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Conserved domains on  [gi|1907129074|ref|XP_036016926|]
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proline-serine-threonine phosphatase-interacting protein 2 isoform X2 [Mus musculus]

Protein Classification

BAR domain-containing protein( domain architecture ID 36964)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 15-247 3.25e-142

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


The actual alignment was detected with superfamily member cd07672:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 240  Bit Score: 401.25  E-value: 3.25e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  15 ILSTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07672     1 LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  95 AQTLREEARKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLF 174
Cdd:cd07672    81 AQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129074 175 VKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDE 247
Cdd:cd07672   161 AKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDE 233
 
Name Accession Description Interval E-value
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-247 3.25e-142

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: 401.25  E-value: 3.25e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  15 ILSTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07672     1 LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  95 AQTLREEARKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLF 174
Cdd:cd07672    81 AQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129074 175 VKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDE 247
Cdd:cd07672   161 AKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDE 233
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 20-93 2.48e-15

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: 69.99  E-value: 2.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRK----KPCGQSEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKflkkKKKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 10-94 9.30e-12

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


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 60.05  E-value: 9.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074   10 FWSTDilsTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPC---GQSEINTLKRALEVFKQQVDN 86
Cdd:smart00055   3 FWSEL---DDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAvrdTEPEYGSLSKAWEVLLSETDA 79


                   ....*...
gi 1907129074   87 VAQCHIQL 94
Cdd:smart00055  80 LAKQHLEL 87
PTZ00121 PTZ00121
MAEBL; Provisional
 36-204 3.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074   36 KEFEDFLK-ERASIEEKYGKDLLNLSRKkpcgqsEINTLKRALEVFKQQVDNVAQCHiQLAQTLREEARKMEEFREKQKL 114
Cdd:PTZ00121  1614 KAEEAKIKaEELKKAEEEKKKVEQLKKK------EAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEED 1686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  115 QRKKTEtimdaAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLFVKLATSKTAVEDSDKAYMLH 194
Cdd:PTZ00121  1687 EKKAAE-----ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761

                          170
                   ....*....|
gi 1907129074  195 INMLEKVRED 204
Cdd:PTZ00121  1762 LKKEEEKKAE 1771
 
Name Accession Description Interval E-value
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-247 3.25e-142

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: 401.25  E-value: 3.25e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  15 ILSTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07672     1 LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  95 AQTLREEARKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLF 174
Cdd:cd07672    81 AQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129074 175 VKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDE 247
Cdd:cd07672   161 AKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDE 233
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-253 1.00e-116

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: 336.37  E-value: 1.00e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  15 ILSTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGQsEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07647     1 FTSTTGFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGD-EIGTLKSSWDSLRKETENVANAHIQL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  95 AQTLREEARKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLF 174
Cdd:cd07647    80 AQSLREEAEKLEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSSGAQPKEAEKLK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129074 175 VKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDEHPSCMR 253
Cdd:cd07647   160 KKAAQCKTSAEEADSAYKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCNLGSMQCVKLDEMYEDVR 238
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 20-255 6.60e-77

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: 235.24  E-value: 6.60e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPcGQSEINTLKRALEVFKQQVDNVAQCHIQLAQTLR 99
Cdd:cd07671     6 GYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAG-GQTEINTLKASFDQLKQQIENIGNSHIQLAGMLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 100 EEARKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLFVKLAT 179
Cdd:cd07671    85 EELKSLEEFRERQKEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSSTGNPKQSEKSQNKAKQ 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129074 180 SKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDEHPSCMRTS 255
Cdd:cd07671   165 CRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCNHFSMQCVKDDELYEEVRTT 240
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 20-253 1.77e-33

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: 123.18  E-value: 1.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPcGQSEINTLKRALEVFKQQVDNVAQCHIQLAQTLR 99
Cdd:cd07651     6 GFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSL-GGSEEGGLKNSLDTLRLETESMAKSHLKFAKQIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 100 EEAR-KMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKdeaeQAVHRSANVANQRQQEKLFVKLA 178
Cdd:cd07651    85 QDLEeKLAAFASSYTQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEADCSKI----NSYTLQSQLTWGKELEKNNAKLN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907129074 179 TSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDEhpSCMR 253
Cdd:cd07651   161 KAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLKSNCWTFANNISTLCVDDDE--SCER 233
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 20-220 9.37e-19

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: 83.93  E-value: 9.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKdLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQLAQTLR 99
Cdd:cd07648     6 GFDVLYHNMKHGQIAVKELADFLRERATIEETYSK-ALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLVQKLQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 100 EEARKMEEFREKQKLQRKKTE----TIMDAAH--KQRNAQFKKamdAKKNYEQKCRDKDEAEQavhrsaNVANQRQQEKL 173
Cdd:cd07648    85 ELIKDVQKYGEEQHKKHKKVKeeesGTAEAVQaiQTTTAALQK---AKEAYHARCLELERLRR------ENASPKEIEKA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907129074 174 FVKLatsKTAVEDsdkaYMLHINMLEKVREDWQSEHIKACEVFEAQE 220
Cdd:cd07648   156 EAKL---KKAQDE----YKALVEKYNNIRADFETKMTDSCKRFQEIE 195
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 6-217 6.58e-16

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: 76.25  E-value: 6.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074   6 FKGNFWSTdilSTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSrKKPCGQSEINTLKRALEVFKQQVD 85
Cdd:cd07673     2 FLENFWGE---KNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLA-KSASNYSQLGTFAPVWDVFKTSTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  86 NVAQCHIQLAQTLREEARKMEEFREKQKLQRKKT-ETIMDAAHKQRNAQ--FKKAMDAKKNYEQKCRD-----KDEAEQA 157
Cdd:cd07673    78 KLANCHLELVRKLQELIKEVQKYGEEQVKSHKKTkEEVAGTLEAVQNIQsiTQALQKSKENYNAKCLEqerlkKEGATQR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907129074 158 VHRSANVANQRQQE--KLFV-KLATSKTAVE-----------DSDKAYMLHIN-MLEKVREDWQSEHIKACEVFE 217
Cdd:cd07673   158 EIEKAAVKSKKATEsyKLYVeKYALAKADFEqkmtetaqkfqDIEETHLIRIKeIIGSYSNSVKEIHIQIGQVHE 232
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 20-93 2.48e-15

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: 69.99  E-value: 2.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRK----KPCGQSEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKflkkKKKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 20-248 1.40e-14

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: 70.83  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCG-QSEINTLKRALEVFKQQVDNVAQCHIQLAQTL 98
Cdd:cd07610     1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKpESGKTSLGTSWNSLREETESAATVHEELSEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  99 REEARKMEEFREKQKLQRKKTETimdaahkqrnAQFKKAMDAKKNYEQKcrdkdeaeqavhrsanvanqrqqeklfvkla 178
Cdd:cd07610    81 SQLIREPLEKVKEDKEQARKKEL----------AEGEKLKKKLQELWAK------------------------------- 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 179 tsktAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNALWLHLNQLSQQCVANDEH 248
Cdd:cd07610   120 ----LAKKADEEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQE 185
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 10-94 9.30e-12

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


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 60.05  E-value: 9.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074   10 FWSTDilsTIGYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPC---GQSEINTLKRALEVFKQQVDN 86
Cdd:smart00055   3 FWSEL---DDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAvrdTEPEYGSLSKAWEVLLSETDA 79


                   ....*...
gi 1907129074   87 VAQCHIQL 94
Cdd:smart00055  80 LAKQHLEL 87
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 20-240 8.87e-11

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central 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: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 60.80  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGQSEiNTLKRALEVFKQQVDNVAQCHIQLAQTLR 99
Cdd:cd07649     6 GFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEE-GTLGEAWAQVKKSLADEAEVHLKFSSKLQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 100 EEARK-MEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKD-EAEQAVHRSANVANQRqqeklfVKL 177
Cdd:cd07649    85 SEVEKpLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKALLERQKDLEgKTQQLEIKLSNKTEED------IKK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129074 178 ATSKTAVEDSDkaYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNalwlHLNQLSQ 240
Cdd:cd07649   159 ARRKSTQAGDD--LMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQ----HLCQYTQ 215
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 20-220 1.23e-10

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 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: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 60.73  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGqSEINTLKRALEVFKQQVDNVAQCHIQLAQTLR 99
Cdd:cd07674     6 GFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNG-SPLGTFAPMWEVFRVSSDKLALCHLELMRKLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 100 EEARKMEEFREKQ-KLQRKKTETIMDAAHKQRNAQFKKAM--DAKKNYEQKCRDKDEAEQavhrsaNVANQRQQEKlfVK 176
Cdd:cd07674    85 DLIKDINRYGDEQvKIHKKTKEEAIGTLEAVQSLQVQSQHlqKSRENYHSKCVEQERLRR------EGVPQKELEK--AE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907129074 177 LATSKTAvedsdKAYMLHINMLEKVREDWQSEHIKACEVFEAQE 220
Cdd:cd07674   157 LKTKKAA-----ESLRGSVEKYNRARGDFEQKMLESAQKFQDIE 195
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-252 8.49e-10

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: 58.48  E-value: 8.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRK------KPCgqsEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07655     7 YKRTVKRIEDGHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKwrdlieKGP---EYGTLETAWKGLLSEAERLSELHLSI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  95 AQTLREEArkMEEFREKQK--------LQRKKTETIMDA---AHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVH--RS 161
Cdd:cd07655    84 RDKLLNDV--VEEVKTWQKenyhksmmGGFKETKEAEDGfakAQKPWAKLLKKVEKAKKAYHAACKAEKSAQKQENnaKS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 162 ANVANQRQQEKLFVKLATSKTAVEDSDKAYmlhinmlEKVREDWQSEHIK----ACEVFE---AQECERINFFRNALwlh 234
Cdd:cd07655   162 DTSLSPDQVKKLQDKVEKCKQEVSKTKDKY-------EKALEDLNKYNPRymedMEQVFDkcqEFEEKRLDFFKEIL--- 231

                         250
                  ....*....|....*...
gi 1907129074 235 lnQLSQQCVANDEHPSCM 252
Cdd:cd07655   232 --LSYHRHLDLSTNPSFK 247
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-231 7.35e-09

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: 55.46  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSR-------KKPcgqsEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:cd07679     7 YKRTVKRIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKrwrqlveKGP----QYGTVEKAWCALMSEAEKVSELHLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  94 LAQTL-REEARKMEEFRE----KQKL----QRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRdkdEAEQAVHRSAN- 163
Cdd:cd07679    83 VKASLmNEDFEKIKNWQKeafhKQMMggfkETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTACK---EEKLATSREANs 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907129074 164 ----VANQRQQEKLFVKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNAL 231
Cdd:cd07679   160 kadpALNPEQLKKLQDKVEKCKQDVLKTKEKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVL 231
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 20-231 1.97e-08

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: 53.92  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  20 GYDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRK--KPCgQSEINTLKRALEVFKQQVDNVAQCHIQLAQT 97
Cdd:cd07658     6 GFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKlsKAS-KSVSGTLSSAWTCVAEEMESEADIHRNLGSA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  98 LREEARK-MEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHrsaNVANQRQQEKLFVK 176
Cdd:cd07658    85 LTEEAIKpLRQVLDEQHKTRKPVENEVDKAAKLLTDWRSEQIKVKKKLHGLARENEKLQDQVE---DNKQSCTKQKMLNK 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907129074 177 LATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNAL 231
Cdd:cd07658   162 LKKSAEVQDKEDEKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWESALRKGL 216
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 21-200 2.52e-08

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: 53.80  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLS-----RKKPCGQSEINTLKrALEVFKQQVDNVAQCHIQLA 95
Cdd:cd07653     7 FDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVkkylpKKKEEDEYSFSSVK-AFRSILNEVNDIAGQHELIA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  96 QTLREEA-RKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVAN--QRQQEK 172
Cdd:cd07653    86 ENLNSNVcKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNltKADVEK 165

                         170       180
                  ....*....|....*....|....*...
gi 1907129074 173 LfvkLATSKTAVEDSDKAYMLHINMLEK 200
Cdd:cd07653   166 A---KANANLKTQAAEEAKNEYAAQLQK 190
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-245 9.89e-08

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: 52.36  E-value: 9.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSR-------KKPcgqsEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:cd07680     7 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKrwrqlieKGP----QYGSLERAWGAIMTEADKVSELHQE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  94 LAQTLREEarKMEEFREKQKlqrkktetimDAAHKQRNAQFKKAMD-------AKKNYEQKCRDKDEAEQAVH------- 159
Cdd:cd07680    83 VKNNLLNE--DLEKVKNWQK----------DAYHKQIMGGFKETKEaedgfrkAQKPWAKKMKELEAAKKAYHlackeek 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074 160 ----RSANVANQR-----QQEKLFVKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNA 230
Cdd:cd07680   151 lamtREANSKAEQsvtpeQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEV 230

                         250
                  ....*....|....*...
gi 1907129074 231 LW---LHLNQLSQQCVAN 245
Cdd:cd07680   231 LLdikRHLNLAESSSYAH 248
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 21-210 5.90e-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: 46.96  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRK---KPCGQSEIN---TLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07676     7 FDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKyqpKKNSKEEEEykyTSCRAFLMTLNEMNDYAGQHEVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  95 AQTLREEArKMEEFREKQKLQRKKTETIMDAAHKQRNAQ--FKKAMDAKKNYEQKCRDKDEAEQAVHR--------SANV 164
Cdd:cd07676    87 SENLASQI-IVELTRYVQELKQERKSHFHDGRKAQQHIEtcWKQLESSKRRFERDCKEADRAQQYFEKmdadinvtKADV 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129074 165 ANQRQQEKLFVKLAtsktavEDSDKAYMLHINMLEKVREDWQSEHI 210
Cdd:cd07676   166 EKARQQAQIRHQMA------EDSKAEYSSYLQKFNKEQHEHYYTHI 205
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-231 1.87e-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: 42.23  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCG---QSEINTLKRALEVFKQQVDNVAQCHIQLAQT 97
Cdd:cd07681     7 YRRTVKRIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARKWRGIvekGPQYGTLEKAWHAFLTAAERLSEIHLELREN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  98 LR-EEARKMEEFRE----KQKL----QRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAE-QAVHRSANVA-N 166
Cdd:cd07681    87 LVgEDSEKVRAWQKeafhKQMIggfrESKEAEEGFRKAQKPWVKKLKEVESSKKGYHAARKDERTAQtRETHAKADSTvS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907129074 167 QRQQEKLFVKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECERINFFRNAL 231
Cdd:cd07681   167 QEQLRKLQDRVEKCTQEAEKAKEQYEKALEELNRYNPRYMEDMEQAFEICQEAERKRLCFFKEML 231
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 34-202 3.07e-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: 41.56  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  34 NCKEFEDFLKERASIEEKYGKDLLNLSRkkpcgqSEINTLKRA---LEVFKQQVDNVAQCHIQLAQT------------- 97
Cdd:cd07652    20 SAKEFATFLKKRAAIEEEHARGLKKLAR------TTLDTYKRPdhkQGSFSNAYHSSLEFHEKLADNglrfakalnemsd 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  98 -LREEARKMEEFREKQKLQRKKTE-TIMDAAHKQRNAQFKkamdakknYEQKCRDKDeaeqavhrsaNVANQRQQEKLFV 175
Cdd:cd07652    94 eLSSLAKTVEKSRKSIKETGKRAEkKVQDAEAAAEKAKAR--------YDSLADDLE----------RVKTGDPGKKLKF 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907129074 176 KLATSKTA----------VEDSDKAYMLHINMLEKVR 202
Cdd:cd07652   156 GLKGNKSAaqhedellrkVQAADQDYASKVNAAQALR 192
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 21-208 3.65e-04

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: 41.57  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  21 YDSIIQHLNNGRKNCKEFEDFLKERASIEEKYGKDLLNLSRKKPCGQSEINTLKR------------ALEVFKQQVDNVA 88
Cdd:cd07675     7 FDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRNLVKKYCPKRSSKDEEPRftsclsfynilnELNDYAGQREVVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  89 Q--CHIQLAQTLReEARKMEEFREKQKLQRKKTETIMDAAHKQRNaqfkkamDAKKNYEQKCRDKDEAEQAVHRSANVAN 166
Cdd:cd07675    87 EemGHRVYGELMR-YSHDLKGERKMHLQEGRKAQQYLDMCWKQMD-------NSKKKFERECREAEKAQQSYERLDNDTN 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907129074 167 qrqqeklfvklaTSKTAVEDSDKAYMLHINMLEKVREDWQSE 208
Cdd:cd07675   159 ------------ATKSDVEKAKQQLNLRTHMADESKNEYAAQ 188
PTZ00121 PTZ00121
MAEBL; Provisional
 36-204 3.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074   36 KEFEDFLK-ERASIEEKYGKDLLNLSRKkpcgqsEINTLKRALEVFKQQVDNVAQCHiQLAQTLREEARKMEEFREKQKL 114
Cdd:PTZ00121  1614 KAEEAKIKaEELKKAEEEKKKVEQLKKK------EAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEED 1686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  115 QRKKTEtimdaAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLFVKLATSKTAVEDSDKAYMLH 194
Cdd:PTZ00121  1687 EKKAAE-----ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761

                          170
                   ....*....|
gi 1907129074  195 INMLEKVRED 204
Cdd:PTZ00121  1762 LKKEEEKKAE 1771
PTZ00121 PTZ00121
MAEBL; Provisional
 39-230 5.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 5.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074   39 EDFLKERASIEE-KYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQLAQTLREEARKMEEFREKQklQRK 117
Cdd:PTZ00121  1039 DDVLKEKDIIDEdIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARK 1116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  118 KTETIMDAAHKQRNAQFKKAMDAKKNYEQKcrdKDEAEQAVHRSANVANQRQQEKlfVKLATSKTAVEDSDKAymlhinm 197
Cdd:PTZ00121  1117 AEEAKKKAEDARKAEEARKAEDARKAEEAR---KAEDAKRVEIARKAEDARKAEE--ARKAEDAKKAEAARKA------- 1184

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907129074  198 lEKVRedwqsehiKACEVFEAQECERINFFRNA 230
Cdd:PTZ00121  1185 -EEVR--------KAEELRKAEDARKAEAARKA 1208
PTZ00121 PTZ00121
MAEBL; Provisional
 100-230 6.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  100 EEARKMEEFREKQKLQRKKTETIMDAAHKQRNAQFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVANQRQQEKLfvKLAT 179
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA--KKAE 1531

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907129074  180 SKTAVEDSDKAYMLH-INMLEKVREDWQSEHIKACEVFEAQECERINFFRNA 230
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
PTZ00121 PTZ00121
MAEBL; Provisional
 100-223 9.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 9.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129074  100 EEARKMEEFREKQKLQRKKTETIMDAAHKQRNA-------QFKKAMDAKKNYEQKCRDKDEAEQAVHRSANVanqRQQEK 172
Cdd:PTZ00121  1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeakkaeEAKKADEAKKAEEAKKADEAKKAEEKKKADEL---KKAEE 1556

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907129074  173 lfVKLATSKTAVEDSDKAYMLHINMLEKVREDWQSEHIKACEVFEAQECER 223
Cdd:PTZ00121  1557 --LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
 
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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