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Conserved domains on  [gi|2462618068|ref|XP_054215869|]
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sorting nexin-31 isoform X11 [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 171-285 1.88e-69

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: 212.44  E-value: 1.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 171 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGpqRTLNQNLELRFQY 250
Cdd:cd13336     1 GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVM--SPLHQHLELRFEY 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462618068 251 SEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 285
Cdd:cd13336    79 QQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS 113
FERM_F1_SNX31 cd16122
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 13-110 4.18e-57

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31); SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 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: 340539  Cd Length: 98  Bit Score: 180.33  E-value: 4.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068  13 IATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGS 92
Cdd:cd16122     1 IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAPFELPYVTLES 80

                          90
                  ....*....|....*...
gi 2462618068  93 SEVENCKVGLRKWYMAPS 110
Cdd:cd16122    81 GEMERCKLGIRKWYMDPS 98
 
Name Accession Description Interval E-value
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 171-285 1.88e-69

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: 212.44  E-value: 1.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 171 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGpqRTLNQNLELRFQY 250
Cdd:cd13336     1 GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVM--SPLHQHLELRFEY 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462618068 251 SEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 285
Cdd:cd13336    79 QQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS 113
FERM_F1_SNX31 cd16122
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 13-110 4.18e-57

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31); SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 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: 340539  Cd Length: 98  Bit Score: 180.33  E-value: 4.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068  13 IATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGS 92
Cdd:cd16122     1 IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAPFELPYVTLES 80

                          90
                  ....*....|....*...
gi 2462618068  93 SEVENCKVGLRKWYMAPS 110
Cdd:cd16122    81 GEMERCKLGIRKWYMDPS 98
SNX17_FERM_C pfam18116
Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 ...
 171-281 2.54e-48

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: 157.96  E-value: 2.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 171 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTllDTDGPQrTLNQNLELRFQY 250
Cdd:pfam18116   1 GYIQFDPCTCDYPEPDSRVTVSVGNNELNCCITLPEKETEEAAFKVTRMRCWRVTALDN--KSMSPQ-DNEQGLELSFEY 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462618068 251 SED-SCWQWFVIYTKQAFLLSSCLKKMISEKM 281
Cdd:pfam18116  78 LFSkDELKWITIASEQAILLSMCLQSMVDELL 109
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 22-152 5.38e-05

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 43.44  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068   22 IFLPNEQSIRIEIITSDTAERVLEVVSHKIGL-CREllgYFGLFLIRFGKEGK--LSVVKKLADFElpyvslgsSEVENC 98
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIrESE---YFGLQFEDPDEDLRhwLDPAKTLLDQD--------VKSEPL 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462618068   99 KVGLRKWYMaPSLDSVLMDCRVAVDLLYMQAIQDIEKGWAKPTQAQRQKLEAFQ 152
Cdd:smart00295  73 TLYFRVKFY-PPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALA 125
 
Name Accession Description Interval E-value
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 171-285 1.88e-69

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: 212.44  E-value: 1.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 171 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGpqRTLNQNLELRFQY 250
Cdd:cd13336     1 GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVM--SPLHQHLELRFEY 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462618068 251 SEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 285
Cdd:cd13336    79 QQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS 113
FERM-like_C_SNX cd13207
Atypical FERM-like domain C-lobe of Sorting nexin family; Sorting nexins function in ...
 171-285 1.58e-61

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: 192.16  E-value: 1.58e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 171 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGPQRTLNQNLELRFQY 250
Cdd:cd13207     1 GYLIFDHCSCDSPEGHVITVISIGNFELSACTELPDSQTQGQLFNQVRAFCWDVTQRWDLLDTDGPQRTDEEGLELCFEY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462618068 251 SED-SCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 285
Cdd:cd13207    81 ARGeKKPQWVKIFTPQANYMSECLERMFCELMVKKE 116
FERM_F1_SNX31 cd16122
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 13-110 4.18e-57

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31); SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 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: 340539  Cd Length: 98  Bit Score: 180.33  E-value: 4.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068  13 IATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGS 92
Cdd:cd16122     1 IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAPFELPYVTLES 80

                          90
                  ....*....|....*...
gi 2462618068  93 SEVENCKVGLRKWYMAPS 110
Cdd:cd16122    81 GEMERCKLGIRKWYMDPS 98
FERM_F1_SNX17_like cd17109
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in PX-FERM family ...
 16-108 4.40e-50

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: 162.00  E-value: 4.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068  16 KKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGSSEV 95
Cdd:cd17109     1 SDVELRVALPNGQTVTVRVKTSDTTEQVLEAVAAKVGLDSTLVGYFALFLVRSHSEGKLSFVRKLAPFELPYVSYISNYT 80

                          90
                  ....*....|...
gi 2462618068  96 ENCKVGLRKWYMA 108
Cdd:cd17109    81 PGTKLTLRKWYFT 93
SNX17_FERM_C pfam18116
Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 ...
 171-281 2.54e-48

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: 157.96  E-value: 2.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 171 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTllDTDGPQrTLNQNLELRFQY 250
Cdd:pfam18116   1 GYIQFDPCTCDYPEPDSRVTVSVGNNELNCCITLPEKETEEAAFKVTRMRCWRVTALDN--KSMSPQ-DNEQGLELSFEY 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462618068 251 SED-SCWQWFVIYTKQAFLLSSCLKKMISEKM 281
Cdd:pfam18116  78 LFSkDELKWITIASEQAILLSMCLQSMVDELL 109
FERM-like_C_SNX17 cd13337
Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding ...
 170-283 1.35e-26

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: 101.65  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068 170 YGYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGPqrtlNQNLELRFQ 249
Cdd:cd13337     1 YGYIQFEPCICDYPKPGTRVLVSIGNRELNFRLKDEEGKVKEGSFRVTRMRCWRITASHIEEDSKKD----EKKLELSFE 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462618068 250 Y--SEDsCWQWFVIYTKQAFLLSSCLKKMISEKMVK 283
Cdd:cd13337    77 YlmSKD-KLQWITIRSDQAILMSLCLQSMVDELLRK 111
FERM_F1_SNX17 cd16121
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 20-106 7.42e-25

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: 96.15  E-value: 7.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068  20 LDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGSSEVENCK 99
Cdd:cd16121     5 LDVFLMNGQKITVNISSTDQTDDVLEAVASKLGLPEELVYYFALFLVKKDDDGNNTIVRKLQDFESPYLSLKSAGKGSHR 84


                  ....*..
gi 2462618068 100 VGLRKWY 106
Cdd:cd16121    85 IVLRKSY 91
FERM_F1_SNX27 cd01777
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 20-110 5.28e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 27 (SNX27); SNX27 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. In addition to a PX (Phox homology) domain that regulates its endosomal localization, SNX27 has a unique PDZ (Psd-95/Dlg/ZO1) domain and an atypical FERM (4.1, ezrin, radixin, moesin) domain that both function to bind short peptide sequence motifs in the cytoplasmic domains of the cargo receptors. 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: 340475  Cd Length: 92  Bit Score: 46.91  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068  20 LDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRfgkegKLSVVKKLADFELP---YVSLGSSEVE 96
Cdd:cd01777     5 LKVLLPDRTTVTVSVKKNSNTDQVYQALVEKLGMDSETANYFALFEII-----EYNFERKLQPNEFPhnlYIQNYSTASA 79

                          90
                  ....*....|....
gi 2462618068  97 NCkVGLRKWYMAPS 110
Cdd:cd01777    80 TC-ITLRKWLFTLA 92
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 22-152 5.38e-05

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 43.44  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618068   22 IFLPNEQSIRIEIITSDTAERVLEVVSHKIGL-CREllgYFGLFLIRFGKEGK--LSVVKKLADFElpyvslgsSEVENC 98
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIrESE---YFGLQFEDPDEDLRhwLDPAKTLLDQD--------VKSEPL 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462618068   99 KVGLRKWYMaPSLDSVLMDCRVAVDLLYMQAIQDIEKGWAKPTQAQRQKLEAFQ 152
Cdd:smart00295  73 TLYFRVKFY-PPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALA 125
 
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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