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Conserved domains on  [gi|1720432655|ref|XP_030100443|]
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talin-2 isoform X1 [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 ...
1658-1829 6.02e-78

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: 255.64  E-value: 6.02e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1658 KAPGQRECDYSIDGINRCIRDIEQASLAAVSQSLATRDDISVEALQEQLTSVVQEIGHLIDPIATAARGEAAQLGHKVTQ 1737
Cdd:cd12150      1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGEAEQLGHAVTQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1738 LASYFEPLILAAVGVASKMLDHQQQMTVLDQTKTLAESALQMLYAAKEGGGNPKAQHTHDAITEAAQLMKEAVDDIMVTL 1817
Cdd:cd12150     81 MAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPKAVHAHPAVDEAAQMLKEAIEDLTQTL 160
                          170
                   ....*....|..
gi 1720432655 1818 NEAASEVGLVGG 1829
Cdd:cd12150    161 EEAASEAGVVSG 172
FERM_F1_TLN2 cd17174
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-2 (TLN2); ...
90-201 6.05e-74

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: 241.48  E-value: 6.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 169
Cdd:cd17174      1 RPQKIRMLDGAVKTIMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720432655  170 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 201
Cdd:cd17174     81 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 112
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
2339-2549 2.15e-70

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


:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 234.95  E-value: 2.15e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  2339 DETLDFEEQILEAAKSIAAATSALVKSASAAQRELVAQGKVGSIPANA-ADDGQWSQGLISAARMVAAATSSLCEAANAS 2417
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFyKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  2418 VQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQvmvtdaggkilllerAAGNAVKRASDNLVRAAQKAAF 2497
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQ---------------AASKAVTNATANLVAAVKSGMI 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720432655  2498 GKADDDD--VVVKTKFVGGIAQIIAAQEEMLKKERELEEARKKLAQIRQQQYKF 2549
Cdd:smart00307  146 FDEEQEEeeDFSKLSLHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYEL 199
Talin_middle pfam09141
Talin, middle domain; Members of this family adopt a structure consisting of five alpha ...
496-657 1.82e-69

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: 230.63  E-value: 1.82e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  496 AQQALMGTINTSMHAVQQAQDDLSELDSLPPLGQDMASRVWVQNKVDESKHEIHSQVDAITAGTASVVNLTAGDPADTDY 575
Cdd:pfam09141    1 PQRALLGTISAGQEAIQAAEAELDTPAQLPPLGSDAASLQWRENTLDVSKQNVSSQLAAMNAATAQVVTLTSGPPDEIDY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  576 TAVGCAITTISSNLTEMSKGVKLLAALMDDDvGSGEDLLRAARTLAGAVSDLLKAVQPTSGEPRQTVLTAAGSIGQASGD 655
Cdd:pfam09141   81 TAVGAAITTISSNLPEMSKGVRMLAALMDDE-DSGDKLLDAARKLCGAFSDLLKAAQPESKEPRQNLLNAASRVGEASQQ 159

                   ..
gi 1720432655  656 LL 657
Cdd:pfam09141  160 LL 161
VBS pfam08913
Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like ...
1852-1976 8.70e-66

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: 218.66  E-value: 8.70e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1852 TFVDYQTTVVKYSKAIAVTAQEMMTKSVTNPEELGGLASQMTTDYGHLALQGQMAAATAEPEEIGFQIRTRVQDLGHGCI 1931
Cdd:pfam08913    1 TFVDYQTTMVRYAKAIAVTAQEMNTKSVTSPEELGQLASQMTSDYGQLAQQGIGASATAEPEEIGFQIRTRVQDLGHGCI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720432655 1932 FLVQKAGALQVCPTDSYTKRELIECARSVTEKVSLVLSALQAGNK 1976
Cdd:pfam08913   81 VLVQKAGALQISPTDSYTKRELIECARAVSEKVSQVLAALQAGNR 125
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
314-405 7.92e-60

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: 200.26  E-value: 7.92e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  314 GVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQI 393
Cdd:cd10569      1 GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYYSVQTTEGEQI 80
                           90
                   ....*....|..
gi 1720432655  394 SQLIAGYIDIIL 405
Cdd:cd10569     81 SQLISGYIDIIL 92
FERM_F0_TLN2 cd17172
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-2 (TLN2); ...
6-89 6.20e-52

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: 177.51  E-value: 6.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    6 LSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEY 85
Cdd:cd17172      1 LSLKICVRQCNVVKTMQFEPSTAVYDACRIIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDVLEY 80

                   ....
gi 1720432655   86 KKKQ 89
Cdd:cd17172     81 KKKQ 84
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
205-318 4.73e-39

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


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 142.02  E-value: 4.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  205 DQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGA---E 281
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKSkelE 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720432655  282 KRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFF 318
Cdd:pfam00373   81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
talin-RS super family cl17094
rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model ...
1047-1176 3.97e-06

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.


The actual alignment was detected with superfamily member cd12150:

Pssm-ID: 213393  Cd Length: 172  Bit Score: 49.56  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1047 EACGPMEIDSALNTVQTLKNELQDAKMAAAESQLKPLPGETLEKCAQDLGSTSKGVGSSMAQlLTCAAQGNEHYTGVAAR 1126
Cdd:cd12150      1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEP-LRSAAKGEAEQLGHAVT 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1127 ETAQALKTLAQAARGVAASTNDPEAAHAMLDSARDVMEGSAMLIQEAKQA 1176
Cdd:cd12150     80 QMAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEA 129
I_LWEQ super family cl47685
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
691-767 9.03e-03

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.


The actual alignment was detected with superfamily member pfam01608:

Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 39.10  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  691 AKNVA------QVAEDTVLQN-----RVIAAATQCALSTSQLVACAKVVSPTISSpvCQEQLIEAGKLVDRSVENCVRAC 759
Cdd:pfam01608   13 AKAVAaatnllVEAADGVVQGqgseeELIVAAKEVAASTAQLVAASRVKADPNSK--TQQRLEAASKAVTDATKNLVAAV 90

                   ....*...
gi 1720432655  760 QAATSDSE 767
Cdd:pfam01608   91 KSAAELQE 98
 
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 ...
1658-1829 6.02e-78

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: 255.64  E-value: 6.02e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1658 KAPGQRECDYSIDGINRCIRDIEQASLAAVSQSLATRDDISVEALQEQLTSVVQEIGHLIDPIATAARGEAAQLGHKVTQ 1737
Cdd:cd12150      1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGEAEQLGHAVTQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1738 LASYFEPLILAAVGVASKMLDHQQQMTVLDQTKTLAESALQMLYAAKEGGGNPKAQHTHDAITEAAQLMKEAVDDIMVTL 1817
Cdd:cd12150     81 MAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPKAVHAHPAVDEAAQMLKEAIEDLTQTL 160
                          170
                   ....*....|..
gi 1720432655 1818 NEAASEVGLVGG 1829
Cdd:cd12150    161 EEAASEAGVVSG 172
FERM_F1_TLN2 cd17174
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-2 (TLN2); ...
90-201 6.05e-74

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: 241.48  E-value: 6.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 169
Cdd:cd17174      1 RPQKIRMLDGAVKTIMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720432655  170 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 201
Cdd:cd17174     81 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 112
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
2339-2549 2.15e-70

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


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 234.95  E-value: 2.15e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  2339 DETLDFEEQILEAAKSIAAATSALVKSASAAQRELVAQGKVGSIPANA-ADDGQWSQGLISAARMVAAATSSLCEAANAS 2417
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFyKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  2418 VQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQvmvtdaggkilllerAAGNAVKRASDNLVRAAQKAAF 2497
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQ---------------AASKAVTNATANLVAAVKSGMI 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720432655  2498 GKADDDD--VVVKTKFVGGIAQIIAAQEEMLKKERELEEARKKLAQIRQQQYKF 2549
Cdd:smart00307  146 FDEEQEEeeDFSKLSLHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYEL 199
Talin_middle pfam09141
Talin, middle domain; Members of this family adopt a structure consisting of five alpha ...
496-657 1.82e-69

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: 230.63  E-value: 1.82e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  496 AQQALMGTINTSMHAVQQAQDDLSELDSLPPLGQDMASRVWVQNKVDESKHEIHSQVDAITAGTASVVNLTAGDPADTDY 575
Cdd:pfam09141    1 PQRALLGTISAGQEAIQAAEAELDTPAQLPPLGSDAASLQWRENTLDVSKQNVSSQLAAMNAATAQVVTLTSGPPDEIDY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  576 TAVGCAITTISSNLTEMSKGVKLLAALMDDDvGSGEDLLRAARTLAGAVSDLLKAVQPTSGEPRQTVLTAAGSIGQASGD 655
Cdd:pfam09141   81 TAVGAAITTISSNLPEMSKGVRMLAALMDDE-DSGDKLLDAARKLCGAFSDLLKAAQPESKEPRQNLLNAASRVGEASQQ 159

                   ..
gi 1720432655  656 LL 657
Cdd:pfam09141  160 LL 161
VBS pfam08913
Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like ...
1852-1976 8.70e-66

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: 218.66  E-value: 8.70e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1852 TFVDYQTTVVKYSKAIAVTAQEMMTKSVTNPEELGGLASQMTTDYGHLALQGQMAAATAEPEEIGFQIRTRVQDLGHGCI 1931
Cdd:pfam08913    1 TFVDYQTTMVRYAKAIAVTAQEMNTKSVTSPEELGQLASQMTSDYGQLAQQGIGASATAEPEEIGFQIRTRVQDLGHGCI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720432655 1932 FLVQKAGALQVCPTDSYTKRELIECARSVTEKVSLVLSALQAGNK 1976
Cdd:pfam08913   81 VLVQKAGALQISPTDSYTKRELIECARAVSEKVSQVLAALQAGNR 125
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
314-405 7.92e-60

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: 200.26  E-value: 7.92e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  314 GVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQI 393
Cdd:cd10569      1 GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYYSVQTTEGEQI 80
                           90
                   ....*....|..
gi 1720432655  394 SQLIAGYIDIIL 405
Cdd:cd10569     81 SQLISGYIDIIL 92
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
92-318 1.95e-55

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: 192.12  E-value: 1.95e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    92 QKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSliqetieekkeegtgtlkkdrtlLRDERKMEKLKaklht 171
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFG-----------------------LQFEDPDEDLR----- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   172 dddlNWLDHSRTFREQGVD-ENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQ 250
Cdd:smart00295   54 ----HWLDPAKTLLDQDVKsEPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAE 129
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720432655   251 FGPHVEHKH-KPGFLDLKEFLPKEYIKQRGA---EKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFF 318
Cdd:smart00295  130 FGDYDEELHdLRGELSLKRFLPKQLLDSRKLkewRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F0_TLN2 cd17172
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-2 (TLN2); ...
6-89 6.20e-52

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: 177.51  E-value: 6.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    6 LSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEY 85
Cdd:cd17172      1 LSLKICVRQCNVVKTMQFEPSTAVYDACRIIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDVLEY 80

                   ....
gi 1720432655   86 KKKQ 89
Cdd:cd17172     81 KKKQ 84
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
2388-2548 4.05e-49

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: 172.00  E-value: 4.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 2388 DDGQWSQGLISAARMVAAATSSLCEAANASVQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQvmvtdag 2467
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLE------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 2468 gkilllerAAGNAVKRASDNLVRAAQKAAFGKADDDDVVV---KTKFVGGIAQIIAAQEEMLKKERELEEARKKLAQIRQ 2544
Cdd:pfam01608   74 --------AASKAVTDATKNLVAAVKSAAELQEEEIEEEMdfsKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRK 145

                   ....
gi 1720432655 2545 QQYK 2548
Cdd:pfam01608  146 AHYH 149
FERM_f0 pfam16511
N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The ...
6-87 6.22e-41

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: 145.88  E-value: 6.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    6 LSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQtGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEY 85
Cdd:pfam16511    1 LSLKISIVGSNVTKTMQFDPSTTVYDACRLIREKIPEGG-LNASEYGLFLADEDPKKGRWLEPGRTLEYYDLRNGDELEY 79

                   ..
gi 1720432655   86 KK 87
Cdd:pfam16511   80 KK 81
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
205-318 4.73e-39

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 142.02  E-value: 4.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  205 DQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGA---E 281
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKSkelE 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720432655  282 KRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFF 318
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 ...
215-310 4.89e-28

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: 110.03  E-value: 4.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  215 QLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGA---EKRIFQEHKNC 291
Cdd:cd14473      1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKPeewEKRIVELHKKL 80
                           90
                   ....*....|....*....
gi 1720432655  292 GEMSEIEAKVKYVKLARSL 310
Cdd:cd14473     81 RGLSPAEAKLKYLKIARKL 99
talin-RS cd12150
rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model ...
1047-1176 3.97e-06

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: 49.56  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1047 EACGPMEIDSALNTVQTLKNELQDAKMAAAESQLKPLPGETLEKCAQDLGSTSKGVGSSMAQlLTCAAQGNEHYTGVAAR 1126
Cdd:cd12150      1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEP-LRSAAKGEAEQLGHAVT 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1127 ETAQALKTLAQAARGVAASTNDPEAAHAMLDSARDVMEGSAMLIQEAKQA 1176
Cdd:cd12150     80 QMAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEA 129
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
94-189 1.19e-04

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 42.19  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   94 IRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLiqETIEEKKEEgtgtlkkdrtllrderkmeklkaklhtdd 173
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGL--QFLDDNGEH----------------------------- 49
                           90
                   ....*....|....*.
gi 1720432655  174 dlNWLDHSRTFREQGV 189
Cdd:pfam09379   50 --RWLDLSKRLSKQAP 63
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
691-767 9.03e-03

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: 39.10  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  691 AKNVA------QVAEDTVLQN-----RVIAAATQCALSTSQLVACAKVVSPTISSpvCQEQLIEAGKLVDRSVENCVRAC 759
Cdd:pfam01608   13 AKAVAaatnllVEAADGVVQGqgseeELIVAAKEVAASTAQLVAASRVKADPNSK--TQQRLEAASKAVTDATKNLVAAV 90

                   ....*...
gi 1720432655  760 QAATSDSE 767
Cdd:pfam01608   91 KSAAELQE 98
 
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 ...
1658-1829 6.02e-78

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: 255.64  E-value: 6.02e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1658 KAPGQRECDYSIDGINRCIRDIEQASLAAVSQSLATRDDISVEALQEQLTSVVQEIGHLIDPIATAARGEAAQLGHKVTQ 1737
Cdd:cd12150      1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGEAEQLGHAVTQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1738 LASYFEPLILAAVGVASKMLDHQQQMTVLDQTKTLAESALQMLYAAKEGGGNPKAQHTHDAITEAAQLMKEAVDDIMVTL 1817
Cdd:cd12150     81 MAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPKAVHAHPAVDEAAQMLKEAIEDLTQTL 160
                          170
                   ....*....|..
gi 1720432655 1818 NEAASEVGLVGG 1829
Cdd:cd12150    161 EEAASEAGVVSG 172
FERM_F1_TLN2 cd17174
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-2 (TLN2); ...
90-201 6.05e-74

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: 241.48  E-value: 6.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 169
Cdd:cd17174      1 RPQKIRMLDGAVKTIMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720432655  170 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 201
Cdd:cd17174     81 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 112
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
2339-2549 2.15e-70

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


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 234.95  E-value: 2.15e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  2339 DETLDFEEQILEAAKSIAAATSALVKSASAAQRELVAQGKVGSIPANA-ADDGQWSQGLISAARMVAAATSSLCEAANAS 2417
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFyKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  2418 VQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQvmvtdaggkilllerAAGNAVKRASDNLVRAAQKAAF 2497
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQ---------------AASKAVTNATANLVAAVKSGMI 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720432655  2498 GKADDDD--VVVKTKFVGGIAQIIAAQEEMLKKERELEEARKKLAQIRQQQYKF 2549
Cdd:smart00307  146 FDEEQEEeeDFSKLSLHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYEL 199
Talin_middle pfam09141
Talin, middle domain; Members of this family adopt a structure consisting of five alpha ...
496-657 1.82e-69

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: 230.63  E-value: 1.82e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  496 AQQALMGTINTSMHAVQQAQDDLSELDSLPPLGQDMASRVWVQNKVDESKHEIHSQVDAITAGTASVVNLTAGDPADTDY 575
Cdd:pfam09141    1 PQRALLGTISAGQEAIQAAEAELDTPAQLPPLGSDAASLQWRENTLDVSKQNVSSQLAAMNAATAQVVTLTSGPPDEIDY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  576 TAVGCAITTISSNLTEMSKGVKLLAALMDDDvGSGEDLLRAARTLAGAVSDLLKAVQPTSGEPRQTVLTAAGSIGQASGD 655
Cdd:pfam09141   81 TAVGAAITTISSNLPEMSKGVRMLAALMDDE-DSGDKLLDAARKLCGAFSDLLKAAQPESKEPRQNLLNAASRVGEASQQ 159

                   ..
gi 1720432655  656 LL 657
Cdd:pfam09141  160 LL 161
VBS pfam08913
Vinculin Binding Site; Vinculin binding sites are predominantly found in talin and talin-like ...
1852-1976 8.70e-66

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: 218.66  E-value: 8.70e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1852 TFVDYQTTVVKYSKAIAVTAQEMMTKSVTNPEELGGLASQMTTDYGHLALQGQMAAATAEPEEIGFQIRTRVQDLGHGCI 1931
Cdd:pfam08913    1 TFVDYQTTMVRYAKAIAVTAQEMNTKSVTSPEELGQLASQMTSDYGQLAQQGIGASATAEPEEIGFQIRTRVQDLGHGCI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720432655 1932 FLVQKAGALQVCPTDSYTKRELIECARSVTEKVSLVLSALQAGNK 1976
Cdd:pfam08913   81 VLVQKAGALQISPTDSYTKRELIECARAVSEKVSQVLAALQAGNR 125
FERM_F1_TLN1 cd17173
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1); ...
90-201 2.52e-63

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: 211.11  E-value: 2.52e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKL 169
Cdd:cd17173      1 RPLKIRMLDGTVKTVMVDDSKTVTDMLMTICARIGITNHDEYSLVREIMEEKKEEVTGTLKKDKTLLRDDKKMEKLKQKL 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720432655  170 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 201
Cdd:cd17173     81 HTDDELNWLDHGRTLREQGVEEHETLLLRRKF 112
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
314-405 7.92e-60

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: 200.26  E-value: 7.92e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  314 GVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQI 393
Cdd:cd10569      1 GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYYSVQTTEGEQI 80
                           90
                   ....*....|..
gi 1720432655  394 SQLIAGYIDIIL 405
Cdd:cd10569     81 SQLISGYIDIIL 92
FERM_F1_TLN cd17090
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin and ...
90-201 1.63e-59

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: 200.26  E-value: 1.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTgTLKKDRTLLRDERKMEKLKAKL 169
Cdd:cd17090      1 RPLRVRTLDGSVKTVLVDDSQTVSQLVETICTKIGITNPEEFSLVREEEEEEKENKA-TLRKSTSRLRDDKKMESLKKKL 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720432655  170 HTDDDLNWLDHSRTFREQGVDENETLLLRRKF 201
Cdd:cd17090     80 HTDDELNWLDHDQTLREQGVDEDETLLLRRKF 111
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
92-318 1.95e-55

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: 192.12  E-value: 1.95e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    92 QKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSliqetieekkeegtgtlkkdrtlLRDERKMEKLKaklht 171
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFG-----------------------LQFEDPDEDLR----- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   172 dddlNWLDHSRTFREQGVD-ENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQ 250
Cdd:smart00295   54 ----HWLDPAKTLLDQDVKsEPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAE 129
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720432655   251 FGPHVEHKH-KPGFLDLKEFLPKEYIKQRGA---EKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFF 318
Cdd:smart00295  130 FGDYDEELHdLRGELSLKRFLPKQLLDSRKLkewRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F0_TLN2 cd17172
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-2 (TLN2); ...
6-89 6.20e-52

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: 177.51  E-value: 6.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    6 LSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEY 85
Cdd:cd17172      1 LSLKICVRQCNVVKTMQFEPSTAVYDACRIIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDVLEY 80

                   ....
gi 1720432655   86 KKKQ 89
Cdd:cd17172     81 KKKQ 84
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
2388-2548 4.05e-49

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: 172.00  E-value: 4.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 2388 DDGQWSQGLISAARMVAAATSSLCEAANASVQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQvmvtdag 2467
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLE------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 2468 gkilllerAAGNAVKRASDNLVRAAQKAAFGKADDDDVVV---KTKFVGGIAQIIAAQEEMLKKERELEEARKKLAQIRQ 2544
Cdd:pfam01608   74 --------AASKAVTDATKNLVAAVKSAAELQEEEIEEEMdfsKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRK 145

                   ....
gi 1720432655 2545 QQYK 2548
Cdd:pfam01608  146 AHYH 149
FERM_F0_TLN1 cd17171
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1); ...
4-89 5.92e-49

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: 168.99  E-value: 5.92e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    4 VALSLKICVRhcNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDIL 83
Cdd:cd17171      1 VALSLKISIG--NVVKTMQFEPSTMVYDACRMIRERVPEAQAGQPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTM 78

                   ....*.
gi 1720432655   84 EYKKKQ 89
Cdd:cd17171     79 EYRKKQ 84
FERM_F0_TLN cd17089
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin and ...
6-89 1.79e-46

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: 162.04  E-value: 1.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    6 LSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEY 85
Cdd:cd17089      1 LSLKIHIVKSGIVKTMQFDPSMTVYDACRLIREKIPEAAQGQASDYGLFLPDEDPKKGRWLEPDRTLEYYDLRNGDELEY 80

                   ....
gi 1720432655   86 KKKQ 89
Cdd:cd17089     81 KKKH 84
FERM_f0 pfam16511
N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The ...
6-87 6.22e-41

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: 145.88  E-value: 6.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655    6 LSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQtGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEY 85
Cdd:pfam16511    1 LSLKISIVGSNVTKTMQFDPSTTVYDACRLIREKIPEGG-LNASEYGLFLADEDPKKGRWLEPGRTLEYYDLRNGDELEY 79

                   ..
gi 1720432655   86 KK 87
Cdd:pfam16511   80 KK 81
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
205-318 4.73e-39

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 142.02  E-value: 4.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  205 DQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGA---E 281
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKSkelE 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720432655  282 KRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFF 318
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 ...
215-310 4.89e-28

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: 110.03  E-value: 4.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  215 QLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGA---EKRIFQEHKNC 291
Cdd:cd14473      1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKPeewEKRIVELHKKL 80
                           90
                   ....*....|....*....
gi 1720432655  292 GEMSEIEAKVKYVKLARSL 310
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 ...
314-405 4.87e-13

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: 67.01  E-value: 4.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  314 GVSFFLVKEKMKGKNklvPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASP-KSFTLDF-GEYQESYYSVQT--TE 389
Cdd:cd00836      1 GVEFFPVKDKSKKGS---PIILGVNPEGISVYDELTGQPLVLFPWPNIKKISFSGaKKFTIVVaDEDKQSKLLFQTpsRQ 77
                           90
                   ....*....|....*.
gi 1720432655  390 GEQISQLIAGYIDIIL 405
Cdd:cd00836     78 AKEIWKLIVGYHRFLL 93
FERM_F1_kindlins cd17096
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the kindlin ...
90-202 3.22e-09

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: 56.13  E-value: 3.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETieekkeegtgtLKKDRTLLRderkmeklKAKL 169
Cdd:cd17096      1 KTLRIQLPDLQYLDLRVDFSVKVFNAVVDLCKELGIRHPEELSLLRPP-----------LYRPKSLVD--------KARL 61
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720432655  170 HTdddlNWLDHSRTFREQGVDENETLLLRRKFF 202
Cdd:cd17096     62 NS----GWLDSSRSLMEQGVRENDTLLLRFKYY 90
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
93-201 3.67e-09

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: 55.29  E-value: 3.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   93 KIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQEtieekkeegtgtlkkdrtllrderkmeklkaklHTD 172
Cdd:cd01765      4 RVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYE---------------------------------DND 50
                           90       100       110
                   ....*....|....*....|....*....|
gi 1720432655  173 DDLNWLDHSRTFREQGV-DENETLLLRRKF 201
Cdd:cd01765     51 GQKHWLDLDKKISKQLKrSGPYQFYFRVKF 80
FERM_F1_KIND2 cd17184
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-2 (KIND2) ...
104-202 2.92e-08

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: 53.48  E-value: 2.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  104 VMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLrDERKMEKlkaklhtdddlNWLDHSRT 183
Cdd:cd17184     15 VKVNFSDRVFKAVSDICKTFNIRHPEELSLLRKPRDPTKKKKLAKMYKPQSLL-DKAKINQ-----------GWLDSSRS 82
                           90
                   ....*....|....*....
gi 1720432655  184 FREQGVDENETLLLRRKFF 202
Cdd:cd17184     83 LMEQDVKENEALLLRFKYY 101
FERM_F1_KIND1 cd17183
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-1 (KIND1) ...
100-202 6.92e-07

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: 49.45  E-value: 6.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  100 SVKTVM--VDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEkkeegtgtLKKDRTLLRderkmeklKAKLHTdddlNW 177
Cdd:cd17183      9 NMKTVRlkVSFSAVVFKAVSDICKTLNIRRSEELSLLKPSLAK--------MYQPRTLLD--------KAKLNA----GW 68
                           90       100
                   ....*....|....*....|....*
gi 1720432655  178 LDHSRTFREQGVDENETLLLRRKFF 202
Cdd:cd17183     69 LDSSRSLMEQGIQEDDQLLLRFKYY 93
talin-RS cd12150
rod-segment of the talin C-terminal domain; The talin rod-segment characterize by this model ...
1047-1176 3.97e-06

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: 49.56  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1047 EACGPMEIDSALNTVQTLKNELQDAKMAAAESQLKPLPGETLEKCAQDLGSTSKGVGSSMAQlLTCAAQGNEHYTGVAAR 1126
Cdd:cd12150      1 KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEP-LRSAAKGEAEQLGHAVT 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720432655 1127 ETAQALKTLAQAARGVAASTNDPEAAHAMLDSARDVMEGSAMLIQEAKQA 1176
Cdd:cd12150     80 QMAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEA 129
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
94-189 1.19e-04

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 42.19  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   94 IRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLiqETIEEKKEEgtgtlkkdrtllrderkmeklkaklhtdd 173
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGL--QFLDDNGEH----------------------------- 49
                           90
                   ....*....|....*.
gi 1720432655  174 dlNWLDHSRTFREQGV 189
Cdd:pfam09379   50 --RWLDLSKRLSKQAP 63
FERM_C_fermitin cd13205
FERM domain C-lobe of the Fermitin family; Fermitin functions as a mediator of integrin ...
313-401 3.22e-04

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: 41.94  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  313 YGVSFFLVKEKMKGKNKLvprlLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAAS--PKSFTLDFGEYQESyYSVQTTEG 390
Cdd:cd13205      2 FGITYFIVRFRGSKKEEL----LGVAYNRLIRMDLHTGDPIKTWRYSTMKAWNVNweIREVIIQFEDENIA-FACLSADC 76
                           90
                   ....*....|.
gi 1720432655  391 EQISQLIAGYI 401
Cdd:cd13205     77 KIVHEFIGGYI 87
FERM_F1_KIND3 cd17185
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-3 (KIND3) ...
90-202 1.03e-03

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: 40.23  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655   90 RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIqetieekkeegtgtlkKDRTLLRDERKMEKlkAKL 169
Cdd:cd17185      1 KPVILSLPNRRSLRIRACFSSPVFRAVAGICRVLSIRHPEELSLL----------------RAPKLYRPSSVTDK--TQI 62
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720432655  170 HTdddlNWLDHSRTFREQGVDENETLLLRRKFF 202
Cdd:cd17185     63 HS----RWLDSSRSLMQQGVQEGDRLWLRFKYY 91
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
93-135 1.17e-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: 40.31  E-value: 1.17e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720432655   93 KIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEE-YSLIQ 135
Cdd:cd17208      7 RFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRSTADgFALYE 50
PTB_DOK4_DOK5_DOK6 cd13164
Downstream of tyrosine kinase 4, 5, and 6 proteins phosphotyrosine-binding domain (PTBi); The ...
334-395 3.54e-03

Downstream of tyrosine kinase 4, 5, and 6 proteins phosphotyrosine-binding domain (PTBi); The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain binds to acidic phospholids and localizes proteins to the plasma membrane, while the PTB domain mediates protein-protein interactions by binding to phosphotyrosine-containing motifs. The C-terminal part of Dok contains multiple tyrosine phosphorylation sites that serve as potential docking sites for Src homology 2-containing proteins such as ras GTPase-activating protein and Nck, leading to inhibition of ras signaling pathway activation and the c-Jun N-terminal kinase (JNK) and c-Jun activation, respectively. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-1 and Dok-2 act as negative regulators of the Ras-Erk pathway downstream of many immunoreceptor-mediated signaling systems, and it is believed that recruitment of p120 rasGAP by Dok-1 and Dok-2 is critical to their negative regulation. Dok-3 is a negative regulator of the activation of JNK and mobilization of Ca2+ in B-cell receptor-mediated signaling, interacting with SHIP-1 and Grb2. Dok-4- 6 play roles in protein tyrosine kinase(PTK)-mediated signaling in neural cells and Dok-7 is the key cytoplasmic activator of MuSK (Muscle-Specific Protein Tyrosine Kinase). PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the IRS-like subgroup.


Pssm-ID: 241318  Cd Length: 103  Bit Score: 39.33  E-value: 3.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720432655  334 LLGITKDSVMRVD-EKTKEVLQEWPLTTVKRWAASPKSFTLDFG---EYQESYYSVQTTEGEQISQ 395
Cdd:cd13164     24 LLQITHENIYLWDiHNPRVKLVSWPLCSLRRYGRDSTWFTFEAGrmcDTGEGLFTFQTREGEQIYQ 89
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
314-409 6.46e-03

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. 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: 270020  Cd Length: 96  Bit Score: 38.39  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  314 GVSFFLVKEKmkGKNKLVPRLL-GITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEY-QESYYSVQTTEGE 391
Cdd:cd13199      1 GSAFFEVKQT--TDPSLPEILLiAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLvRGSKLLCETSLGY 78
                           90
                   ....*....|....*...
gi 1720432655  392 QISQLIAGYIDIILKKKQ 409
Cdd:cd13199     79 KMDDLLTSYISLLLSNMK 96
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
691-767 9.03e-03

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: 39.10  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432655  691 AKNVA------QVAEDTVLQN-----RVIAAATQCALSTSQLVACAKVVSPTISSpvCQEQLIEAGKLVDRSVENCVRAC 759
Cdd:pfam01608   13 AKAVAaatnllVEAADGVVQGqgseeELIVAAKEVAASTAQLVAASRVKADPNSK--TQQRLEAASKAVTDATKNLVAAV 90

                   ....*...
gi 1720432655  760 QAATSDSE 767
Cdd:pfam01608   91 KSAAELQE 98
 
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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