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Conserved domains on  [gi|240104577|pdb|3HAI|C]
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Chain C, human PACSIN1 F-BAR

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 19-276 0e+00

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: 499.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 98
Cdd:cd07680   1 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSK 178
Cdd:cd07680  81 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREANSK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      179 TEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 258
Cdd:cd07680 161 AEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 240

                       250
                ....*....|....*...
3HAI_C      259 AENSSYIHVYRELEQAIR 276
Cdd:cd07680 241 AESSSYAHVYRELEQTIR 258
 
Name Accession Description Interval E-value
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 19-276 0e+00

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: 499.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 98
Cdd:cd07680   1 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSK 178
Cdd:cd07680  81 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREANSK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      179 TEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 258
Cdd:cd07680 161 AEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 240

                       250
                ....*....|....*...
3HAI_C      259 AENSSYIHVYRELEQAIR 276
Cdd:cd07680 241 AESSSYAHVYRELEQTIR 258
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 17-101 6.67e-20

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: 82.39  E-value: 6.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C          17 DSFWEVG--NYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKV 94
Cdd:smart00055   1 MGFWSELddGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYGSLSKAWEVLLSETDAL 80


                   ....*..
3HAI_C          95 SELHQEV 101
Cdd:smart00055  81 AKQHLEL 87
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 25-100 1.40e-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: 73.07  E-value: 1.40e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3HAI_C         25 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKG-PQYGSLERAWGAIMTEADKVSELHQE 100
Cdd:pfam00611   2 FKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPeDDGGTLKKAWDELLTETEQLAKQHLK 78
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 124-225 7.46e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 36.74  E-value: 7.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      124 QIMGGFKETKEAEDGFRKAQKPWAKK----MKELEAAKKAYhlacKEEKLAMTREMNSKTEQSVTpEQQKKLQDKVDKCK 199
Cdd:COG2825  33 RILQESPEGKAAQKKLEKEFKKRQAElqklEKELQALQEKL----QKEAATLSEEERQKKERELQ-KKQQELQRKQQEAQ 107

                        90       100
                ....*....|....*....|....*..
3HAI_C      200 QDVQKTQEK-YEKVLEDVGKTTPQYME 225
Cdd:COG2825 108 QDLQKRQQElLQPILEKIQKAIKEVAK 134
 
Name Accession Description Interval E-value
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 19-276 0e+00

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: 499.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 98
Cdd:cd07680   1 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSK 178
Cdd:cd07680  81 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREANSK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      179 TEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 258
Cdd:cd07680 161 AEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 240

                       250
                ....*....|....*...
3HAI_C      259 AENSSYIHVYRELEQAIR 276
Cdd:cd07680 241 AESSSYAHVYRELEQTIR 258
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 19-276 3.13e-155

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: 434.11  E-value: 3.13e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 98
Cdd:cd07679   1 FWEVGNYKRTVKRIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKRWRQLVEKGPQYGTVEKAWCALMSEAEKVSELH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSK 178
Cdd:cd07679  81 LEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTACKEEKLATSREANSK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      179 TEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 258
Cdd:cd07679 161 ADPALNPEQLKKLQDKVEKCKQDVLKTKEKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDL 240

                       250
                ....*....|....*...
3HAI_C      259 AENSSYIHVYRELEQAIR 276
Cdd:cd07679 241 SNVASYKNIYRELEQSIK 258
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 19-276 3.54e-146

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: 411.32  E-value: 3.54e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 98
Cdd:cd07655   1 FWEVGNYKRTVKRIEDGHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKWRDLIEKGPEYGTLETAWKGLLSEAERLSELH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSK 178
Cdd:cd07655  81 LSIRDKLLNDVVEEVKTWQKENYHKSMMGGFKETKEAEDGFAKAQKPWAKLLKKVEKAKKAYHAACKAEKSAQKQENNAK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      179 TEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 258
Cdd:cd07655 161 SDTSLSPDQVKKLQDKVEKCKQEVSKTKDKYEKALEDLNKYNPRYMEDMEQVFDKCQEFEEKRLDFFKEILLSYHRHLDL 240

                       250
                ....*....|....*...
3HAI_C      259 AENSSYIHVYRELEQAIR 276
Cdd:cd07655 241 STNPSFKAIYRDLQQTII 258
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 19-275 2.62e-119

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: 343.07  E-value: 2.62e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELH 98
Cdd:cd07681   1 FWEAGNYRRTVKRIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARKWRGIVEKGPQYGTLEKAWHAFLTAAERLSEIH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSK 178
Cdd:cd07681  81 LELRENLVGEDSEKVRAWQKEAFHKQMIGGFRESKEAEEGFRKAQKPWVKKLKEVESSKKGYHAARKDERTAQTRETHAK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      179 TEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNL 258
Cdd:cd07681 161 ADSTVSQEQLRKLQDRVEKCTQEAEKAKEQYEKALEELNRYNPRYMEDMEQAFEICQEAERKRLCFFKEMLLDLHQHLDL 240

                       250
                ....*....|....*..
3HAI_C      259 AENSSYIHVYRELEQAI 275
Cdd:cd07681 241 SSSDSFHALYRDLHQTI 257
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 28-276 9.54e-25

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: 98.57  E-value: 9.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       28 TVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQ-----YGSLERAWGAIMTEADKVSELHQEVK 102
Cdd:cd07610   1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPEsgktsLGTSWNSLREETESAATVHEELSEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      103 NNLLNEDLEKVKNWQKDAyhkqimgGFKETKEAEDGFRKAQKPWAKKMKeleaakkayhlackeeklamtremnskteqs 182
Cdd:cd07610  81 SQLIREPLEKVKEDKEQA-------RKKELAEGEKLKKKLQELWAKLAK------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      183 vtpeqqkklqdkvdkckqdvqktqEKYEKVLEDVGKTTPQYMENMeQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENS 262
Cdd:cd07610 123 ------------------------KADEEYREQVEKLNPAQSEYE-EEKLNKIQAEQEREEERLEILKDNLKNYINAIKE 177

                       250
                ....*....|....
3HAI_C      263 SYIHVYRELEQAIR 276
Cdd:cd07610 178 IPQKIQQELEQSIN 191
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 17-101 6.67e-20

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: 82.39  E-value: 6.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C          17 DSFWEVG--NYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKV 94
Cdd:smart00055   1 MGFWSELddGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYGSLSKAWEVLLSETDAL 80


                   ....*..
3HAI_C          95 SELHQEV 101
Cdd:smart00055  81 AKQHLEL 87
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 25-249 6.80e-17

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: 78.29  E-value: 6.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       25 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKrwrqLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNN 104
Cdd:cd07647   7 FDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSK----SAGPGDEIGTLKSSWDSLRKETENVANAHIQLAQS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      105 LLNE--DLEKVKNWQKdayhkqimggfKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAmtREMNSKTEQS 182
Cdd:cd07647  83 LREEaeKLEEFREKQK-----------EERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKA--EQAYEKSSSG 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      183 VTPEQQKKLQDKVDKCKQDVQKTQEKYE---KVLEDVGKTTPQYMENMEQVFeqcQQFEEKRLVFLKEVL 249
Cdd:cd07647 150 AQPKEAEKLKKKAAQCKTSAEEADSAYKssiGCLEDARVEWESEHATACQVF---QNMEEERIKFLRNAL 216
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 25-100 1.40e-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: 73.07  E-value: 1.40e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3HAI_C         25 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKG-PQYGSLERAWGAIMTEADKVSELHQE 100
Cdd:pfam00611   2 FKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPeDDGGTLKKAWDELLTETEQLAKQHLK 78
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 31-249 3.31e-11

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: 61.93  E-value: 3.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       31 RIDDGHRLCNDLMNCVQERAKIEKAYgqqltdwAKRWRQLIEK---GPQYGSLERAWGAIMTEADKVSELHQEVKNNLLN 107
Cdd:cd07651  13 RIKDSLRTLEELRSFYKERASIEEEY-------AKRLEKLSRKslgGSEEGGLKNSLDTLRLETESMAKSHLKFAKQIRQ 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      108 EDLEKVKNWQkDAYHKQImggfketKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKeeklamtrEMNSKTEQSVTPEQ 187
Cdd:cd07651  86 DLEEKLAAFA-SSYTQKR-------KKIQSHMEKLLKKKQDQEKYLEKAREKYEADCS--------KINSYTLQSQLTWG 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3HAI_C      188 QK--KLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVL 249
Cdd:cd07651 150 KEleKNNAKLNKAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLKSNC 213
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 19-249 8.19e-10

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN 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. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization.


Pssm-ID: 153342 [Multi-domain]  Cd Length: 239  Bit Score: 58.16  E-value: 8.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       19 FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPqyGSLERAWGAIMTEADKVSELH 98
Cdd:cd07658   1 FMGQKGFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKLSKASKSVS--GTLSSAWTCVAEEMESEADIH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       99 QEVKNNLLNEDLEKVKNWQkDAYHKQImggfketKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKE-EKL--AMTREM 175
Cdd:cd07658  79 RNLGSALTEEAIKPLRQVL-DEQHKTR-------KPVENEVDKAAKLLTDWRSEQIKVKKKLHGLAREnEKLqdQVEDNK 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      176 NSKTEQS----------VTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFL 245
Cdd:cd07658 151 QSCTKQKmlnklkksaeVQDKEDEKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWESALRKGLNQYESLEEERLQHL 230


                ....
3HAI_C      246 KEVL 249
Cdd:cd07658 231 KHSL 234
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 25-249 6.05e-09

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: 55.74  E-value: 6.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       25 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEkgpqYGSLERAWGAIMTEADKVSELHQEVKNN 104
Cdd:cd07671   7 YEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTE----INTLKASFDQLKQQIENIGNSHIQLAGM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      105 LLNE--DLEKVKNWQKDayhkqimggfkETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAmtREMNSKTEQS 182
Cdd:cd07671  83 LREElkSLEEFRERQKE-----------QRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEA--EQTFERSSST 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3HAI_C      183 VTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVL 249
Cdd:cd07671 150 GNPKQSEKSQNKAKQCRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNAL 216
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 41-249 1.73e-06

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: 48.52  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       41 DLMNCVQERAKIEKAYGQQLTDWAKRWRQLiekgPQYGSLERAWGAIMTEADKVSELHQEVKNNLLnedlEKVKNWQKda 120
Cdd:cd07673  30 ELSDFIRERATIEEAYSRSMTKLAKSASNY----SQLGTFAPVWDVFKTSTEKLANCHLELVRKLQ----ELIKEVQK-- 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      121 YHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKE-EKLamtremnskteqsvtpEQQKKLQDKVDKCK 199
Cdd:cd07673 100 YGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEqERL----------------KKEGATQREIEKAA 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
3HAI_C      200 QDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVL 249
Cdd:cd07673 164 VKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEII 213
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 46-249 4.07e-06

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: 47.35  E-value: 4.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       46 VQERAKIEKAYGQQLTDWAKRWR----QLIEKGPQYGSLeRAWGAIMTEADKVSELHQEVKNNL-------LNEDLEKVK 114
Cdd:cd07676  28 VKERTEIELSYAKQLRNLSKKYQpkknSKEEEEYKYTSC-RAFLMTLNEMNDYAGQHEVISENLasqiiveLTRYVQELK 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      115 NWQKDAYHkqimggfketkeaeDGfRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDK 194
Cdd:cd07676 107 QERKSHFH--------------DG-RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQ 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
3HAI_C      195 VDKCKQDVQKTQEKYEKVLEDVGKTTPQ-YMENMEQVFEQCQQFEEKRLVFLKEVL 249
Cdd:cd07676 172 AQIRHQMAEDSKAEYSSYLQKFNKEQHEhYYTHIPNIFQKIQEMEERRIGRVGESM 227
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 22-249 1.15e-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: 45.71  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       22 VGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRwrqLIEKGPQYGSLERAWGAIMTEADKVSELHQEV 101
Cdd:cd07672   4 TGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKK---KPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      102 KNNLLNE--DLEKVKNWQK----------DAYHKQIMGGFKETKEaedgfrkaqkpwakkmkeleaAKKAYHLACKEEKL 169
Cdd:cd07672  81 AQTLRDEakKMEDFRERQKlarkkielimDAIHKQRAMQFKKTME---------------------SKKNYEQKCRDKDE 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      170 AmtREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVL 249
Cdd:cd07672 140 A--EQAVNRNANLVNVKQQEKLFAKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAV 217
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 46-304 2.70e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in 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: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 44.64  E-value: 2.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       46 VQERAKIEKAYGQQLTDWAKRWRQLIekgpQYGSLERAWGAIMTEADKVSELHQEVKNNLlnEDLekVKNWQKdaYHKQI 125
Cdd:cd07648  28 LRERATIEETYSKALNKLAKQASNSS----QLGTFAPLWLVLRVSTEKLSELHLQLVQKL--QEL--IKDVQK--YGEEQ 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      126 MGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKE-EKLamtremnsKTEQSVTPEqqkklqdkVDKCKQDVQK 204
Cdd:cd07648  98 HKKHKKVKEEESGTAEAVQAIQTTTAALQKAKEAYHARCLElERL--------RRENASPKE--------IEKAEAKLKK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      205 TQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNlaENSSYIH-VYRELEQAIRGADAQED 283
Cdd:cd07648 162 AQDEYKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVLS--ENHSAVGqVHEEFKRQVDELTVDKL 239

                       250       260
                ....*....|....*....|...
3HAI_C      284 LRWFRSTSGPGM--PMNwPQFEE 304
Cdd:cd07648 240 LRQFVESKGTGTekPEL-IEFEE 261
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 30-250 2.75e-05

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: 44.55  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       30 KRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYG-SLERAWGAIMTEADKVSELHQEVKNNLLNE 108
Cdd:cd07653  12 KHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKKKEEDEYSfSSVKAFRSILNEVNDIAGQHELIAENLNSN 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      109 DLEKVKNWQKDayHKQimggfkETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKE-EKLAMTREmnsKTEQ--SVTP 185
Cdd:cd07653  92 VCKELKTLISE--LRQ------ERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEaEKAKQKYE---KADAdmNLTK 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3HAI_C      186 EQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQ-YMENMEQVFEQCQQFEEKRLVFLKEVLL 250
Cdd:cd07653 161 ADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQhYSTDLPQIFDKLQELDEKRINRTVELLL 226
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 46-247 3.43e-03

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: 38.49  E-value: 3.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       46 VQERAKIEKAYGQQLTDWAKRW---RQLIEKGPQYGSLeRAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYh 122
Cdd:cd07675  28 VKERLEIEQNYAKQLRNLVKKYcpkRSSKDEEPRFTSC-LSFYNILNELNDYAGQREVVAEEMGHRVYGELMRYSHDLK- 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      123 kqimggfKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDV 202
Cdd:cd07675 106 -------GERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKSDVEKAKQQLNLRTHMA 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
3HAI_C      203 QKTQEKYEKVLEDV-GKTTPQYMENMEQVFEQCQQFEEKRLVFLKE 247
Cdd:cd07675 179 DESKNEYAAQLQNFnGEQHKHFYIVIPQIYKQLQEMDERRTVKLSE 224
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
 38-209 4.18e-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: 4.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C       38 LCNDLMNCVQERAKIEKAYGQQLTDWAKRW------RQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLE 111
Cdd:cd07654  20 LLEDIRTYSQKKAAIEREYGQALQKLASQFlkrewpGSGELKPEDDRSGYTVWGAWLEGLDAVAQSRQNRCEAYRRYISE 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      112 KVKNW--QKDayhkqimggfKETKEAEDGFRKAQKPWAKKMKELEAAKKAY-------HLACKEEKLAMTREMNSKTE-- 180
Cdd:cd07654 100 PAKTGrsAKE----------QQLKKCTEQLQRAQAEVQQTVRELSKSRKTYfereqvaHLAREKAADVQAREARSDLSif 169

                       170       180       190
                ....*....|....*....|....*....|.
3HAI_C      181 QSVTPEQQK--KLQDKVDKCKQDVQKTQEKY 209
Cdd:cd07654 170 QSRTSLQKAsvKLSARKAECSSKATAARNDY 200
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 124-225 7.46e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 36.74  E-value: 7.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HAI_C      124 QIMGGFKETKEAEDGFRKAQKPWAKK----MKELEAAKKAYhlacKEEKLAMTREMNSKTEQSVTpEQQKKLQDKVDKCK 199
Cdd:COG2825  33 RILQESPEGKAAQKKLEKEFKKRQAElqklEKELQALQEKL----QKEAATLSEEERQKKERELQ-KKQQELQRKQQEAQ 107

                        90       100
                ....*....|....*....|....*..
3HAI_C      200 QDVQKTQEK-YEKVLEDVGKTTPQYME 225
Cdd:COG2825 108 QDLQKRQQElLQPILEKIQKAIKEVAK 134
 
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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