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Conserved domains on  [gi|227116327|ref|NP_035732|]
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talin-1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
talin-RS cd12150
rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model ...
 1654-1826 1.28e-81

rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model interacts with its N-terminal FERM domain to mask its integrin-binding site and interferes with interactions between the FERM domain and the cellular membrane. Talin is a large and ubiquitous cytoskeletal protein concentrated at focal adhesion sites. It is involved in linking integrins to the actin cytoskeleton.


:

Pssm-ID: 213393  Cd Length: 172  Bit Score: 266.04  E-value: 1.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327 1654 KAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQ 1733
Cdd:cd12150     1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGEAEQLGHAVTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327 1734 MAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKqAAHTQEALEEAVQMMTEAVEDLTTT 1813
Cdd:cd12150    81 MAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPK-AVHAHPAVDEAAQMLKEAIEDLTQT 159

                         170
                  ....*....|...
gi 227116327 1814 LNEAASAAGVVGG 1826
Cdd:cd12150   160 LEEAASEAGVVSG 172
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 2336-2532 1.22e-76

I/LWEQ domain; Thought to possess an F-actin binding function.


:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 253.06  E-value: 1.22e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   2336 DESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALD-DGQWSQGLISAARMVAAATNNLCEAANAA 2414
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKkNSRWTEGLISAAKAVAAATNVLVEAADGV 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   2415 VQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAF-EDQENETVVVKEK 2493
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 227116327   2494 MVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKF 2532
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYEL 199
FERM_F1_TLN1 cd17173
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); ...
 86-197 4.49e-75

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain.


:

Pssm-ID: 340693  Cd Length: 112  Bit Score: 245.01  E-value: 4.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKL 165
Cdd:cd17173     1 RPLKIRMLDGTVKTVMVDDSKTVTDMLMTICARIGITNHDEYSLVREIMEEKKEEVTGTLKKDKTLLRDDKKMEKLKQKL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 227116327  166 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 197
Cdd:cd17173    81 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 112
Talin_middle pfam09141
Talin, middle domain; Members of this family adopt a structure consisting of five alpha ...
 491-652 9.85e-68

Talin, middle domain; Members of this family adopt a structure consisting of five alpha helices that fold into a bundle. They contain a Vinculin binding site (VBS) composed of a hydrophobic surface spanning five turns of helix four. Activation of the VBS causes subsequent recruitment of Vinculin, which enables maturation of small integrin/talin complexes into more stable adhesions. Formation of the complex between VBS and Vinculin requires prior unfolding of this middle domain: once released from the talin hydrophobic core, the VBS helix is then available to induce the 'bundle conversion' conformational change within the vinculin head domain thereby displacing the intramolecular interaction with the vinculin tail, allowing vinculin to bind actin.


:

Pssm-ID: 462691  Cd Length: 161  Bit Score: 226.01  E-value: 9.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   491 AQQALTGTINSSMQAVQAAQATLDDFETLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDY 570
Cdd:pfam09141    1 PQRALLGTISAGQEAIQAAEAELDTPAQLPPLGSDAASLQWRENTLDVSKQNVSSQLAAMNAATAQVVTLTSGPPDEIDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   571 TAVGCAVTTISSNLTEMSRGVKLLAALLEDEgGNGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGE 650
Cdd:pfam09141   81 TAVGAAITTISSNLPEMSKGVRMLAALMDDE-DSGDKLLDAARKLCGAFSDLLKAAQPESKEPRQNLLNAASRVGEASQQ 159


                   ..
gi 227116327   651 LL 652
Cdd:pfam09141  160 LL 161
VBS pfam08913
Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like ...
 1849-1973 2.34e-63

Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like molecules, enabling binding of vinculin to talin, stabilising integrin-mediated cell-matrix junctions. Talin, in turn, links integrins to the actin cytoskeleton. The consensus sequence for Vinculin binding sites is LxxAAxxVAxxVxxLIxxA, with a secondary structure prediction of four amphipathic helices. The hydrophobic residues that define the VBS are themselves 'masked' and are buried in the core of a series of helical bundles that make up the talin rod.


:

Pssm-ID: 430312  Cd Length: 125  Bit Score: 211.72  E-value: 2.34e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  1849 SFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASQAKPAAVAAENEEIGAHIKHRVQELGHGCS 1928
Cdd:pfam08913    1 TFVDYQTTMVRYAKAIAVTAQEMNTKSVTSPEELGQLASQMTSDYGQLAQQGIGASATAEPEEIGFQIRTRVQDLGHGCI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 227116327  1929 ALVTKAGALQCSPSDVYTKKELIECARRVSEKVSHVLAALQAGNR 1973
Cdd:pfam08913   81 VLVQKAGALQISPTDSYTKRELIECARAVSEKVSQVLAALQAGNR 125
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 88-313 9.71e-59

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: 201.75  E-value: 9.71e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327     88 LKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEkkdegtgtlrkdktllrdekkmeklkqklht 167
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDE------------------------------- 50

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    168 dDELNWLDHGRTLREQGVE-EHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQ 246
Cdd:smart00295   51 -DLRHWLDPAKTLLDQDVKsEPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAE 129

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227116327    247 FGPHNEQKH-KAGFLDLKDFLPKEYVKQKG----ERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFF 313
Cdd:smart00295  130 FGDYDEELHdLRGELSLKRFLPKQLLDSRKlkewRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
 309-400 2.31e-57

FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . 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: 269973  Cd Length: 92  Bit Score: 193.33  E-value: 2.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  309 GVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQI 388
Cdd:cd10569     1 GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYYSVQTTEGEQI 80

                          90
                  ....*....|..
gi 227116327  389 AQLIAGYIDIIL 400
Cdd:cd10569    81 SQLISGYIDIIL 92
FERM_F0_TLN1 cd17171
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); ...
 2-85 3.80e-57

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain.


:

Pssm-ID: 340691  Cd Length: 84  Bit Score: 192.49  E-value: 3.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    2 VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:cd17171     1 VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERVPEAQAGQPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 80


                  ....
gi 227116327   82 RKKQ 85
Cdd:cd17171    81 RKKQ 84
ILWEQ super family cl47033
I/LWEQ domain; Thought to possess an F-actin binding function.
 607-759 1.23e-03

I/LWEQ domain; Thought to possess an F-actin binding function.


The actual alignment was detected with superfamily member smart00307:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 42.35  E-value: 1.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    607 PLLQAAKGLAGAVSELLRSAQPAsaeprQNLLQAAGNVGQASGELLqqigesDTDPHFQDVLMQLAKAVASAAAALVLKA 686
Cdd:smart00307    9 SILEAAKAITKAIAALVKAATNA-----QREIVAQGRGGASPGEFY------KKNSRWTEGLISAAKAVAAATNVLVEAA 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227116327    687 KSVAQRTEDsglQTQVIAAATQCALSTSQLVACTKVVApTISSPVcQEQLVEAGRLVAKAVEGCVSASQAATE 759
Cdd:smart00307   78 DGVVTGKGS---EEELIVAAKEVAASTAQLVAASRVKA-DKDSQA-QDRLQAASKAVTNATANLVAAVKSGMI 145
 
Name Accession Description Interval E-value
talin-RS cd12150
rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model ...
 1654-1826 1.28e-81

rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model interacts with its N-terminal FERM domain to mask its integrin-binding site and interferes with interactions between the FERM domain and the cellular membrane. Talin is a large and ubiquitous cytoskeletal protein concentrated at focal adhesion sites. It is involved in linking integrins to the actin cytoskeleton.


Pssm-ID: 213393  Cd Length: 172  Bit Score: 266.04  E-value: 1.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327 1654 KAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQ 1733
Cdd:cd12150     1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGEAEQLGHAVTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327 1734 MAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKqAAHTQEALEEAVQMMTEAVEDLTTT 1813
Cdd:cd12150    81 MAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPK-AVHAHPAVDEAAQMLKEAIEDLTQT 159

                         170
                  ....*....|...
gi 227116327 1814 LNEAASAAGVVGG 1826
Cdd:cd12150   160 LEEAASEAGVVSG 172
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 2336-2532 1.22e-76

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 253.06  E-value: 1.22e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   2336 DESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALD-DGQWSQGLISAARMVAAATNNLCEAANAA 2414
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKkNSRWTEGLISAAKAVAAATNVLVEAADGV 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   2415 VQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAF-EDQENETVVVKEK 2493
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 227116327   2494 MVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKF 2532
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYEL 199
FERM_F1_TLN1 cd17173
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); ...
 86-197 4.49e-75

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain.


Pssm-ID: 340693  Cd Length: 112  Bit Score: 245.01  E-value: 4.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKL 165
Cdd:cd17173     1 RPLKIRMLDGTVKTVMVDDSKTVTDMLMTICARIGITNHDEYSLVREIMEEKKEEVTGTLKKDKTLLRDDKKMEKLKQKL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 227116327  166 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 197
Cdd:cd17173    81 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 112
Talin_middle pfam09141
Talin, middle domain; Members of this family adopt a structure consisting of five alpha ...
 491-652 9.85e-68

Talin, middle domain; Members of this family adopt a structure consisting of five alpha helices that fold into a bundle. They contain a Vinculin binding site (VBS) composed of a hydrophobic surface spanning five turns of helix four. Activation of the VBS causes subsequent recruitment of Vinculin, which enables maturation of small integrin/talin complexes into more stable adhesions. Formation of the complex between VBS and Vinculin requires prior unfolding of this middle domain: once released from the talin hydrophobic core, the VBS helix is then available to induce the 'bundle conversion' conformational change within the vinculin head domain thereby displacing the intramolecular interaction with the vinculin tail, allowing vinculin to bind actin.


Pssm-ID: 462691  Cd Length: 161  Bit Score: 226.01  E-value: 9.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   491 AQQALTGTINSSMQAVQAAQATLDDFETLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDY 570
Cdd:pfam09141    1 PQRALLGTISAGQEAIQAAEAELDTPAQLPPLGSDAASLQWRENTLDVSKQNVSSQLAAMNAATAQVVTLTSGPPDEIDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   571 TAVGCAVTTISSNLTEMSRGVKLLAALLEDEgGNGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGE 650
Cdd:pfam09141   81 TAVGAAITTISSNLPEMSKGVRMLAALMDDE-DSGDKLLDAARKLCGAFSDLLKAAQPESKEPRQNLLNAASRVGEASQQ 159


                   ..
gi 227116327   651 LL 652
Cdd:pfam09141  160 LL 161
VBS pfam08913
Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like ...
 1849-1973 2.34e-63

Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like molecules, enabling binding of vinculin to talin, stabilising integrin-mediated cell-matrix junctions. Talin, in turn, links integrins to the actin cytoskeleton. The consensus sequence for Vinculin binding sites is LxxAAxxVAxxVxxLIxxA, with a secondary structure prediction of four amphipathic helices. The hydrophobic residues that define the VBS are themselves 'masked' and are buried in the core of a series of helical bundles that make up the talin rod.


Pssm-ID: 430312  Cd Length: 125  Bit Score: 211.72  E-value: 2.34e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  1849 SFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASQAKPAAVAAENEEIGAHIKHRVQELGHGCS 1928
Cdd:pfam08913    1 TFVDYQTTMVRYAKAIAVTAQEMNTKSVTSPEELGQLASQMTSDYGQLAQQGIGASATAEPEEIGFQIRTRVQDLGHGCI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 227116327  1929 ALVTKAGALQCSPSDVYTKKELIECARRVSEKVSHVLAALQAGNR 1973
Cdd:pfam08913   81 VLVQKAGALQISPTDSYTKRELIECARAVSEKVSQVLAALQAGNR 125
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 88-313 9.71e-59

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: 201.75  E-value: 9.71e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327     88 LKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEkkdegtgtlrkdktllrdekkmeklkqklht 167
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDE------------------------------- 50

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    168 dDELNWLDHGRTLREQGVE-EHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQ 246
Cdd:smart00295   51 -DLRHWLDPAKTLLDQDVKsEPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAE 129

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227116327    247 FGPHNEQKH-KAGFLDLKDFLPKEYVKQKG----ERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFF 313
Cdd:smart00295  130 FGDYDEELHdLRGELSLKRFLPKQLLDSRKlkewRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
 309-400 2.31e-57

FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . 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: 269973  Cd Length: 92  Bit Score: 193.33  E-value: 2.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  309 GVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQI 388
Cdd:cd10569     1 GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYYSVQTTEGEQI 80

                          90
                  ....*....|..
gi 227116327  389 AQLIAGYIDIIL 400
Cdd:cd10569    81 SQLISGYIDIIL 92
FERM_F0_TLN1 cd17171
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); ...
 2-85 3.80e-57

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain.


Pssm-ID: 340691  Cd Length: 84  Bit Score: 192.49  E-value: 3.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    2 VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:cd17171     1 VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERVPEAQAGQPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 80


                  ....
gi 227116327   82 RKKQ 85
Cdd:cd17171    81 RKKQ 84
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
 2385-2531 5.82e-55

I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.


Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 188.95  E-value: 5.82e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  2385 DDGQWSQGLISAARMVAAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVK 2464
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227116327  2465 RASDNLVKAAQKAAAFEDQENETVVVKEK--MVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYK 2531
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEEIEEEMDFSKlsLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
FERM_f0 pfam16511
N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The ...
 4-83 3.39e-37

N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The fold is an ubiquitin-like fold joined to the f1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components, No binding partner has yet been found for it.


Pssm-ID: 465152  Cd Length: 81  Bit Score: 135.48  E-value: 3.39e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327     4 LSLKISI--GNVVKTMQFEPSTMVYDACRMIRERIPEAlAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:pfam16511    1 LSLKISIvgSNVTKTMQFDPSTTVYDACRLIREKIPEG-GLNASEYGLFLADEDPKKGRWLEPGRTLEYYDLRNGDELEY 79


                   ..
gi 227116327    82 RK 83
Cdd:pfam16511   80 KK 81
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 201-313 6.81e-37

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 135.86  E-value: 6.81e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   201 DQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKG----E 276
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKskelE 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 227116327   277 RKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFF 313
Cdd:pfam00373   81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 211-305 1.11e-27

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: 108.87  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  211 QLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKG----ERKIFQAHKNC 286
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKpeewEKRIVELHKKL 80

                          90
                  ....*....|....*....
gi 227116327  287 GQMSEIEAKVRYVKLARSL 305
Cdd:cd14473    81 RGLSPAEAKLKYLKIARKL 99
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 607-759 1.23e-03

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 42.35  E-value: 1.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    607 PLLQAAKGLAGAVSELLRSAQPAsaeprQNLLQAAGNVGQASGELLqqigesDTDPHFQDVLMQLAKAVASAAAALVLKA 686
Cdd:smart00307    9 SILEAAKAITKAIAALVKAATNA-----QREIVAQGRGGASPGEFY------KKNSRWTEGLISAAKAVAAATNVLVEAA 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227116327    687 KSVAQRTEDsglQTQVIAAATQCALSTSQLVACTKVVApTISSPVcQEQLVEAGRLVAKAVEGCVSASQAATE 759
Cdd:smart00307   78 DGVVTGKGS---EEELIVAAKEVAASTAQLVAASRVKA-DKDSQA-QDRLQAASKAVTNATANLVAAVKSGMI 145
 
Name Accession Description Interval E-value
talin-RS cd12150
rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model ...
 1654-1826 1.28e-81

rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model interacts with its N-terminal FERM domain to mask its integrin-binding site and interferes with interactions between the FERM domain and the cellular membrane. Talin is a large and ubiquitous cytoskeletal protein concentrated at focal adhesion sites. It is involved in linking integrins to the actin cytoskeleton.


Pssm-ID: 213393  Cd Length: 172  Bit Score: 266.04  E-value: 1.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327 1654 KAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQ 1733
Cdd:cd12150     1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGEAEQLGHAVTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327 1734 MAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKqAAHTQEALEEAVQMMTEAVEDLTTT 1813
Cdd:cd12150    81 MAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPK-AVHAHPAVDEAAQMLKEAIEDLTQT 159

                         170
                  ....*....|...
gi 227116327 1814 LNEAASAAGVVGG 1826
Cdd:cd12150   160 LEEAASEAGVVSG 172
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 2336-2532 1.22e-76

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 253.06  E-value: 1.22e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   2336 DESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALD-DGQWSQGLISAARMVAAATNNLCEAANAA 2414
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKkNSRWTEGLISAAKAVAAATNVLVEAADGV 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   2415 VQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAF-EDQENETVVVKEK 2493
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 227116327   2494 MVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKF 2532
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYEL 199
FERM_F1_TLN1 cd17173
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); ...
 86-197 4.49e-75

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain.


Pssm-ID: 340693  Cd Length: 112  Bit Score: 245.01  E-value: 4.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKL 165
Cdd:cd17173     1 RPLKIRMLDGTVKTVMVDDSKTVTDMLMTICARIGITNHDEYSLVREIMEEKKEEVTGTLKKDKTLLRDDKKMEKLKQKL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 227116327  166 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 197
Cdd:cd17173    81 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 112
Talin_middle pfam09141
Talin, middle domain; Members of this family adopt a structure consisting of five alpha ...
 491-652 9.85e-68

Talin, middle domain; Members of this family adopt a structure consisting of five alpha helices that fold into a bundle. They contain a Vinculin binding site (VBS) composed of a hydrophobic surface spanning five turns of helix four. Activation of the VBS causes subsequent recruitment of Vinculin, which enables maturation of small integrin/talin complexes into more stable adhesions. Formation of the complex between VBS and Vinculin requires prior unfolding of this middle domain: once released from the talin hydrophobic core, the VBS helix is then available to induce the 'bundle conversion' conformational change within the vinculin head domain thereby displacing the intramolecular interaction with the vinculin tail, allowing vinculin to bind actin.


Pssm-ID: 462691  Cd Length: 161  Bit Score: 226.01  E-value: 9.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   491 AQQALTGTINSSMQAVQAAQATLDDFETLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDY 570
Cdd:pfam09141    1 PQRALLGTISAGQEAIQAAEAELDTPAQLPPLGSDAASLQWRENTLDVSKQNVSSQLAAMNAATAQVVTLTSGPPDEIDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   571 TAVGCAVTTISSNLTEMSRGVKLLAALLEDEgGNGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGE 650
Cdd:pfam09141   81 TAVGAAITTISSNLPEMSKGVRMLAALMDDE-DSGDKLLDAARKLCGAFSDLLKAAQPESKEPRQNLLNAASRVGEASQQ 159


                   ..
gi 227116327   651 LL 652
Cdd:pfam09141  160 LL 161
VBS pfam08913
Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like ...
 1849-1973 2.34e-63

Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like molecules, enabling binding of vinculin to talin, stabilising integrin-mediated cell-matrix junctions. Talin, in turn, links integrins to the actin cytoskeleton. The consensus sequence for Vinculin binding sites is LxxAAxxVAxxVxxLIxxA, with a secondary structure prediction of four amphipathic helices. The hydrophobic residues that define the VBS are themselves 'masked' and are buried in the core of a series of helical bundles that make up the talin rod.


Pssm-ID: 430312  Cd Length: 125  Bit Score: 211.72  E-value: 2.34e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  1849 SFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASQAKPAAVAAENEEIGAHIKHRVQELGHGCS 1928
Cdd:pfam08913    1 TFVDYQTTMVRYAKAIAVTAQEMNTKSVTSPEELGQLASQMTSDYGQLAQQGIGASATAEPEEIGFQIRTRVQDLGHGCI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 227116327  1929 ALVTKAGALQCSPSDVYTKKELIECARRVSEKVSHVLAALQAGNR 1973
Cdd:pfam08913   81 VLVQKAGALQISPTDSYTKRELIECARAVSEKVSQVLAALQAGNR 125
FERM_F1_TLN2 cd17174
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-2 (TLN2); ...
 86-197 4.55e-63

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-2 (TLN2); TLN2 is a cytoskeletal protein that plays an important role in cell adhesion and recycling of synaptic vesicles. TLN2 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN2 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain.


Pssm-ID: 340694  Cd Length: 112  Bit Score: 210.66  E-value: 4.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKL 165
Cdd:cd17174     1 RPQKIRMLDGAVKTIMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 227116327  166 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 197
Cdd:cd17174    81 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 112
FERM_F1_TLN cd17090
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin and ...
 86-197 9.11e-63

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin and similar proteins; Talin is a cytoskeletal protein that activates integrins and couples them to cytoskeletal actin. Talin consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain that is joined to the F1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components; no binding partner has yet been found for it.


Pssm-ID: 340610  Cd Length: 111  Bit Score: 209.50  E-value: 9.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTgTLRKDKTLLRDEKKMEKLKQKL 165
Cdd:cd17090     1 RPLRVRTLDGSVKTVLVDDSQTVSQLVETICTKIGITNPEEFSLVREEEEEEKENKA-TLRKSTSRLRDDKKMESLKKKL 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 227116327  166 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 197
Cdd:cd17090    80 HTDDELNWLDHDQTLREQGVDEDETLLLRRKF 111
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 88-313 9.71e-59

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: 201.75  E-value: 9.71e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327     88 LKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEkkdegtgtlrkdktllrdekkmeklkqklht 167
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDE------------------------------- 50

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    168 dDELNWLDHGRTLREQGVE-EHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQ 246
Cdd:smart00295   51 -DLRHWLDPAKTLLDQDVKsEPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAE 129

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227116327    247 FGPHNEQKH-KAGFLDLKDFLPKEYVKQKG----ERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFF 313
Cdd:smart00295  130 FGDYDEELHdLRGELSLKRFLPKQLLDSRKlkewRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
 309-400 2.31e-57

FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . 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: 269973  Cd Length: 92  Bit Score: 193.33  E-value: 2.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  309 GVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQI 388
Cdd:cd10569     1 GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYYSVQTTEGEQI 80

                          90
                  ....*....|..
gi 227116327  389 AQLIAGYIDIIL 400
Cdd:cd10569    81 SQLISGYIDIIL 92
FERM_F0_TLN1 cd17171
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); ...
 2-85 3.80e-57

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain.


Pssm-ID: 340691  Cd Length: 84  Bit Score: 192.49  E-value: 3.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    2 VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:cd17171     1 VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERVPEAQAGQPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 80


                  ....
gi 227116327   82 RKKQ 85
Cdd:cd17171    81 RKKQ 84
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
 2385-2531 5.82e-55

I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.


Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 188.95  E-value: 5.82e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  2385 DDGQWSQGLISAARMVAAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVK 2464
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227116327  2465 RASDNLVKAAQKAAAFEDQENETVVVKEK--MVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYK 2531
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEEIEEEMDFSKlsLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
FERM_F0_TLN cd17089
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin and ...
 4-85 4.61e-43

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin and similar proteins; Talin is a cytoskeletal protein that activates integrins and couples them to cytoskeletal actin. Talin consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain that is joined to the F1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components; no binding partner has yet been found for it.


Pssm-ID: 340609  Cd Length: 84  Bit Score: 152.03  E-value: 4.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    4 LSLKISI--GNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:cd17089     1 LSLKIHIvkSGIVKTMQFDPSMTVYDACRLIREKIPEAAQGQASDYGLFLPDEDPKKGRWLEPDRTLEYYDLRNGDELEY 80


                  ....
gi 227116327   82 RKKQ 85
Cdd:cd17089    81 KKKH 84
FERM_F0_TLN2 cd17172
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-2 (TLN2); ...
 4-85 2.55e-37

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-2 (TLN2); TLN2 is a cytoskeletal protein that plays an important role in cell adhesion and recycling of synaptic vesicles. TLN2 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN2 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain.


Pssm-ID: 340692  Cd Length: 84  Bit Score: 135.91  E-value: 2.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    4 LSLKISIG--NVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:cd17172     1 LSLKICVRqcNVVKTMQFEPSTAVYDACRIIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDVLEY 80


                  ....
gi 227116327   82 RKKQ 85
Cdd:cd17172    81 KKKQ 84
FERM_f0 pfam16511
N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The ...
 4-83 3.39e-37

N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The fold is an ubiquitin-like fold joined to the f1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components, No binding partner has yet been found for it.


Pssm-ID: 465152  Cd Length: 81  Bit Score: 135.48  E-value: 3.39e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327     4 LSLKISI--GNVVKTMQFEPSTMVYDACRMIRERIPEAlAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEY 81
Cdd:pfam16511    1 LSLKISIvgSNVTKTMQFDPSTTVYDACRLIREKIPEG-GLNASEYGLFLADEDPKKGRWLEPGRTLEYYDLRNGDELEY 79


                   ..
gi 227116327    82 RK 83
Cdd:pfam16511   80 KK 81
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 201-313 6.81e-37

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 135.86  E-value: 6.81e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   201 DQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKG----E 276
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKskelE 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 227116327   277 RKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFF 313
Cdd:pfam00373   81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 211-305 1.11e-27

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: 108.87  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  211 QLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKG----ERKIFQAHKNC 286
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKpeewEKRIVELHKKL 80

                          90
                  ....*....|....*....
gi 227116327  287 GQMSEIEAKVRYVKLARSL 305
Cdd:cd14473    81 RGLSPAEAKLKYLKIARKL 99
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 309-400 2.53e-14

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: 70.48  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  309 GVSFFLVKEKMKGKNklvPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASP-KSFTLDFGD-YQDGYYSVQT--TE 384
Cdd:cd00836     1 GVEFFPVKDKSKKGS---PIILGVNPEGISVYDELTGQPLVLFPWPNIKKISFSGaKKFTIVVADeDKQSKLLFQTpsRQ 77

                          90
                  ....*....|....*.
gi 227116327  385 GEQIAQLIAGYIDIIL 400
Cdd:cd00836    78 AKEIWKLIVGYHRFLL 93
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 86-197 3.46e-12

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 64.15  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRElmeekkdegtgtlrkdktllrdekkmeklkqkl 165
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYE--------------------------------- 47

                          90       100       110
                  ....*....|....*....|....*....|...
gi 227116327  166 HTDDELNWLDHGRTLREQGVE-EHETLLLRRKF 197
Cdd:cd01765    48 DNDGQKHWLDLDKKISKQLKRsGPYQFYFRVKF 80
FERM_F1_kindlins cd17096
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the kindlin ...
 86-198 3.59e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the kindlin family; The kindlin family is composed of Kindlin-1, 2 and 3, which are FERM domain-containing adaptor molecules that interact with the cytoplasmic component of integrins and regulate cell-matrix connections. Kindlins belong to the 4.1- ezrin-ridixin-moesin (FERM) domain containing protein family. They contain F1, F2 and F3 subdomains that typify FERM family members, and these subdomains are preceded by an N-terminal F0 subdomain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain. In addition, a distinctive feature of kindlins is the insertion of a pleckstrin homology (PH) subdomain into the F2 subdomain.


Pssm-ID: 340616  Cd Length: 90  Bit Score: 58.83  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELmeekkdegtgtLRKDKTLLRdekkmeklKQKL 165
Cdd:cd17096     1 KTLRIQLPDLQYLDLRVDFSVKVFNAVVDLCKELGIRHPEELSLLRPP-----------LYRPKSLVD--------KARL 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 227116327  166 HTddelNWLDHGRTLREQGVEEHETLLLRRKFF 198
Cdd:cd17096    62 NS----GWLDSSRSLMEQGVRENDTLLLRFKYY 90
FERM_F1_KIND2 cd17184
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-2 (KIND2) ...
 106-198 3.19e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-2 (KIND2); KIND2, also termed fermitin family homolog 2 (FERMT2), or mitogen-inducible gene 2 protein (MIG-2), or Pleckstrin homology (PH) domain-containing family C member 1, is an adaptor protein that is widely distributed and is particularly abundant in adherent cells. It binds to the integrin beta cytoplasmic tail to promote integrin activation. It promotes carcinogenesis through regulation of cell-cell and cell-extracellular matrix adhesion. KIND2 also plays an important role in cardiac development. KIND2 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain.


Pssm-ID: 340704  Cd Length: 101  Bit Score: 50.79  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327  106 KTVTDmlmtICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLrDEKKMEKlkqklhtddelNWLDHGRTLREQGV 185
Cdd:cd17184    25 KAVSD----ICKTFNIRHPEELSLLRKPRDPTKKKKLAKMYKPQSLL-DKAKINQ-----------GWLDSSRSLMEQDV 88

                          90
                  ....*....|...
gi 227116327  186 EEHETLLLRRKFF 198
Cdd:cd17184    89 KENEALLLRFKYY 101
FERM_F1_KIND1 cd17183
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-1 (KIND1) ...
 86-198 6.00e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-1 (KIND1); KIND1, also termed Kindlerin, or Kindler syndrome protein, or fermitin family homolog 1 (FERMT1), or Unc-112-related protein 1 (URP1), is an integrin-interacting protein that has been implicated in cell adhesion, proliferation, polarity, and motility. It is essential for maintaining the structure of cell-matrix adhesion, such as focal adhesions and podosomes. KIND1 is expressed primarily in epithelial cells. Loss or mutations of KIND1 gene may cause the Kindler syndrome (KS), an autosomal recessive skin disorder with an intriguing progressive phenotype comprising skin blistering, photosensitivity, progressive poikiloderma with extensive skin atrophy, and propensity to skin cancer. KIND1 forms a molecular complex with the key transforming growth factor (TGF)-beta/Smad3 signaling components including type I TGFbeta receptor (TbetaRI), Smad3 and Smad anchor for receptor activation (SARA) to control the activation of TGF-beta/Smad3 signaling pathway. KIND1 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain.


Pssm-ID: 340703  Cd Length: 93  Bit Score: 44.06  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEkkdegtgtLRKDKTLLRdekkmeklKQKL 165
Cdd:cd17183     1 KLLRLQLPNMKTVRLKVSFSAVVFKAVSDICKTLNIRRSEELSLLKPSLAK--------MYQPRTLLD--------KAKL 64

                          90       100       110
                  ....*....|....*....|....*....|...
gi 227116327  166 HTddelNWLDHGRTLREQGVEEHETLLLRRKFF 198
Cdd:cd17183    65 NA----GWLDSSRSLMEQGIQEDDQLLLRFKYY 93
FERM_F1_KIND3 cd17185
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-3 (KIND3) ...
 86-198 4.57e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-3 (KIND3); KIND3, also termed fermitin family homolog 3 (FERMT3), or MIG2-like protein, or Unc-112-related protein 2, is an adaptor protein that expressed primarily in hematopoietic cells. It plays a central role in cell adhesion in hematopoietic cells, and also promotes integrin activation, clustering and outside-in signaling. KIND3, together with talin-1, contributes essentially to the activation of beta2-integrins in neutrophils. In addition, KIND3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells. Mutations in the KIND3 gene cause leukocyte adhesion deficiency type III (LAD III), which is characterized by high susceptibility to infections, spontaneous and episodic bleedings, and osteopetrosis. KIND3 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain.


Pssm-ID: 340705  Cd Length: 91  Bit Score: 41.39  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327   86 RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTgtlrkDKTLLrdekkmeklkqkl 165
Cdd:cd17185     1 KPVILSLPNRRSLRIRACFSSPVFRAVAGICRVLSIRHPEELSLLRAPKLYRPSSVT-----DKTQI------------- 62

                          90       100       110
                  ....*....|....*....|....*....|...
gi 227116327  166 HTddelNWLDHGRTLREQGVEEHETLLLRRKFF 198
Cdd:cd17185    63 HS----RWLDSSRSLMQQGVQEGDRLWLRFKYY 91
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 607-759 1.23e-03

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 42.35  E-value: 1.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116327    607 PLLQAAKGLAGAVSELLRSAQPAsaeprQNLLQAAGNVGQASGELLqqigesDTDPHFQDVLMQLAKAVASAAAALVLKA 686
Cdd:smart00307    9 SILEAAKAITKAIAALVKAATNA-----QREIVAQGRGGASPGEFY------KKNSRWTEGLISAAKAVAAATNVLVEAA 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227116327    687 KSVAQRTEDsglQTQVIAAATQCALSTSQLVACTKVVApTISSPVcQEQLVEAGRLVAKAVEGCVSASQAATE 759
Cdd:smart00307   78 DGVVTGKGS---EEELIVAAKEVAASTAQLVAASRVKA-DKDSQA-QDRLQAASKAVTNATANLVAAVKSGMI 145
FERM_C_fermitin cd13205
FERM domain C-lobe of the Fermitin family; Fermitin functions as a mediator of integrin ...
 308-359 2.39e-03

FERM domain C-lobe of the Fermitin family; Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. 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). This cd is not included in the C-lobe hierarchy based on its position in the tree. One thing to note is that unlike the other members of the C-lobe hierarchy it contains 2 FERM M domains which might also reflect a difference in its evolutionary history. 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: 270026  Cd Length: 91  Bit Score: 39.25  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 227116327  308 YGVSFFLVKEKMKGKNKLvprlLGITKECVMRVDEKTKEVIQEWSLTNIKRW 359
Cdd:cd13205     2 FGITYFIVRFRGSKKEEL----LGVAYNRLIRMDLHTGDPIKTWRYSTMKAW 49
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
 86-129 4.70e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each 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: 340728  Cd Length: 98  Bit Score: 38.77  E-value: 4.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 227116327   86 RPL--KIRMLDGTVKTIMVDDSKTVTDMLMTICARIGIT-NHDEYSL 129
Cdd:cd17208     2 RPIvaRFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRsTADGFAL 48
 
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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