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Conserved domains on  [gi|767985668|ref|XP_011520469|]
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proline-serine-threonine phosphatase-interacting protein 1 isoform X9 [Homo sapiens]

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 ...
 16-276 1.16e-137

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 cd07671:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 242  Bit Score: 389.70  E-value: 1.16e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  16 FTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLA 95
Cdd:cd07671    1 FTLNTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  96 LTLREELRSLEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQ 175
Cdd:cd07671   81 GMLREELKSLEEFRERQKEQRKK-------------------YEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSN 255
Cdd:cd07671  142 TFERSSSTGNPKQSEKSQNKAKQCRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCN 221

                        250       260
                 ....*....|....*....|.
gi 767985668 256 QLSMQCVKDDELYEEVRLTLE 276
Cdd:cd07671  222 HFSMQCVKDDELYEEVRTTLE 242
 
Name Accession Description Interval E-value
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 16-276 1.16e-137

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: 389.70  E-value: 1.16e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  16 FTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLA 95
Cdd:cd07671    1 FTLNTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  96 LTLREELRSLEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQ 175
Cdd:cd07671   81 GMLREELKSLEEFRERQKEQRKK-------------------YEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSN 255
Cdd:cd07671  142 TFERSSSTGNPKQSEKSQNKAKQCRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCN 221

                        250       260
                 ....*....|....*....|.
gi 767985668 256 QLSMQCVKDDELYEEVRLTLE 276
Cdd:cd07671  222 HFSMQCVKDDELYEEVRTTLE 242
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 12-94 3.48e-16

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: 72.37  E-value: 3.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668    12 WCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARK----AGGQTEINSLRASFDSLKQQMENV 87
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKlravRDTEPEYGSLSKAWEVLLSETDAL 80


                   ....*..
gi 767985668    88 GSSHIQL 94
Cdd:smart00055  81 AKQHLEL 87
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 21-93 7.17e-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: 68.45  E-value: 7.17e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767985668   21 GYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQ-----TEINSLRASFDSLKQQMENVGSSHIQ 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKkkkpeDDGGTLKKAWDELLTETEQLAKQHLK 78
PTZ00121 PTZ00121
MAEBL; Provisional
 45-236 3.87e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668   45 QRAQAEERYGKELVQIARKAGGQTEINSLRASfDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKGMAVPR 124
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  125 QSD----CMEVKSPSWEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCK 200
Cdd:PTZ00121 1697 EAEeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767985668  201 DSATEAERVYRQSiaqlEKVRAEWEQEHRTTCEAFQ 236
Cdd:PTZ00121 1777 KEAVIEEELDEED----EKRRMEVDKKIKDIFDNFA 1808
 
Name Accession Description Interval E-value
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 16-276 1.16e-137

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: 389.70  E-value: 1.16e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  16 FTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLA 95
Cdd:cd07671    1 FTLNTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  96 LTLREELRSLEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQ 175
Cdd:cd07671   81 GMLREELKSLEEFRERQKEQRKK-------------------YEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSN 255
Cdd:cd07671  142 TFERSSSTGNPKQSEKSQNKAKQCRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCN 221

                        250       260
                 ....*....|....*....|.
gi 767985668 256 QLSMQCVKDDELYEEVRLTLE 276
Cdd:cd07671  222 HFSMQCVKDDELYEEVRTTLE 242
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 16-273 2.38e-117

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: 337.91  E-value: 2.38e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  16 FTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLA 95
Cdd:cd07647    1 FTSTTGFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIGTLKSSWDSLRKETENVANAHIQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  96 LTLREELRSLEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQ 175
Cdd:cd07647   81 QSLREEAEKLEEFREKQKEERKK-------------------TEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSN 255
Cdd:cd07647  142 AYEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCN 221

                        250
                 ....*....|....*...
gi 767985668 256 QLSMQCVKDDELYEEVRL 273
Cdd:cd07647  222 LGSMQCVKLDEMYEDVRK 239
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 17-272 1.43e-79

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: 242.16  E-value: 1.43e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  17 TAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKA-GGQTEINSLRASFDSLKQQMENVGSSHIQLA 95
Cdd:cd07672    2 TSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKpCGQTEINTLKRSLDVFKQQIDNVGQSHIQLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  96 LTLREELRSLEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQ 175
Cdd:cd07672   82 QTLRDEAKKMEDFRERQKLARKK-------------------IELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQ 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSN 255
Cdd:cd07672  143 AVNRNANLVNVKQQEKLFAKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVN 222

                        250
                 ....*....|....*..
gi 767985668 256 QLSMQCVKDDELYEEVR 272
Cdd:cd07672  223 QLSQQCVTSDEMYEEVR 239
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 21-273 3.55e-28

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: 108.93  E-value: 3.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  21 GYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLRE 100
Cdd:cd07651    6 GFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHLKFAKQIRQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 101 ELRS-LEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDAddaeQAFER 179
Cdd:cd07651   86 DLEEkLAAFASSYTQKRKK-------------------IQSHMEKLLKKKQDQEKYLEKAREKYEADCSKI----NSYTL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 180 ISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSM 259
Cdd:cd07651  143 QSQLTWGKELEKNNAKLNKAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLKSNCWTFANNIST 222

                        250
                 ....*....|....
gi 767985668 260 QCVKDDELYEEVRL 273
Cdd:cd07651  223 LCVDDDESCERIRS 236
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 21-273 9.31e-28

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: 106.65  E-value: 9.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  21 GYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTE--INSLRASFDSLKQQMENVGSSHIQLALTL 98
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPEsgKTSLGTSWNSLREETESAATVHEELSEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  99 REELRSLEEFRERQKEQRKKgmavprqsdcmevkspswEYEAVMDRVQKSKLSLYKKAMEskktyeqkcrdaddaeqafe 178
Cdd:cd07610   81 SQLIREPLEKVKEDKEQARK------------------KELAEGEKLKKKLQELWAKLAK-------------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 179 risanghqkqveksqnkarqckdsatEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLS 258
Cdd:cd07610  123 --------------------------KADEEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIK 176

                        250
                 ....*....|....*
gi 767985668 259 MQCVKDDELYEEVRL 273
Cdd:cd07610  177 EIPQKIQQELEQSIN 191
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 19-299 2.50e-24

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: 99.34  E-value: 2.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  19 HTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTL 98
Cdd:cd07648    4 NNGFDVLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLVQKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  99 REELRSLEEFRERQKEQRKKgmavprqsdcmeVKSP-SWEYEAVMdRVQKSKLSLYKkameSKKTYEQKCRDADDAEQaf 177
Cdd:cd07648   84 QELIKDVQKYGEEQHKKHKK------------VKEEeSGTAEAVQ-AIQTTTAALQK----AKEAYHARCLELERLRR-- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 178 erisANGHQKQVEKSQNKARQCKDSateaervYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQL 257
Cdd:cd07648  145 ----ENASPKEIEKAEAKLKKAQDE-------YKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVL 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767985668 258 SMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPG 299
Cdd:cd07648  214 SENHSAVGQVHEEFKRQVDELTVDKLLRQFVESKGTGTEKPE 255
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 7-302 8.97e-20

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: 87.04  E-value: 8.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668   7 FKDAFWCRDftaHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMEN 86
Cdd:cd07673    2 FLENFWGEK---NSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  87 VGSSHIQLALTLREELRSLEEFRERQKEQRKKGMAvprqsdcmevkspswEYEAVMDRVQKSKlSLYKKAMESKKTYEQK 166
Cdd:cd07673   79 LANCHLELVRKLQELIKEVQKYGEEQVKSHKKTKE---------------EVAGTLEAVQNIQ-SITQALQKSKENYNAK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 167 CrdaddAEQafERISANG-HQKQVEKSQNKARQCKDSateaervYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTI 245
Cdd:cd07673  143 C-----LEQ--ERLKKEGaTQREIEKAAVKSKKATES-------YKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIR 208

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767985668 246 LRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPGSLD 302
Cdd:cd07673  209 IKEIIGSYSNSVKEIHIQIGQVHEEFINNMANTTVESLIQKFAESKGTGKERPGPIE 265
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 12-94 3.48e-16

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: 72.37  E-value: 3.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668    12 WCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARK----AGGQTEINSLRASFDSLKQQMENV 87
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKlravRDTEPEYGSLSKAWEVLLSETDAL 80


                   ....*..
gi 767985668    88 GSSHIQL 94
Cdd:smart00055  81 AKQHLEL 87
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 21-302 5.90e-15

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: 73.44  E-value: 5.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  21 GYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLRE 100
Cdd:cd07674    6 GFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELMRKLND 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 101 ELRSLEEFRERQKEQRKKgmavprqsdCMEvkspswEYEAVMDRVQKskLSLYKKAME-SKKTYEQKCRDAddaeqafER 179
Cdd:cd07674   86 LIKDINRYGDEQVKIHKK---------TKE------EAIGTLEAVQS--LQVQSQHLQkSRENYHSKCVEQ-------ER 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 180 ISANGH-QKQVEKSQNKARQCKDSateaervYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLS 258
Cdd:cd07674  142 LRREGVpQKELEKAELKTKKAAES-------LRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVE 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 767985668 259 MQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPGSLD 302
Cdd:cd07674  215 DTHVQIGQVHEEFKQNVENVGVENLIRKFAESKGTGKERPGPVG 258
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 21-93 7.17e-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: 68.45  E-value: 7.17e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767985668   21 GYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQ-----TEINSLRASFDSLKQQMENVGSSHIQ 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKkkkpeDDGGTLKKAWDELLTETEQLAKQHLK 78
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 17-250 1.22e-13

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: 69.27  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  17 TAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLAL 96
Cdd:cd07649    2 TTVTGFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  97 TLREEL-RSLEEFRERQKEQRKKgmavprqsdcmevkspsweYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQ 175
Cdd:cd07649   82 KLQSEVeKPLLNFRENFKKDMKK-------------------LDHHIADLRKQLASRYAAVEKARKALLERQKDLEGKTQ 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSiaqlekvRAEWEQEHRTTCEAFQLQEFDRLTILRNAL 250
Cdd:cd07649  143 QLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQA-------QSKWFEEMVTTSLELERLEVERIEMIRQHL 210
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 22-250 1.85e-10

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: 60.44  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  22 YEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTE----INSLRASFDSLKQQMENVGSSHIQLALT 97
Cdd:cd07680    7 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEkgpqYGSLERAWGAIMTEADKVSELHQEVKNN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  98 LREElrSLEEFRERQKEQRKKGMavprqsdcMEVKSPSWEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDA--EQ 175
Cdd:cd07680   87 LLNE--DLEKVKNWQKDAYHKQI--------MGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAmtRE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNAL 250
Cdd:cd07680  157 ANSKAEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVL 231
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 22-250 5.54e-10

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: 58.92  E-value: 5.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  22 YEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTE----INSLRASFDSLKQQMENVGSSHIQLALT 97
Cdd:cd07679    7 YKRTVKRIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKRWRQLVEkgpqYGTVEKAWCALMSEAEKVSELHLEVKAS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  98 LREElrSLEEFRERQKEQRKKGMavprqsdcMEVKSPSWEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDA--EQ 175
Cdd:cd07679   87 LMNE--DFEKIKNWQKEAFHKQM--------MGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTACKEEKLAtsRE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985668 176 AFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNAL 250
Cdd:cd07679  157 ANSKADPALNPEQLKKLQDKVEKCKQDVLKTKEKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVL 231
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 27-250 9.79e-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: 58.09  E-value: 9.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  27 QRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQT----EINSLRASFDSLKQQMENVGSSHIQLALTLREEl 102
Cdd:cd07655   12 KRIEDGHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKWRDLIekgpEYGTLETAWKGLLSEAERLSELHLSIRDKLLND- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 103 rSLEEFRERQKEQ-RKKGMAVPRqsdcmEVKspswEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAfERIS 181
Cdd:cd07655   91 -VVEEVKTWQKENyHKSMMGGFK-----ETK----EAEDGFAKAQKPWAKLLKKVEKAKKAYHAACKAEKSAQKQ-ENNA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767985668 182 A---NGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNAL 250
Cdd:cd07655  160 KsdtSLSPDQVKKLQDKVEKCKQEVSKTKDKYEKALEDLNKYNPRYMEDMEQVFDKCQEFEEKRLDFFKEIL 231
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 16-250 3.65e-09

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: 56.24  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  16 FTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKA--GGQTEINSLRASFDSLKQQMENVGSSHIQ 93
Cdd:cd07658    1 FMGQKGFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKLskASKSVSGTLSSAWTCVAEEMESEADIHRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  94 LALTLREELrsLEEFRERQKEQRKkgmavPRQSDCMEVKSPSWEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDA 173
Cdd:cd07658   81 LGSALTEEA--IKPLRQVLDEQHK-----TRKPVENEVDKAAKLLTDWRSEQIKVKKKLHGLARENEKLQDQVEDNKQSC 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 174 EQAFERI----SANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNA 249
Cdd:cd07658  154 TKQKMLNklkkSAEVQDKEDEKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWESALRKGLNQYESLEEERLQHLKHS 233


                 .
gi 767985668 250 L 250
Cdd:cd07658  234 L 234
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 22-250 1.50e-06

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: 48.78  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  22 YEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREE 101
Cdd:cd07681    7 YRRTVKRIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARKWRGIVEKGPQYGTLEKAWHAFLTAAERLSEIHLELREN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 102 L--RSLEEFRERQKEQRKKGMAVPRQSdcmevkspSWEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFER 179
Cdd:cd07681   87 LvgEDSEKVRAWQKEAFHKQMIGGFRE--------SKEAEEGFRKAQKPWVKKLKEVESSKKGYHAARKDERTAQTRETH 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767985668 180 ISANG--HQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNAL 250
Cdd:cd07681  159 AKADStvSQEQLRKLQDRVEKCTQEAEKAKEQYEKALEELNRYNPRYMEDMEQAFEICQEAERKRLCFFKEML 231
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 42-247 3.10e-06

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: 47.63  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  42 LLRQRAQAEERYGKELVQIA------RKAGGQTEINSLRAsFDSLKQQMENVGSSHIQLALTLREE-LRSLEEFRERQKE 114
Cdd:cd07653   27 FVKERAAIEQEYAKKLRKLVkkylpkKKEEDEYSFSSVKA-FRSILNEVNDIAGQHELIAENLNSNvCKELKTLISELRQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 115 QRKKgmavprqsDCMEVKSPSWEYEAVMDRVQKSKlslykkameskKTYEQKCRDADDAEQAFERISANGH--QKQVEKS 192
Cdd:cd07653  106 ERKK--------HLSEGSKLQQKLESSIKQLEKSK-----------KAYEKAFKEAEKAKQKYEKADADMNltKADVEKA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767985668 193 QNKARQCKDSATEAERVYrqsIAQLEKVRAEWEQEHRTTCEAF--QLQEFDRLTILR 247
Cdd:cd07653  167 KANANLKTQAAEEAKNEY---AAQLQKFNKEQRQHYSTDLPQIfdKLQELDEKRINR 220
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 153-241 1.55e-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: 39.65  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668 153 YKKAMESKKTYEQKCRDADDAEQAFERI--SANGHQKQVEKSQNKARQCKDSATEAERVYrqsIAQLEKVRAE-WEQEHR 229
Cdd:cd07675  126 WKQMDNSKKKFERECREAEKAQQSYERLdnDTNATKSDVEKAKQQLNLRTHMADESKNEY---AAQLQNFNGEqHKHFYI 202

                         90
                 ....*....|...
gi 767985668 230 TTCEAF-QLQEFD 241
Cdd:cd07675  203 VIPQIYkQLQEMD 215
PTZ00121 PTZ00121
MAEBL; Provisional
 45-236 3.87e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668   45 QRAQAEERYGKELVQIARKAGGQTEINSLRASfDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKGMAVPR 124
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985668  125 QSD----CMEVKSPSWEYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCK 200
Cdd:PTZ00121 1697 EAEeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767985668  201 DSATEAERVYRQSiaqlEKVRAEWEQEHRTTCEAFQ 236
Cdd:PTZ00121 1777 KEAVIEEELDEED----EKRRMEVDKKIKDIFDNFA 1808
 
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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