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Conserved domains on  [gi|23956088|ref|NP_062279|]
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formin-binding protein 1 isoform b [Mus musculus]

Protein Classification

F-BAR domain-containing protein( domain architecture ID 10166631)

F-BAR (FES-CIP4 homology and Bin/Amphiphysin/Rvs) domain-containing protein

Graphical summary

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List of domain hits

 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; ...
 5-257 2.91e-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: 470.68  E-value: 2.91e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYA 84
Cdd:cd07676   1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  85 GQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 164
Cdd:cd07676  81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 165 TKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPI 244
Cdd:cd07676 161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                       250
                ....*....|...
gi 23956088 245 IGKCLDGIVKAAE 257
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; ...
 5-257 2.91e-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: 470.68  E-value: 2.91e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYA 84
Cdd:cd07676   1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  85 GQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 164
Cdd:cd07676  81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 165 TKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPI 244
Cdd:cd07676 161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                       250
                ....*....|...
gi 23956088 245 IGKCLDGIVKAAE 257
Cdd:cd07676 241 IGKCLDGITKAAE 253
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 10-88 1.46e-17

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: 76.15  E-value: 1.46e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956088    10 QFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEykYTACKAFLSTLNEMNDYAGQHE 88
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDG--GTLKKAWDELLTETEQLAKQHL 77
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 1-88 3.04e-13

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: 64.67  E-value: 3.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088      1 MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKkyQPKKNSKEEEEYKYTAcKAFLSTLNEM 80
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK--KLRAVRDTEPEYGSLS-KAWEVLLSET 77


                   ....*...
gi 23956088     81 NDYAGQHE 88
Cdd:smart00055  78 DALAKQHL 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; ...
 5-257 2.91e-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: 470.68  E-value: 2.91e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYA 84
Cdd:cd07676   1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  85 GQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 164
Cdd:cd07676  81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 165 TKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPI 244
Cdd:cd07676 161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                       250
                ....*....|...
gi 23956088 245 IGKCLDGIVKAAE 257
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 ...
 5-257 1.02e-115

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: 334.99  E-value: 1.02e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKnsKEEEEYKYTACKAFLSTLNEMNDYA 84
Cdd:cd07653   1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKK--KEEDEYSFSSVKAFRSILNEVNDIA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  85 GQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 164
Cdd:cd07653  79 GQHELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 165 TKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPI 244
Cdd:cd07653 159 TKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPI 238

                       250
                ....*....|...
gi 23956088 245 IGKCLDGIVKAAE 257
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; ...
 5-257 2.75e-111

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: 323.93  E-value: 2.75e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEyKYTACKAFLSTLNEMNDYA 84
Cdd:cd07675   1 TELWDQFDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRNLVKKYCPKRSSKDEEP-RFTSCLSFYNILNELNDYA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  85 GQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 164
Cdd:cd07675  80 GQREVVAEEMGHRVYGELMRYSHDLKGERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 165 TKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPI 244
Cdd:cd07675 160 TKSDVEKAKQQLNLRTHMADESKNEYAAQLQNFNGEQHKHFYIVIPQIYKQLQEMDERRTVKLSECYRGFADSERKVIPI 239

                       250
                ....*....|...
gi 23956088 245 IGKCLDGIVKAAE 257
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 ...
 10-254 4.13e-26

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: 102.80  E-value: 4.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  10 QFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKnskeeeEYKYTACKAFLSTLNEMNDYAGQHEV 89
Cdd:cd07610   1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKP------ESGKTSLGTSWNSLREETESAATVHE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  90 ISENMTSQITVDLMRYVQEL-KQERKSNFHDGRKAQQHIETCWKQLESSKrrferdckeadraqqyfekmdadinvtkad 168
Cdd:cd07610  75 ELSEKLSQLIREPLEKVKEDkEQARKKELAEGEKLKKKLQELWAKLAKKA------------------------------ 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 169 vekarqqaqirqqmaedsKADYSLILQRFNQEQWEYYHTHIPNIfQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKC 248
Cdd:cd07610 125 ------------------DEEYREQVEKLNPAQSEYEEEKLNKI-QAEQEREEERLEILKDNLKNYINAIKEIPQKIQQE 185


                ....*.
gi 23956088 249 LDGIVK 254
Cdd:cd07610 186 LEQSIN 191
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 10-88 1.46e-17

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: 76.15  E-value: 1.46e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956088    10 QFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEykYTACKAFLSTLNEMNDYAGQHE 88
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 ...
 11-224 1.12e-13

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: 69.43  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  11 FDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKnskeeeeyKYTACKAFLSTLNEMNDYAGQ-HEV 89
Cdd:cd07647   7 FDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGD--------EIGTLKSSWDSLRKETENVANaHIQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  90 ISENMTSQITvDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDAdiNVTKADV 169
Cdd:cd07647  79 LAQSLREEAE-KLEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSS--GAQPKEA 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23956088 170 EKARQQAQIRQQMAEDSKADYSL---ILQRFNQEqWEYYHTHIPNIFQKiqeMEERRI 224
Cdd:cd07647 156 EKLKKKAAQCKTSAEEADSAYKSsigCLEDARVE-WESEHATACQVFQN---MEEERI 209
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 1-88 3.04e-13

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: 64.67  E-value: 3.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088      1 MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKkyQPKKNSKEEEEYKYTAcKAFLSTLNEM 80
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK--KLRAVRDTEPEYGSLS-KAWEVLLSET 77


                   ....*...
gi 23956088     81 NDYAGQHE 88
Cdd:smart00055  78 DALAKQHL 85
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 28-234 5.60e-08

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: 53.09  E-value: 5.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  28 YIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEykyTACKAFLSTLNEMNDYAGQHEVISENMTSQItvdlmryVQ 107
Cdd:cd07655  24 LMKMVQERAEIEKAYAKKLKEWAKKWRDLIEKGPEYG---TLETAWKGLLSEAERLSELHLSIRDKLLNDV-------VE 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 108 ELKQERKSNFH--------------DG-RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKA 172
Cdd:cd07655  94 EVKTWQKENYHksmmggfketkeaeDGfAKAQKPWAKLLKKVEKAKKAYHAACKAEKSAQKQENNAKSDTSLSPDQVKKL 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956088 173 RQQAQIRQQMAEDSKADYSLILQRFNQEQwEYYHTHIPNIFQKIQEMEERRIVRIGESMKTY 234
Cdd:cd07655 174 QDKVEKCKQEVSKTKDKYEKALEDLNKYN-PRYMEDMEQVFDKCQEFEEKRLDFFKEILLSY 234
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-229 4.92e-07

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: 50.43  E-value: 4.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  32 VKERTEIELSYAKQLRNLSKKYQ------PKKNSKEeeeykytacKAFLSTLNEMNDYAGQHEVISENMTSQitvDLmry 105
Cdd:cd07680  28 VQERAKIEKAYGQQLTDWAKRWRqliekgPQYGSLE---------RAWGAIMTEADKVSELHQEVKNNLLNE---DL--- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 106 vQELKQERKSNFH--------------DG-RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVE 170
Cdd:cd07680  93 -EKVKNWQKDAYHkqimggfketkeaeDGfRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREANSKAEQSVTPEQQK 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23956088 171 KARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHThIPNIFQKIQEMEERRIVRIGE 229
Cdd:cd07680 172 KLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMEN-MEQVFEQCQQFEEKRLVFLKE 229
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 11-171 2.18e-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: 48.07  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  11 FDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQpkkNSKEEEEYKytacKAFLSTLNEMNDYAGQHEVI 90
Cdd:cd07651   7 FDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSL---GGSEEGGLK----NSLDTLRLETESMAKSHLKF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  91 SENMTSQITVDLMRYVQELKQERKsnfhdgrKAQQHIE-------TCWKQLESSKRRFERDC---------------KEA 148
Cdd:cd07651  80 AKQIRQDLEEKLAAFASSYTQKRK-------KIQSHMEkllkkkqDQEKYLEKAREKYEADCskinsytlqsqltwgKEL 152

                       170       180
                ....*....|....*....|...
gi 23956088 149 DRAQQYFEKMDADINVTKADVEK 171
Cdd:cd07651 153 EKNNAKLNKAQSSINSSRRDYQN 175
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 31-286 7.80e-05

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: 43.51  E-value: 7.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  31 FVKERTEIELSYAKQLRNLSKKyqpkknskeeeeykytackafLSTLNEMNDYAGQHEVI--SENMTSQITVDLMRYVQE 108
Cdd:cd07673  34 FIRERATIEEAYSRSMTKLAKS---------------------ASNYSQLGTFAPVWDVFktSTEKLANCHLELVRKLQE 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 109 LKQE--------------RKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYfekmdadiNVTKADVEKARQ 174
Cdd:cd07673  93 LIKEvqkygeeqvkshkkTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKE--------GATQREIEKAAV 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 175 QAQIRQQMAEDSKADYSLILQRFNQEQWEyyhthipnIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVK 254
Cdd:cd07673 165 KSKKATESYKLYVEKYALAKADFEQKMTE--------TAQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQIGQVHEEFIN 236

                       250       260       270
                ....*....|....*....|....*....|..
gi 23956088 255 AAESIDQKNDSQLVVEAYKSGFEPPGDIEFED 286
Cdd:cd07673 237 NMANTTVESLIQKFAESKGTGKERPGPIEFEE 268
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 9-214 8.22e-05

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: 43.46  E-value: 8.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   9 DQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKY-----QPKKNSKEEEEYKYTACKAFLstlnEMNDY 83
Cdd:cd07678   5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFlkrdwHRGGNETEMDRSVRTVWGAWR----EGTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  84 AGQHEVISENMTSQITvDLMRYVQELKQER--KSNFHDGRKAQQHIETCWKQLESSKRRF---ERDCKEA-DRA---QQY 154
Cdd:cd07678  81 TGQGRVTRLEAYRRLR-DEAGKTGRSAKEQvlKKSTEQLQKAQAELLETVKELSKSKKLYgqlERVSEVAkEKAadvEAR 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956088 155 FEKMDADINVTKADVEKarQQAQIRQQMAEDSKA------DYSLILQRFNQEQWEYYHTHIPNIFQ 214
Cdd:cd07678 160 LNKSDHGIFHSKASLQK--LSAKFSAQSAEYSQQlqaarnEYLLNLVAANAHLDHYYQEELPAIMK 223
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 11-220 8.77e-05

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: 43.40  E-value: 8.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  11 FDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKyqpkknsKEEEEYKYTACKAFLSTLNEMNDYAGQHEVI 90
Cdd:cd07672   7 YDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKK-------KPCGQTEINTLKRSLDVFKQQIDNVGQSHIQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  91 SENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKAdvE 170
Cdd:cd07672  80 LAQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQ--E 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 23956088 171 KARQQAQIRQQMAEDSKADYSLILQRFNQ--EQWEYYHTHIPNIFQKiQEME 220
Cdd:cd07672 158 KLFAKLAQSKQNAEDADRLYMQNISVLDKirEDWQKEHVKACEFFEK-QECE 208
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 9-216 2.15e-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: 42.42  E-value: 2.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   9 DQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQ----PKKNSKEEEEYK--YTACKAFLSTLNEMnd 82
Cdd:cd07677   5 EQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLksdwRGMKADERADYRsmYTVWKSFLEGTMQV-- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  83 yAGQHEVISENMTSQITvDLMRYVQELKQERKSNFHDG-RKAQQHIETCWKQLESSKRRFerdcKEADR-AQQYFEKMDA 160
Cdd:cd07677  83 -AQSRINICENYKNLIS-EPARTVRLYKEQQLKRCVDQlTKIQAELQETVKDLAKGKKKY----FETEQmAHAVREKADI 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956088 161 D-----------INVTKADVeKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKI 216
Cdd:cd07677 157 EaksklslfqsrISLQKASV-KLKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKAL 222
F-BAR_Fer cd07686
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine ...
 5-237 2.18e-04

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: 41.97  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKkyQPKKNSKEEEEYKYTACKAFLSTLNEMNDYA 84
Cdd:cd07686   1 SDLRNSHEALLKLQDWELRLLETVKKFMALRVKSDKEYASTLQNLCN--QVDKESTSQLDYVSNVSKSWLHMVQQTEQLS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  85 GQHEVISENMTSQITVDLMRYVQELKQERKS--NFHDGRKAQQhIETCWKQLESSKRRFERDCKEADRAQQYFEkmdaDI 162
Cdd:cd07686  79 KIMKTHAEELNSGPLHRLTMMIKDKQQVKKSyiGVHQQIEAEM-YKVTKTELEKLKCSYRQLTKEVNSAKEKYK----DA 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956088 163 NVTKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEV 237
Cdd:cd07686 154 VAKGKETEKARERYDKATMKLHMLHNQYVLAVKGAQLHQHQYYDFTLPLLLDSLQKMQEEMIKALKGILDEYSQI 228
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 33-224 2.69e-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: 41.85  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  33 KERTEIELSYAKQLRNLSKKYqpkKNSKEEEEYKYTACKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQEL--K 110
Cdd:cd07681  29 QERAKIEKGYAQQLSDWARKW---RGIVEKGPQYGTLEKAWHAFLTAAERLSEIHLELRENLVGEDSEKVRAWQKEAfhK 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 111 Q------ERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRQQMAE 184
Cdd:cd07681 106 QmiggfrESKEAEEGFRKAQKPWVKKLKEVESSKKGYHAARKDERTAQTRETHAKADSTVSQEQLRKLQDRVEKCTQEAE 185

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23956088 185 DSKADYSLILQRFNQEQWEYYHThIPNIFQKIQEMEERRI 224
Cdd:cd07681 186 KAKEQYEKALEELNRYNPRYMED-MEQAFEICQEAERKRL 224
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-224 2.93e-04

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: 41.97  E-value: 2.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  32 VKERTEIELSYAKQLRNLSKKYqpkKNSKEEEEYKYTACKAFLSTLNEMNDYAGQH-EVISENMTSQItvdlmryvQELK 110
Cdd:cd07679  28 LHERARIEKVYAQQLTEWAKRW---RQLVEKGPQYGTVEKAWCALMSEAEKVSELHlEVKASLMNEDF--------EKIK 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 111 QERKSNFH--------------DG-RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQ 175
Cdd:cd07679  97 NWQKEAFHkqmmggfketkeaeDGfRKAQKPWAKKLKEVEAAKKAYHTACKEEKLATSREANSKADPALNPEQLKKLQDK 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23956088 176 AQIRQQMAEDSKADYSLILQRFNQEQWEYYHtHIPNIFQKIQEMEERRI 224
Cdd:cd07679 177 VEKCKQDVLKTKEKYEKSLKELDQTTPQYME-NMEQVFEQCQQFEEKRL 224
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 5-111 3.11e-04

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: 41.61  E-value: 3.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTacKAFLSTLN------ 78
Cdd:cd07684   1 TQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRTSREHQFKKD--QQLLSPVNcwylvl 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 23956088  79 -----EMNDYAGQHEVISENMT---SQITVDLMRYVQELKQ 111
Cdd:cd07684  79 eqtrrESRDHATLNDIFNNNVIvrlSQISEDVIRLFKKSKE 119
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 32-226 3.52e-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: 41.48  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  32 VKERTEIELSYAKQLRNLSKKY--QPKKNSkeeeeykytaCKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQEL 109
Cdd:cd07671  28 LKQRAQAEERYGKELVQIARKAggQTEINT----------LKASFDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQ 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088 110 KQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDAdiNVTKADVEKARQQAQIRQQMAEDSKAD 189
Cdd:cd07671  98 KEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSS--TGNPKQSEKSQNKAKQCRDAATEAERV 175

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23956088 190 YSLILQRFNQ--EQWEYYHTHIPNIFQkIQEMEERRIVR 226
Cdd:cd07671 176 YKQNIEQLDKarTEWETEHILTCEVFQ-LQEDDRITILR 213
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 26-150 5.52e-04

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: 40.79  E-value: 5.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  26 EKYIKFVKERTEIELSYAKQLRNLSKKYQpkknskeeEEYKYTACKA--FLSTLNEMndyAGQHEVISENMTSQITV--- 100
Cdd:cd07652  22 KEFATFLKKRAAIEEEHARGLKKLARTTL--------DTYKRPDHKQgsFSNAYHSS---LEFHEKLADNGLRFAKAlne 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 23956088 101 ---DLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADR 150
Cdd:cd07652  91 msdELSSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLER 143
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 5-103 9.84e-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: 40.01  E-value: 9.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   5 TELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPK---KNSKEEEEYKYTACKAFLSTLNEMN 81
Cdd:cd07656   1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKhknEKSKREDWSLLSPVNCWNTLLVQTK 80

                        90       100
                ....*....|....*....|..
gi 23956088  82 DYAGQHEVISENMTSQITVDLM 103
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 ...
 9-214 4.84e-03

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: 37.95  E-value: 4.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088   9 DQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQ----PKKNSKEEEEYK--YTACKAFLSTLNEMnd 82
Cdd:cd07654   5 EQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLkrewPGSGELKPEDDRsgYTVWGAWLEGLDAV-- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956088  83 yAGQHEVISENMTSQItVDLMRYVQELK-QERKSNFHDGRKAQQHIETCWKQLESSKRR-FER-----DCKE-ADRAQQY 154
Cdd:cd07654  83 -AQSRQNRCEAYRRYI-SEPAKTGRSAKeQQLKKCTEQLQRAQAEVQQTVRELSKSRKTyFEReqvahLAREkAADVQAR 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956088 155 FEKMDADINVTKADVEKA----RQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQ 214
Cdd:cd07654 161 EARSDLSIFQSRTSLQKAsvklSARKAECSSKATAARNDYLLNLAATNAHQDRYYQTDLPAIIK 224
 
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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