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Conserved domains on  [gi|578838523|ref|XP_006724772|]
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FERM and PDZ domain-containing protein 3 isoform X5 [Homo sapiens]

Protein Classification

ubiquitin family protein( domain architecture ID 13219386)

ubiquitin family protein such as polyubiquitin, which when attached to a target protein, has different functions depending on the Lys residue of the ubiquitin that is linked

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_FRMPD1_FRMPD3_FRMPD4 cd13183
FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The ...
 191-294 2.00e-52

FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the 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: 270004  Cd Length: 105  Bit Score: 179.13  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523  191 TGVLFNTVGL-DEKQSATTLLVGPRHGISHVIDLKTNLTTVLSEFSKISKIQLFRENQGVARVETSIMDAKPLVLLMEWP 269
Cdd:cd13183     1 GGRSFQATLMlQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDVKPITLLMESP 80

                          90       100
                  ....*....|....*....|....*
gi 578838523  270 EATNFACLIAGYCRLLLDSRKMVFS 294
Cdd:cd13183    81 DAKDLACLIAGYYRLLVDPRRSIFS 105
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 1-65 2.10e-38

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17169:

Pssm-ID: 475130  Cd Length: 93  Bit Score: 138.80  E-value: 2.10e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578838523    1 MLTLQDRLSLRFIEHFALVLEYAGPEQNHKFLLLQDKQPLAYVVQRTHYHGMKCLFRISFFPKDP 65
Cdd:cd17169    29 MLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAHVVQRTHYQGMKCLFRICFFPKDP 93
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 3-195 8.33e-26

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: 106.61  E-value: 8.33e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523      3 TLQDRLSLRFIEHFALVLEYagPEQNHKFLLLQDKQPLAYVVQRTHYhgmKCLFRISFFPKDPvELLRRDPAAFEYLYIQ 82
Cdd:smart00295   28 TVCRKLGIRESEYFGLQFED--PDEDLRHWLDPAKTLLDQDVKSEPL---TLYFRVKFYPPDP-NQLKEDPTRLNLLYLQ 101

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523     83 SRNDVIRERFGMDpkPEMLLGLAALHIYITVsatrPSQKISLKNVEKEWGLEPFLPPSLLQVIKEKNLRKSLSQQLKAHq 162
Cdd:smart00295  102 VRNDILEGRLPCP--EEEALLLAALALQAEF----GDYDEELHDLRGELSLKRFLPKQLLDSRKLKEWRERIVELHKEL- 174

                           170       180       190
                    ....*....|....*....|....*....|...
gi 578838523    163 thpsCGTkgSAIQAKLQYLRILNELPTFtGVLF 195
Cdd:smart00295  175 ----IGL--SPEEAKLKYLELARKLPTY-GVEL 200
 
Name Accession Description Interval E-value
FERM_C_FRMPD1_FRMPD3_FRMPD4 cd13183
FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The ...
 191-294 2.00e-52

FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the 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: 270004  Cd Length: 105  Bit Score: 179.13  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523  191 TGVLFNTVGL-DEKQSATTLLVGPRHGISHVIDLKTNLTTVLSEFSKISKIQLFRENQGVARVETSIMDAKPLVLLMEWP 269
Cdd:cd13183     1 GGRSFQATLMlQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDVKPITLLMESP 80

                          90       100
                  ....*....|....*....|....*
gi 578838523  270 EATNFACLIAGYCRLLLDSRKMVFS 294
Cdd:cd13183    81 DAKDLACLIAGYYRLLVDPRRSIFS 105
FERM_F1_FRMPD3 cd17169
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 1-65 2.10e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 3 (FRMPD3); FRMPD3 is an uncharacterized FERM and PDZ domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340689  Cd Length: 93  Bit Score: 138.80  E-value: 2.10e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578838523    1 MLTLQDRLSLRFIEHFALVLEYAGPEQNHKFLLLQDKQPLAYVVQRTHYHGMKCLFRISFFPKDP 65
Cdd:cd17169    29 MLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAHVVQRTHYQGMKCLFRICFFPKDP 93
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 3-195 8.33e-26

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: 106.61  E-value: 8.33e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523      3 TLQDRLSLRFIEHFALVLEYagPEQNHKFLLLQDKQPLAYVVQRTHYhgmKCLFRISFFPKDPvELLRRDPAAFEYLYIQ 82
Cdd:smart00295   28 TVCRKLGIRESEYFGLQFED--PDEDLRHWLDPAKTLLDQDVKSEPL---TLYFRVKFYPPDP-NQLKEDPTRLNLLYLQ 101

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523     83 SRNDVIRERFGMDpkPEMLLGLAALHIYITVsatrPSQKISLKNVEKEWGLEPFLPPSLLQVIKEKNLRKSLSQQLKAHq 162
Cdd:smart00295  102 VRNDILEGRLPCP--EEEALLLAALALQAEF----GDYDEELHDLRGELSLKRFLPKQLLDSRKLKEWRERIVELHKEL- 174

                           170       180       190
                    ....*....|....*....|....*....|...
gi 578838523    163 thpsCGTkgSAIQAKLQYLRILNELPTFtGVLF 195
Cdd:smart00295  175 ----IGL--SPEEAKLKYLELARKLPTY-GVEL 200
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 65-195 2.48e-25

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 102.35  E-value: 2.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523    65 PVELLRRDPAAFEYLYIQSRNDVIRERFGMDpkPEMLLGLAALHIYITVSATRPSQKISlknveKEWGLEPFLPPSLLQV 144
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCS--EEEALLLAALQLQAEFGDYQPSSHTS-----EYLSLESFLPKQLLRK 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578838523   145 IKEKNLRKSLSQQLKAHQThpscgtkGSAIQAKLQYLRILNELPTFTGVLF 195
Cdd:pfam00373   74 MKSKELEKRVLEAHKNLRG-------LSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 75-187 7.40e-14

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the 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, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 68.81  E-value: 7.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523   75 AFEYLYIQSRNDVIRERFGMDpkPEMLLGLAALHIYITVSATRPSQKislknVEKEWGLEPFLPPSLLQVIKEKNLRKSL 154
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCS--EETAALLAALALQAEYGDYDPSEH-----KPKYLSLKRFLPKQLLKQRKPEEWEKRI 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 578838523  155 SQQLKAHQTHpscgtkgSAIQAKLQYLRILNEL 187
Cdd:cd14473    74 VELHKKLRGL-------SPAEAKLKYLKIARKL 99
 
Name Accession Description Interval E-value
FERM_C_FRMPD1_FRMPD3_FRMPD4 cd13183
FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The ...
 191-294 2.00e-52

FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the 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: 270004  Cd Length: 105  Bit Score: 179.13  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523  191 TGVLFNTVGL-DEKQSATTLLVGPRHGISHVIDLKTNLTTVLSEFSKISKIQLFRENQGVARVETSIMDAKPLVLLMEWP 269
Cdd:cd13183     1 GGRSFQATLMlQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDVKPITLLMESP 80

                          90       100
                  ....*....|....*....|....*
gi 578838523  270 EATNFACLIAGYCRLLLDSRKMVFS 294
Cdd:cd13183    81 DAKDLACLIAGYYRLLVDPRRSIFS 105
FERM_F1_FRMPD3 cd17169
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 1-65 2.10e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 3 (FRMPD3); FRMPD3 is an uncharacterized FERM and PDZ domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340689  Cd Length: 93  Bit Score: 138.80  E-value: 2.10e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578838523    1 MLTLQDRLSLRFIEHFALVLEYAGPEQNHKFLLLQDKQPLAYVVQRTHYHGMKCLFRISFFPKDP 65
Cdd:cd17169    29 MLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAHVVQRTHYQGMKCLFRICFFPKDP 93
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 3-195 8.33e-26

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: 106.61  E-value: 8.33e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523      3 TLQDRLSLRFIEHFALVLEYagPEQNHKFLLLQDKQPLAYVVQRTHYhgmKCLFRISFFPKDPvELLRRDPAAFEYLYIQ 82
Cdd:smart00295   28 TVCRKLGIRESEYFGLQFED--PDEDLRHWLDPAKTLLDQDVKSEPL---TLYFRVKFYPPDP-NQLKEDPTRLNLLYLQ 101

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523     83 SRNDVIRERFGMDpkPEMLLGLAALHIYITVsatrPSQKISLKNVEKEWGLEPFLPPSLLQVIKEKNLRKSLSQQLKAHq 162
Cdd:smart00295  102 VRNDILEGRLPCP--EEEALLLAALALQAEF----GDYDEELHDLRGELSLKRFLPKQLLDSRKLKEWRERIVELHKEL- 174

                           170       180       190
                    ....*....|....*....|....*....|...
gi 578838523    163 thpsCGTkgSAIQAKLQYLRILNELPTFtGVLF 195
Cdd:smart00295  175 ----IGL--SPEEAKLKYLELARKLPTY-GVEL 200
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 65-195 2.48e-25

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 102.35  E-value: 2.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523    65 PVELLRRDPAAFEYLYIQSRNDVIRERFGMDpkPEMLLGLAALHIYITVSATRPSQKISlknveKEWGLEPFLPPSLLQV 144
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCS--EEEALLLAALQLQAEFGDYQPSSHTS-----EYLSLESFLPKQLLRK 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578838523   145 IKEKNLRKSLSQQLKAHQThpscgtkGSAIQAKLQYLRILNELPTFTGVLF 195
Cdd:pfam00373   74 MKSKELEKRVLEAHKNLRG-------LSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_F1_FRMPD1_like cd17088
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 1-62 1.33e-24

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing proteins FRMPD1, FRMPD3, FRMPD4, and similar proteins; This family includes FERM and PDZ domain-containing proteins FRMPD1, FRMPD3, and FRMPD4, which all contain a PDZ domain and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMPD1, also termed FERM domain-containing protein 2, is an activator of G-protein signaling 3 (AGS3)-binding protein that regulates the subcellular location of AGS3 and its interaction with G-proteins. FRMPD4, also termed PDZ domain-containing protein 10, or PSD-95-interacting regulator of spine morphogenesis (Preso), is a multiscaffolding protein that modulates both Homer1 and post-synaptic density protein 95 activity. Both FRMPD1 and FRMPD4 can associate with the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. The biological role of FRMPD3 remains unclear.


Pssm-ID: 340608  Cd Length: 90  Bit Score: 99.27  E-value: 1.33e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838523    1 MLTLQDRLSLRFIEHFALVLEYAGPEQNHKFLLLQDKQPLAYVVQRTHYHGMKCLFRISFFP 62
Cdd:cd17088    29 LLSLQEKLGIKSMEHFSLVLEYVKSPRTNKLSLLQPDESLAQVAARPGSHHLRCLFRISFVP 90
FERM_F1_FRMPD4 cd17170
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 1-65 3.01e-17

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 4 (FRMPD4); FRMPD4, also termed PDZ domain-containing protein 10, or PSD-95-interacting regulator of spine morphogenesis (Preso), is a multiscaffolding protein that modulates both Homer1 and postsynaptic density protein 95 activity. It can associate with the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. Moreover, FRMPD4 is asymmetrically distributed in the cytosol and nuclei of neural stem/progenitor cells in the adult brain, suggesting a significant role in cell differentiation via association with cell polarity machinery. FRMPD4 contains a WW domain, a PDZ domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340690  Cd Length: 94  Bit Score: 78.56  E-value: 3.01e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578838523    1 MLTLQDRLSLRFIEHFALVLEYAGPEQNHKFLLLQDKQPLAYVVQRTHYHGMKCLFRISFFPKDP 65
Cdd:cd17170    30 ILTLQEKLSIKCIEHFSLMLEQRTEGSGTKLLLLHEQETLTQVTQRPGSHKMRCLFRISFVPKDP 94
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 75-187 7.40e-14

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the 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, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 68.81  E-value: 7.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523   75 AFEYLYIQSRNDVIRERFGMDpkPEMLLGLAALHIYITVSATRPSQKislknVEKEWGLEPFLPPSLLQVIKEKNLRKSL 154
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCS--EETAALLAALALQAEYGDYDPSEH-----KPKYLSLKRFLPKQLLKQRKPEEWEKRI 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 578838523  155 SQQLKAHQTHpscgtkgSAIQAKLQYLRILNEL 187
Cdd:cd14473    74 VELHKKLRGL-------SPAEAKLKYLKIARKL 99
FERM_F1_FRMPD1 cd17168
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 1-64 1.57e-11

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 1 (FRMPD1); FRMPD1, also termed FERM domain-containing protein 2, is an activator of G-protein signaling 3 (AGS3)-binding protein that regulates the subcellular location of AGS3 and its interaction with G-proteins. It also binds to the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. FRMPD1 contains a PDZ domain and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340688  Cd Length: 90  Bit Score: 61.81  E-value: 1.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578838523    1 MLTLQDRLSLRFIEHFALVLEyagpEQNH--KFLLLQDKQPLAYVVQRTHYHGMKCLFRISFFPKD 64
Cdd:cd17168    29 ILTLKEKLSIRSIEHFALVLE----EQYSisKLYLLHEEELIEQVVEKRESHDYRCLFRVCFVPKD 90
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 193-286 2.54e-09

FERM domain C-lobe; The 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. The FERM domain is found in the 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: 275389  Cd Length: 93  Bit Score: 55.84  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523  193 VLFNTVGLDEKQSATTLLVGPrHGIsHVIDLKTNLTTVLSEFSKISKIQLFRENqgvaRVETSIMD-AKPLVLLMEWP-- 269
Cdd:cd00836     3 EFFPVKDKSKKGSPIILGVNP-EGI-SVYDELTGQPLVLFPWPNIKKISFSGAK----KFTIVVADeDKQSKLLFQTPsr 76

                          90
                  ....*....|....*..
gi 578838523  270 EATNFACLIAGYCRLLL 286
Cdd:cd00836    77 QAKEIWKLIVGYHRFLL 93
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
 206-296 5.02e-08

FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion kinase-related nonkinase; p125FAK/pp125FAK;PTK2/Protein-tyrosine kinase 2 protein tyrosine kinase 2 (PTK2) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. It has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival. The N-terminal region of FAK1 contains a FERM domain, a linker, a kinase domain, and a C-terminal FRNK (FAK-related-non-kinase) domain. Three subdomains of FERM: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), form a cloverleaf fold, similar to those of known FERM structures despite the low sequence conservation. The C-lobe/F3 within the FERM domain is part of the PH domain family. The phosphoinositide-binding site found in ERM family proteins is not present in the FERM domain of FAK1. The adjacent Src SH3 and SH2 binding sites in the linker of FAK1 associates with the F3 and F1 lobes and are thought to be involved in regulation. The FERM domain of FAK1 can inhibit enzymatic activity and repress FAK signaling. In an inactive state of FAK1, the FERM domain is thought to interact with the catalytic domain of FAK1 to repress its activity. Upon activation this interaction is disrupted and its kinase activity restored. The FRNK domain is thought to function as a negative regulator of kinase activity. The C-lobe/F3 is the third structural domain within the FERM domain. The FERM domain is found in the 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: 270011  Cd Length: 111  Bit Score: 52.63  E-value: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838523  206 ATTLLVGPRHGISHVIDLKTNLTTvLSEFSKISKIQLFRENQGVAR------VETSimdAKPLVL-LMEWPEATNFACLI 278
Cdd:cd13190    16 PVDLVIGPEVGISYLTDKGSAPTH-LADFEQIQSIQTSKSEDKDGKallqlkIAGA---SEPLSItCSSLATAESLADLI 91

                          90
                  ....*....|....*...
gi 578838523  279 AGYCRLLLDSRKMVFSRP 296
Cdd:cd13190    92 DGYCRLVNQTDSSLIIRP 109
 
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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