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Conserved domains on  [gi|149241439]
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Chain A, Formin-binding protein 1

Protein Classification

BAR domain-containing protein( domain architecture ID 36964)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature

CATH:  1.20.1270.60
Gene Ontology:  GO:0097753|GO:0140090
PubMed:  19379681|16524918|14993925|15649145|30456600
SCOP:  4001895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 10-262 2.80e-169

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07676:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 253  Bit Score: 469.53  E-value: 2.80e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNE*NDYA 89
Cdd:cd07676    1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  90 GQHEVISEN*ASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINV 169
Cdd:cd07676   81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 170 TKADVEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQE*EERRIVR*GES*KTYAEVDRQVIPI 249
Cdd:cd07676  161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                        250
                 ....*....|...
gi 149241439 250 IGKCLDGIVKAAE 262
Cdd:cd07676  241 IGKCLDGITKAAE 253
 
Name Accession Description Interval E-value
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 10-262 2.80e-169

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153360 [Multi-domain]  Cd Length: 253  Bit Score: 469.53  E-value: 2.80e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNE*NDYA 89
Cdd:cd07676    1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  90 GQHEVISEN*ASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINV 169
Cdd:cd07676   81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 170 TKADVEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQE*EERRIVR*GES*KTYAEVDRQVIPI 249
Cdd:cd07676  161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                        250
                 ....*....|...
gi 149241439 250 IGKCLDGIVKAAE 262
Cdd:cd07676  241 IGKCLDGITKAAE 253
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 15-93 3.37e-16

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 71.92  E-value: 3.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149241439   15 QFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEykYTSCKAFISNLNE*NDYAGQHE 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDG--GTLKKAWDELLTETEQLAKQHL 77
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-93 8.57e-12

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 60.05  E-value: 8.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439     7 SWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKkyQPKKNSKEEEEYKYTScKAFISNLNE*N 86
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK--KLRAVRDTEPEYGSLS-KAWEVLLSETD 78


                   ....*..
gi 149241439    87 DYAGQHE 93
Cdd:smart00055  79 ALAKQHL 85
 
Name Accession Description Interval E-value
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 10-262 2.80e-169

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153360 [Multi-domain]  Cd Length: 253  Bit Score: 469.53  E-value: 2.80e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNE*NDYA 89
Cdd:cd07676    1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  90 GQHEVISEN*ASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINV 169
Cdd:cd07676   81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 170 TKADVEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQE*EERRIVR*GES*KTYAEVDRQVIPI 249
Cdd:cd07676  161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                        250
                 ....*....|...
gi 149241439 250 IGKCLDGIVKAAE 262
Cdd:cd07676  241 IGKCLDGITKAAE 253
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 10-262 6.29e-117

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 336.92  E-value: 6.29e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKnsKEEEEYKYTSCKAFISNLNE*NDYA 89
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKK--KEEDEYSFSSVKAFRSILNEVNDIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  90 GQHEVISEN*ASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINV 169
Cdd:cd07653   79 GQHELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 170 TKADVEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQE*EERRIVR*GES*KTYAEVDRQVIPI 249
Cdd:cd07653  159 TKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPI 238

                        250
                 ....*....|...
gi 149241439 250 IGKCLDGIVKAAE 262
Cdd:cd07653  239 IAKCLDGIKKAGD 251
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 10-262 5.34e-107

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FormiN Binding Protein 1-Like (FNBP1L), also known as Toca-1 (Transducer of Cdc42-dependent actin assembly), forms a complex with neural Wiskott-Aldrich syndrome protein (N-WASP). The FNBP1L/N-WASP complex induces the formation of filopodia and endocytic vesicles. FNBP1L is required for Cdc42-induced actin assembly and is essential for autophagy of intracellular pathogens. It contains an N-terminal F-BAR domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153359 [Multi-domain]  Cd Length: 252  Bit Score: 311.60  E-value: 5.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEyKYTSCKAFISNLNE*NDYA 89
Cdd:cd07675    1 TELWDQFDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRNLVKKYCPKRSSKDEEP-RFTSCLSFYNILNELNDYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  90 GQHEVISEN*ASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINV 169
Cdd:cd07675   80 GQREVVAEEMGHRVYGELMRYSHDLKGERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 170 TKADVEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQE*EERRIVR*GES*KTYAEVDRQVIPI 249
Cdd:cd07675  160 TKSDVEKAKQQLNLRTHMADESKNEYAAQLQNFNGEQHKHFYIVIPQIYKQLQEMDERRTVKLSECYRGFADSERKVIPI 239

                        250
                 ....*....|...
gi 149241439 250 IGKCLDGIVKAAE 262
Cdd:cd07675  240 ISKCLEGMVLAAK 252
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 15-259 2.08e-29

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 110.51  E-value: 2.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  15 QFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKnskeeeEYKYTSCKAFISNLNE*NDYAGQHEV 94
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKP------ESGKTSLGTSWNSLREETESAATVHE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  95 ISEN*ASQIIVDLARYVQEL-KQERKSNFHDGRKAQQHIETCWKQLESSKrrferdckeadraqqyfek*dadinvtkad 173
Cdd:cd07610   75 ELSEKLSQLIREPLEKVKEDkEQARKKELAEGEKLKKKLQELWAKLAKKA------------------------------ 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 174 vekarqqaqirhq*aedsKADYSSILQKFNHEQHEYYHTHIPNIfQKIQE*EERRIVR*GES*KTYAEVDRQVIPIIGKC 253
Cdd:cd07610  125 ------------------DEEYREQVEKLNPAQSEYEEEKLNKI-QAEQEREEERLEILKDNLKNYINAIKEIPQKIQQE 185


                 ....*.
gi 149241439 254 LDGIVK 259
Cdd:cd07610  186 LEQSIN 191
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 15-93 3.37e-16

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 71.92  E-value: 3.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149241439   15 QFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEykYTSCKAFISNLNE*NDYAGQHE 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDG--GTLKKAWDELLTETEQLAKQHL 77
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 16-229 3.47e-12

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 64.81  E-value: 3.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  16 FDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKnskeeeeyKYTSCKAFISNLNE*NDYAGQHEVI 95
Cdd:cd07647    7 FDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGD--------EIGTLKSSWDSLRKETENVANAHIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  96 SEN*ASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DAdiNVTKADVE 175
Cdd:cd07647   79 LAQSLREEAEKLEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSS--GAQPKEAE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149241439 176 KARQQAQIRHQ*AEDSKADYSS---ILQKfNHEQHEYYHTHIPNIFQKIqe*EERRI 229
Cdd:cd07647  157 KLKKKAAQCKTSAEEADSAYKSsigCLED-ARVEWESEHATACQVFQNM---EEERI 209
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-93 8.57e-12

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 60.05  E-value: 8.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439     7 SWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKkyQPKKNSKEEEEYKYTScKAFISNLNE*N 86
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK--KLRAVRDTEPEYGSLS-KAWEVLLSETD 78


                   ....*..
gi 149241439    87 DYAGQHE 93
Cdd:smart00055  79 ALAKQHL 85
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 33-229 1.55e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153339 [Multi-domain]  Cd Length: 258  Bit Score: 51.55  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  33 YIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISnlnE*NDYAGQHEVISEN*ASQIivdlaryVQ 112
Cdd:cd07655   24 LMKMVQERAEIEKAYAKKLKEWAKKWRDLIEKGPEYGTLETAWKGLLS---EAERLSELHLSIRDKLLNDV-------VE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 113 ELKQERKSNFH--------------DG-RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINVTKADVEKA 177
Cdd:cd07655   94 EVKTWQKENYHksmmggfketkeaeDGfAKAQKPWAKLLKKVEKAKKAYHAACKAEKSAQKQENNAKSDTSLSPDQVKKL 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149241439 178 RQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHThIPNIFQKIQE*EERRI 229
Cdd:cd07655  174 QDKVEKCKQEVSKTKDKYEKALEDLNKYNPRYMED-MEQVFDKCQEFEEKRL 224
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 14-219 1.90e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153362 [Multi-domain]  Cd Length: 263  Bit Score: 48.47  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  14 DQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKY-----QPKKNSKEEEEYKYTSCKAFIsnlnE*NDY 88
Cdd:cd07678    5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFlkrdwHRGGNETEMDRSVRTVWGAWR----EGTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  89 AGQHEVISeN*ASQIIVDLARYVQELKQER--KSNFHDGRKAQQHIETCWKQLESSKRRF---ERDCKEA-DRA---QQY 159
Cdd:cd07678   81 TGQGRVTR-LEAYRRLRDEAGKTGRSAKEQvlKKSTEQLQKAQAELLETVKELSKSKKLYgqlERVSEVAkEKAadvEAR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149241439 160 FEK*DADINVTKADVEK-----ARQQAQIRHQ*AEdSKADYSSILQKFNHEQHEYYHTHIPNIFQ 219
Cdd:cd07678  160 LNKSDHGIFHSKASLQKlsakfSAQSAEYSQQLQA-ARNEYLLNLVAANAHLDHYYQEELPAIMK 223
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 37-230 2.08e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 48.12  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  37 VKERTEIELSYAKQLRNLSKKYQpkknSKEEEEYKYTSC-KAFISNLNE*NDYAGQHEVISEN*ASQIIVDLARYVQEL- 114
Cdd:cd07680   28 VQERAKIEKAYGQQLTDWAKRWR----QLIEKGPQYGSLeRAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAy 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 115 -KQ------ERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINVTKADVEKARQQAQIRHQ* 187
Cdd:cd07680  104 hKQimggfkETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREANSKAEQSVTPEQQKKLQDKVDKCKQD 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 149241439 188 AEDSKADYSSILQKFNHEQHEYYHThIPNIFQKIQE*EERRIV 230
Cdd:cd07680  184 VQKTQEKYEKVLDDVGKTTPQYMEN-MEQVFEQCQQFEEKRLV 225
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 16-204 4.14e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 46.91  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  16 FDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQpkkNSKEEEEYKytscKAFISNLNE*NDYAGQHEVI 95
Cdd:cd07651    7 FDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSL---GGSEEGGLK----NSLDTLRLETESMAKSHLKF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  96 SEN*ASQIIVDLARYVQELKQERKsnfhdgrKAQQHIE-------TCWKQLESSKRRFERDC---------------KEA 153
Cdd:cd07651   80 AKQIRQDLEEKLAAFASSYTQKRK-------KIQSHMEkllkkkqDQEKYLEKAREKYEADCskinsytlqsqltwgKEL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149241439 154 DRAQQYFEK*DADINVTKADVEKARQQAQIRHQ*AEDskaDYSSILQKFNH 204
Cdd:cd07651  153 EKNNAKLNKAQSSINSSRRDYQNAVKALRELNEIWNR---EWKAALDDFQD 200
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 37-229 6.59e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 2 (PACSIN2); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSIN 2 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153363 [Multi-domain]  Cd Length: 258  Bit Score: 43.52  E-value: 6.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  37 VKERTEIELSYAKQLRNLSKKYqpkKNSKEEEEYKYTSCKAFISNLNE*NDYAGQHEvisEN*ASQIIVDLaryvQELKQ 116
Cdd:cd07679   28 LHERARIEKVYAQQLTEWAKRW---RQLVEKGPQYGTVEKAWCALMSEAEKVSELHL---EVKASLMNEDF----EKIKN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 117 ERKSNFH--------------DG-RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINVTKADVEKARQQA 181
Cdd:cd07679   98 WQKEAFHkqmmggfketkeaeDGfRKAQKPWAKKLKEVEAAKKAYHTACKEEKLATSREANSKADPALNPEQLKKLQDKV 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 149241439 182 QIRHQ*AEDSKADYSSILQKFNHEQHEYYHtHIPNIFQKIQE*EERRI 229
Cdd:cd07679  178 EKCKQDVLKTKEKYEKSLKELDQTTPQYME-NMEQVFEQCQQFEEKRL 224
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 38-229 1.03e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 3 or Syndapin III is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSIN 3 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153365 [Multi-domain]  Cd Length: 258  Bit Score: 43.00  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  38 KERTEIELSYAKQLRNLSKKYqpkKNSKEEEEYKYTSCKAFISNLNE*NDYAGQHEVISEN*ASQIIVDLARYVQEL--K 115
Cdd:cd07681   29 QERAKIEKGYAQQLSDWARKW---RGIVEKGPQYGTLEKAWHAFLTAAERLSEIHLELRENLVGEDSEKVRAWQKEAfhK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 116 Q------ERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DADINVTKADVEKARQQAQIRHQ*AE 189
Cdd:cd07681  106 QmiggfrESKEAEEGFRKAQKPWVKKLKEVESSKKGYHAARKDERTAQTRETHAKADSTVSQEQLRKLQDRVEKCTQEAE 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 149241439 190 DSKADYSSILQKFNHEQHEYYHThIPNIFQKIQE*EERRI 229
Cdd:cd07681  186 KAKEQYEKALEELNRYNPRYMED-MEQAFEICQEAERKRL 224
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 115-229 1.25e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 42.64  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 115 KQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEK*DAdiNVTKADVEKARQQAQIRHQ*AEDSKAD 194
Cdd:cd07671   98 KEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSS--TGNPKQSEKSQNKAKQCRDAATEAERV 175

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 149241439 195 YSSILQKFNHEQHEYYHTHIpNIFQKIQE*EERRI 229
Cdd:cd07671  176 YKQNIEQLDKARTEWETEHI-LTCEVFQLQEDDRI 209
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 14-221 1.39e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 (FCHSD2); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 2 (FCHSD2) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153361 [Multi-domain]  Cd Length: 260  Bit Score: 42.81  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  14 DQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPK--KNSKEEEEYKYTSCKAFISNLNE*NDYAGQ 91
Cdd:cd07677    5 EQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLKSdwRGMKADERADYRSMYTVWKSFLEGTMQVAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  92 HEV-ISEN*ASqIIVDLARYVQELKQERKSNFHDG-RKAQQHIETCWKQLESSKRRFerdcKEADR-AQQYFEK*DAD-- 166
Cdd:cd07677   85 SRInICENYKN-LISEPARTVRLYKEQQLKRCVDQlTKIQAELQETVKDLAKGKKKY----FETEQmAHAVREKADIEak 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149241439 167 ---------INVTKADVE-KARQQAQirHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKI 221
Cdd:cd07677  160 sklslfqsrISLQKASVKlKARRSEC--NSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKAL 222
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 16-214 2.59e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 41.47  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  16 FDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKyqpkknsKEEEEYKYTSCKAFISNLNE*NDYAGQHEVi 95
Cdd:cd07672    7 YDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKK-------KPCGQTEINTLKRSLDVFKQQIDNVGQSHI- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  96 sen*ASQIIVDLARYVQELKQERKsnfHDGRKAQQHIETCWKQ-------LESSKRRFERDCKEADRAQQYFEK*DADIN 168
Cdd:cd07672   79 ---QLAQTLRDEAKKMEDFRERQK---LARKKIELIMDAIHKQramqfkkTMESKKNYEQKCRDKDEAEQAVNRNANLVN 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 149241439 169 VTKAdvEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHI 214
Cdd:cd07672  153 VKQQ--EKLFAKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHV 196
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 36-291 3.34e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 41.58  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  36 FVKERTEIELSYAKQLRNLSKKyqpkknskeeeeykytsckafISNLNE*NDYAGQHEVI--SEN*ASQIIVDLARYVQE 113
Cdd:cd07673   34 FIRERATIEEAYSRSMTKLAKS---------------------ASNYSQLGTFAPVWDVFktSTEKLANCHLELVRKLQE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 114 LKQE--------------RKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYfek*dadiNVTKADVEKArq 179
Cdd:cd07673   93 LIKEvqkygeeqvkshkkTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKE--------GATQREIEKA-- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439 180 qaQIRHQ*AEDSkadYSSILQKFNHEQHEYyHTHIPNIFQKIQE*EERRIVR*GES*KTYAEVDRQVIPIIGKCLDGIVK 259
Cdd:cd07673  163 --AVKSKKATES---YKLYVEKYALAKADF-EQKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQIGQVHEEFIN 236

                        250       260       270
                 ....*....|....*....|....*....|..
gi 149241439 260 AAESIDQKNDSQLVIEAYKSGFEPPGDIEFED 291
Cdd:cd07673  237 NMANTTVESLIQKFAESKGTGKERPGPIEFEE 268
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 10-108 6.02e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs, all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153340 [Multi-domain]  Cd Length: 241  Bit Score: 40.39  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPK---KNSKEEEEYKYTSCKAFISNLNE*N 86
Cdd:cd07656    1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKhknEKSKREDWSLLSPVNCWNTLLVQTK 80

                         90       100
                 ....*....|....*....|..
gi 149241439  87 DYAGQHEVISEN*ASQIIVDLA 108
Cdd:cd07656   81 QESRDHSTLSDIYSNNLVQRLG 102
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
 14-219 6.34e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153338 [Multi-domain]  Cd Length: 264  Bit Score: 40.64  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  14 DQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKK--NSKEEEEYKYTSCKAFISNLNE*NDYAGQ 91
Cdd:cd07654    5 EQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLKREwpGSGELKPEDDRSGYTVWGAWLEGLDAVAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  92 HEV-ISEN*ASQiIVDLARYVQELK-QERKSNFHDGRKAQQHIETCWKQLESSKRR-FERDC------KEADRAQQYFEK 162
Cdd:cd07654   85 SRQnRCEAYRRY-ISEPAKTGRSAKeQQLKKCTEQLQRAQAEVQQTVRELSKSRKTyFEREQvahlarEKAADVQAREAR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149241439 163 *DADINVTKADVEKARQQAQIR----HQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQ 219
Cdd:cd07654  164 SDLSIFQSRTSLQKASVKLSARkaecSSKATAARNDYLLNLAATNAHQDRYYQTDLPAIIK 224
F-BAR_Fer cd07686
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine ...
 10-229 1.17e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine kinase; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fer (Fes related) is a cytoplasmic (or nonreceptor) tyrosine kinase expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells. It contains an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153370 [Multi-domain]  Cd Length: 234  Bit Score: 39.66  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKkyQPKKNSKEEEEYKYTSCKAFISNLNE*NDYA 89
Cdd:cd07686    1 SDLRNSHEALLKLQDWELRLLETVKKFMALRVKSDKEYASTLQNLCN--QVDKESTSQLDYVSNVSKSWLHMVQQTEQLS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  90 GQHEVISEN*ASQIIVDLARYVQELKQERKS--NFHDGRKAQQhIETCWKQLESSKRRFERDCKEADRAQQYFEk*daDI 167
Cdd:cd07686   79 KIMKTHAEELNSGPLHRLTMMIKDKQQVKKSyiGVHQQIEAEM-YKVTKTELEKLKCSYRQLTKEVNSAKEKYK----DA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149241439 168 NVTKADVEKARQQAQIRHQ*AEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQE*EERRI 229
Cdd:cd07686  154 VAKGKETEKARERYDKATMKLHMLHNQYVLAVKGAQLHQHQYYDFTLPLLLDSLQKMQEEMI 215
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 10-71 2.73e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 3; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP3, also called MEGAP (MEntal disorder associated GTPase-Activating Protein), is a Rho GAP with activity towards Rac1 and Cdc42. It impacts cell migration by regulating actin and microtubule cytoskeletal dynamics. The association between srGAP3 haploinsufficiency and mental retardation is under debate. srGAP3 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153368 [Multi-domain]  Cd Length: 253  Bit Score: 38.53  E-value: 2.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149241439  10 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYK 71
Cdd:cd07684    1 TQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRTSREHQFK 62
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 31-155 4.94e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 37.71  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149241439  31 EKYIKFVKERTEIELSYAKQLRNLSKKYQpkknskeeEEYKYTSCKAfISNLNE*NDYAGQHEVISEN*AS------QII 104
Cdd:cd07652   22 KEFATFLKKRAAIEEEHARGLKKLARTTL--------DTYKRPDHKQ-GSFSNAYHSSLEFHEKLADNGLRfakalnEMS 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149241439 105 VDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADR 155
Cdd:cd07652   93 DELSSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLER 143
 
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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