17 (SNX17); SNX17 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It localizes to early endosomes, and plays an important role in mediating endocytic internalization, recycling, and/or protection from lysosomal degradation of NPxY-motif containing cell surface proteins including amyloid precursor protein (APP), P-selectin, beta1-integrin, low density lipoprotein receptor (LDLR), LDLR related protein (Lrp1), ApoER2, and FEEL1. SNX17 also affects T cell activation by regulating T cell receptor and integrin recycling. SNX17 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340538  Cd Length: 93  Bit Score: 118.49  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 118 QYVTLDVFLGNGEKTTIKCLVSDSTLEIMKIICEKLGFknKDQFIYHFGLFMAKGRDPTNACysvttenfnplLTRFLRN 197
Cdd:cd16121    1 EEVSLDVFLMNGQKITVNISSTDQTDDVLEAVASKLGL--PEELVYYFALFLVKKDDDGNNT-----------IVRKLQD 67

                         90       100       110
                 ....*....|....*....|....*....|..
gi 133901974 198 FEAPFVSLSTANQkynengHYHFLCLRKLIWD 229
Cdd:cd16121   68 FESPYLSLKSAGK------GSHRIVLRKSYWD 93
 
Name Accession Description Interval E-value
FERM-like_C_SNX17 cd13337
Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding ...
 292-395 4.10e-51

Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding protein that interacts with the free kindlin-binding site in endosomes to stabilize beta1 integrins, resulting in their recycling to the cell surface where they can be reused. SNX17 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. SNX17 binds Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270145  Cd Length: 113  Bit Score: 169.06  E-value: 4.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 292 YSYEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRITQVM---------DKISFQFEYLMA 362
Cdd:cd13337    1 YGYIQFEPCICDYPKPGTRVLVSIGNRELNFRLKDEEGKVKEGSFRVTRMRCWRITASHieedskkdeKKLELSFEYLMS 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 133901974 363 KDTFEWITLDTDQSILMSLLLQSIGSEILYEHN 395
Cdd:cd13337   81 KDKLQWITIRSDQAILMSLCLQSMVDELLRKKN 113
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 3-109 8.02e-49

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: 162.88  E-value: 8.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   3 HVDVPDTKTLVERsdGITKYTAYNIHINGWYHGSVRFSHLYEFAELIKQKFSQRyKGPEFPAKKLFKLDPKAIDERRQKI 82
Cdd:cd06885    1 HFSIPDTQELSDE--GGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNR-KLPPFPPKKLLPLTPAQLEERRLQL 77

                         90       100
                 ....*....|....*....|....*..
gi 133901974  83 TKYFQALVQHPEVARHYLVEKKLLGFQ 109
Cdd:cd06885   78 EKYLQAVVQDPRIANSDIFNSFLLNAQ 104
FERM_F1_SNX17 cd16121
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 118-229 2.71e-32

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 17 (SNX17); SNX17 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It localizes to early endosomes, and plays an important role in mediating endocytic internalization, recycling, and/or protection from lysosomal degradation of NPxY-motif containing cell surface proteins including amyloid precursor protein (APP), P-selectin, beta1-integrin, low density lipoprotein receptor (LDLR), LDLR related protein (Lrp1), ApoER2, and FEEL1. SNX17 also affects T cell activation by regulating T cell receptor and integrin recycling. SNX17 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340538  Cd Length: 93  Bit Score: 118.49  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 118 QYVTLDVFLGNGEKTTIKCLVSDSTLEIMKIICEKLGFknKDQFIYHFGLFMAKGRDPTNACysvttenfnplLTRFLRN 197
Cdd:cd16121    1 EEVSLDVFLMNGQKITVNISSTDQTDDVLEAVASKLGL--PEELVYYFALFLVKKDDDGNNT-----------IVRKLQD 67

                         90       100       110
                 ....*....|....*....|....*....|..
gi 133901974 198 FEAPFVSLSTANQkynengHYHFLCLRKLIWD 229
Cdd:cd16121   68 FESPYLSLKSAGK------GSHRIVLRKSYWD 93
SNX17_FERM_C pfam18116
Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 ...
 294-391 2.70e-27

Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 (SNX17) present in Homo sapiens. SNX17 localizes to early endosomes where it directly binds NPX(Y/F) motifs in the target receptors to mediate their rates of endocytic internalization, recycling, or degradation. The domain is known as terminal band 4.1/ezrin/radixin/moesin (FERM) domain. The FERM domain binds directly to the common motif, NPX(Y/F), in the cytoplasmic region of its target proteins.


Pssm-ID: 436285  Cd Length: 109  Bit Score: 105.19  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974  294 YEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRITQVMDK----------ISFQFEYLMAK 363
Cdd:pfam18116   2 YIQFDPCTCDYPEPDSRVTVSVGNNELNCCITLPEKETEEAAFKVTRMRCWRVTALDNKsmspqdneqgLELSFEYLFSK 81

                          90       100
                  ....*....|....*....|....*...
gi 133901974  364 DTFEWITLDTDQSILMSLLLQSIGSEIL 391
Cdd:pfam18116  82 DELKWITIASEQAILLSMCLQSMVDELL 109
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 14-101 1.35e-13

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 66.60  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974    14 ERSDGITKYTAYNIHING---WYHGSVRFSHLYEFAELIKQKFSqRYKGPEFPAKKLF----KLDPKAIDERRQKITKYF 86
Cdd:smart00312   6 KIGDGKHYYYVIEIETKTgleEWTVSRRYSDFLELHSKLKKHFP-RSILPPLPGKKLFgrlnNFSEEFIEKRRRGLEKYL 84

                           90
                   ....*....|....*
gi 133901974    87 QALVQHPEVARHYLV 101
Cdd:smart00312  85 QSLLNHPELINHSEV 99
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 25-101 1.81e-13

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 65.73  E-value: 1.81e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133901974   25 YNIHINGWYHGSVRFSHLYEFAELIKQKFSQRyKGPEFPAKK-LFKLDPKAIDERRQKITKYFQALVQHPEVARHYLV 101
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSV-IIPPLPPKRwLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVL 77
 
Name Accession Description Interval E-value
FERM-like_C_SNX17 cd13337
Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding ...
 292-395 4.10e-51

Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding protein that interacts with the free kindlin-binding site in endosomes to stabilize beta1 integrins, resulting in their recycling to the cell surface where they can be reused. SNX17 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. SNX17 binds Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270145  Cd Length: 113  Bit Score: 169.06  E-value: 4.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 292 YSYEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRITQVM---------DKISFQFEYLMA 362
Cdd:cd13337    1 YGYIQFEPCICDYPKPGTRVLVSIGNRELNFRLKDEEGKVKEGSFRVTRMRCWRITASHieedskkdeKKLELSFEYLMS 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 133901974 363 KDTFEWITLDTDQSILMSLLLQSIGSEILYEHN 395
Cdd:cd13337   81 KDKLQWITIRSDQAILMSLCLQSMVDELLRKKN 113
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 3-109 8.02e-49

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: 162.88  E-value: 8.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   3 HVDVPDTKTLVERsdGITKYTAYNIHINGWYHGSVRFSHLYEFAELIKQKFSQRyKGPEFPAKKLFKLDPKAIDERRQKI 82
Cdd:cd06885    1 HFSIPDTQELSDE--GGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNR-KLPPFPPKKLLPLTPAQLEERRLQL 77

                         90       100
                 ....*....|....*....|....*..
gi 133901974  83 TKYFQALVQHPEVARHYLVEKKLLGFQ 109
Cdd:cd06885   78 EKYLQAVVQDPRIANSDIFNSFLLNAQ 104
FERM_F1_SNX17 cd16121
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 118-229 2.71e-32

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 17 (SNX17); SNX17 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It localizes to early endosomes, and plays an important role in mediating endocytic internalization, recycling, and/or protection from lysosomal degradation of NPxY-motif containing cell surface proteins including amyloid precursor protein (APP), P-selectin, beta1-integrin, low density lipoprotein receptor (LDLR), LDLR related protein (Lrp1), ApoER2, and FEEL1. SNX17 also affects T cell activation by regulating T cell receptor and integrin recycling. SNX17 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340538  Cd Length: 93  Bit Score: 118.49  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 118 QYVTLDVFLGNGEKTTIKCLVSDSTLEIMKIICEKLGFknKDQFIYHFGLFMAKGRDPTNACysvttenfnplLTRFLRN 197
Cdd:cd16121    1 EEVSLDVFLMNGQKITVNISSTDQTDDVLEAVASKLGL--PEELVYYFALFLVKKDDDGNNT-----------IVRKLQD 67

                         90       100       110
                 ....*....|....*....|....*....|..
gi 133901974 198 FEAPFVSLSTANQkynengHYHFLCLRKLIWD 229
Cdd:cd16121   68 FESPYLSLKSAGK------GSHRIVLRKSYWD 93
SNX17_FERM_C pfam18116
Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 ...
 294-391 2.70e-27

Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 (SNX17) present in Homo sapiens. SNX17 localizes to early endosomes where it directly binds NPX(Y/F) motifs in the target receptors to mediate their rates of endocytic internalization, recycling, or degradation. The domain is known as terminal band 4.1/ezrin/radixin/moesin (FERM) domain. The FERM domain binds directly to the common motif, NPX(Y/F), in the cytoplasmic region of its target proteins.


Pssm-ID: 436285  Cd Length: 109  Bit Score: 105.19  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974  294 YEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRITQVMDK----------ISFQFEYLMAK 363
Cdd:pfam18116   2 YIQFDPCTCDYPEPDSRVTVSVGNNELNCCITLPEKETEEAAFKVTRMRCWRVTALDNKsmspqdneqgLELSFEYLFSK 81

                          90       100
                  ....*....|....*....|....*...
gi 133901974  364 DTFEWITLDTDQSILMSLLLQSIGSEIL 391
Cdd:pfam18116  82 DELKWITIASEQAILLSMCLQSMVDELL 109
FERM-like_C_SNX cd13207
Atypical FERM-like domain C-lobe of Sorting nexin family; Sorting nexins function in ...
 294-391 6.17e-15

Atypical FERM-like domain C-lobe of Sorting nexin family; Sorting nexins function in regulating recycling from endosomes to the cell surface. SNX17, SNX27, and SNX31 contain a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. All three proteins are able to bind the Ras GTPase through their FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275395  Cd Length: 116  Bit Score: 70.82  E-value: 6.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 294 YEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRITQVMDKIS-------------FQFEYL 360
Cdd:cd13207    2 YLIFDHCSCDSPEGHVITVISIGNFELSACTELPDSQTQGQLFNQVRAFCWDVTQRWDLLDtdgpqrtdeegleLCFEYA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 133901974 361 MAKDTFEWITLDTDQSILMSLLLQSIGSEIL 391
Cdd:cd13207   82 RGEKKPQWVKIFTPQANYMSECLERMFCELM 112
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 14-101 1.35e-13

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 66.60  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974    14 ERSDGITKYTAYNIHING---WYHGSVRFSHLYEFAELIKQKFSqRYKGPEFPAKKLF----KLDPKAIDERRQKITKYF 86
Cdd:smart00312   6 KIGDGKHYYYVIEIETKTgleEWTVSRRYSDFLELHSKLKKHFP-RSILPPLPGKKLFgrlnNFSEEFIEKRRRGLEKYL 84

                           90
                   ....*....|....*
gi 133901974    87 QALVQHPEVARHYLV 101
Cdd:smart00312  85 QSLLNHPELINHSEV 99
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 25-101 1.81e-13

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 65.73  E-value: 1.81e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133901974   25 YNIHINGWYHGSVRFSHLYEFAELIKQKFSQRyKGPEFPAKK-LFKLDPKAIDERRQKITKYFQALVQHPEVARHYLV 101
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSV-IIPPLPPKRwLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVL 77
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 3-103 5.38e-12

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: 62.38  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   3 HVDVPDTKTlveRSDGITKYTAYNIHI----NGWYHGSVRFSHLYEFAELIKQKFSQRYKgPEFPAKKLFK-LDPKAIDE 77
Cdd:cd06093    1 SVSIPDYEK---VKDGGKKYVVYIIEVttqgGEEWTVYRRYSDFEELHEKLKKKFPGVIL-PPLPPKKLFGnLDPEFIEE 76

                         90       100
                 ....*....|....*....|....*.
gi 133901974  78 RRQKITKYFQALVQHPEVARHYLVEK 103
Cdd:cd06093   77 RRKQLEQYLQSLLNHPELRNSEELKE 102
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 294-389 6.93e-09

Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling from endosomes to the cell surface. SNX31 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. It bind Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275415  Cd Length: 113  Bit Score: 53.74  E-value: 6.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 294 YEIMSPCSCDYPKPGTPCEIKFGRRQIIMTTRDETGKPKPSIFRATRIRVWRIT-------QVMDK----ISFQFEYlMA 362
Cdd:cd13336    2 YLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTflgpkkqEVMSPlhqhLELRFEY-QQ 80

                         90       100
                 ....*....|....*....|....*..
gi 133901974 363 KDTFEWITLDTDQSILMSLLLQSIGSE 389
Cdd:cd13336   81 GSSWKWIVIRTKQAFLLSSCLKKMISE 107
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 2-87 1.06e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; 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. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.


Pssm-ID: 132796  Cd Length: 106  Bit Score: 52.80  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   2 IHVDVPDTKTlVERSDgiTKYTAYNIHINGWYHGSVRFSHLYEFAELIKQKFSQrYKGPEFPAKKLFKLDPKAIDERRQK 81
Cdd:cd06886    4 VPISIPDYKH-VEQNG--EKFVVYNIYMAGRQLCSRRYREFANLHQNLKKEFPD-FQFPKLPGKWPFSLSEQQLDARRRG 79


                 ....*.
gi 133901974  82 ITKYFQ 87
Cdd:cd06886   80 LEQYLE 85
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 3-95 2.01e-06

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: 46.50  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   3 HVDVPDTKtlvERSDgitKYTAYNIHINGWYHGSV---RFShlyEFAELIKQKFSQRYKGP--EFPAKKLFKL---DPKA 74
Cdd:cd06897    2 EISIPTTS---VSPK---PYTVYNIQVRLPLRSYTvsrRYS---EFVALHKQLESEVGIEPpyPLPPKSWFLStssNPKL 72

                         90       100
                 ....*....|....*....|.
gi 133901974  75 IDERRQKITKYFQALVQHPEV 95
Cdd:cd06897   73 VEERRVGLEAFLRALLNDEDS 93
FERM_F1_SNX17_like cd17109
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in PX-FERM family ...
 120-229 3.72e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in PX-FERM family sorting nexin proteins; This family includes three endosome-associated PX (Phox homology) and FERM (Band 4.1, ezrin, radixin, moesin) domain-containing proteins called sorting nexin (SNX) 17, SNX27, and SNX31, which are modular peripheral membrane proteins acting as central scaffolds mediating protein-lipid interactions, cargo binding, and regulatory protein recruitment. They are key regulators of endosomal recycling and bind conserved NPX(Y/F) peptide sorting motifs in transmembrane cargos via an atypical FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340629  Cd Length: 93  Bit Score: 45.28  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974 120 VTLDVFLGNGEKTTIKCLVSDSTLEIMKIICEKLGFknKDQFIYHFGLFMAkgRDPTNACYSVttenfnpllTRFLRNFE 199
Cdd:cd17109    3 VELRVALPNGQTVTVRVKTSDTTEQVLEAVAAKVGL--DSTLVGYFALFLV--RSHSEGKLSF---------VRKLAPFE 69

                         90       100       110
                 ....*....|....*....|....*....|
gi 133901974 200 APFVSLStanQKYNENghyHFLCLRKLIWD 229
Cdd:cd17109   70 LPYVSYI---SNYTPG---TKLTLRKWYFT 93
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 22-100 1.80e-04

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: 40.72  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974  22 YTAYNIHI--NGWYHgSV--RFSHLYEFAELIKQKfsqrYKGPEFPAKKLFKLDPKAIDERRQKITKYFQALVQHPEVAR 97
Cdd:cd06880   19 YTVFTIEVlvNGRRH-TVekRYSEFHALHKKLKKS----IKTPDFPPKRVRNWNPKVLEQRRQGLEAYLQGLLKINELPK 93


                 ...
gi 133901974  98 HYL 100
Cdd:cd06880   94 QLL 96
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 4-96 6.96e-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: 39.23  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974   4 VDVPDTkTLVERSDGITKYTAYNIHINGWYHGSV------RFSHLYEFAELIKQKFSQRYKG--PEFPAKKLF-----KL 70
Cdd:cd07280    5 VNVGDY-TIVGGDTGGGAYVVWKITIETKDLIGSsivaykRYSEFVQLREALLDEFPRHKRNeiPQLPPKVPWydsrvNL 83

                         90       100
                 ....*....|....*....|....*.
gi 133901974  71 DPKAIDERRQKITKYFQALVQHPEVA 96
Cdd:cd07280   84 NKAWLEKRRRGLQYFLNCVLLNPVFG 109
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 21-98 9.06e-04

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: 38.93  E-value: 9.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974  21 KYTAYNIHI---NGWYHGSVRFSHLYEFAELIKQKF-SQRYKgpeFPAKKLF--KLDPKAIDERRQKITKYFQALVQHPE 94
Cdd:cd06870   19 RFTVYKVVVsvgRSSWFVFRRYAEFDKLYESLKKQFpASNLK---IPGKRLFgnNFDPDFIKQRRAGLDEFIQRLVSDPK 95


                 ....
gi 133901974  95 VARH 98
Cdd:cd06870   96 LLNH 99
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 11-95 1.21e-03

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


Pssm-ID: 132786  Cd Length: 133  Bit Score: 38.83  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901974  11 TLVERSDGITKYTAYNIHINGWYHGSV--------RFSHLYE--------FAELIKQKFSQRYKGPEFPAKKLFkldpka 74
Cdd:cd06876   27 YISDVEEEGKEFVVYLIEVQRLNNDDQssgwvvarRYSEFLElhkylkkrYPGVLKLDFPQKRKISLKYSKTLL------ 100

                         90       100
                 ....*....|....*....|.
gi 133901974  75 IDERRQKITKYFQALVQHPEV 95
Cdd:cd06876  101 VEERRKALEKYLQELLKIPEV 121
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 38-99 2.42e-03

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


Pssm-ID: 132783  Cd Length: 120  Bit Score: 38.02  E-value: 2.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133901974  38 RFSHLYEFAELIKQKFSQRYKGPeFPAKKLFK-LDPKAIDERRQKITKYFQALVQhPEVARHY 99
Cdd:cd06873   46 RYSDFHDLHMRLKEKFPNLSKLS-FPGKKTFNnLDRAFLEKRRKMLNQYLQSLLN-PEVLDAN 106
 
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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