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Conserved domains on  [gi|767937894|ref|XP_011536002|]
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F-BAR and double SH3 domains protein 1 isoform X5 [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 ...
 16-275 2.55e-139

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 cd07678:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 263  Bit Score: 401.31  E-value: 2.55e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  16 LRFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSG---EMDSRGRTVFGAWRCLLDA 92
Cdd:cd07678    1 LRFLEQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGnetEMDRSVRTVWGAWREGTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  93 TVAGGQTRLQASDRYRDLAGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARL 172
Cdd:cd07678   81 TGQGRVTRLEAYRRLRDEAGKTGRSAKEQVLKKSTEQLQKAQAELLETVKELSKSKKLYGQLERVSEVAKEKAADVEARL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 173 NRSDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTSL 252
Cdd:cd07678  161 NKSDHGIFHSKASLQKLSAKFSAQSAEYSQQLQAARNEYLLNLVAANAHLDHYYQEELPAIMKALDGDLYERLRDPLTSL 240

                        250       260
                 ....*....|....*....|...
gi 767937894 253 SHTELEAAEVILEHAHRGEQTTS 275
Cdd:cd07678  241 SHTELEACEVTQEHFHRIEQATS 263
 
Name Accession Description Interval E-value
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 16-275 2.55e-139

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


Pssm-ID: 153362 [Multi-domain]  Cd Length: 263  Bit Score: 401.31  E-value: 2.55e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  16 LRFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSG---EMDSRGRTVFGAWRCLLDA 92
Cdd:cd07678    1 LRFLEQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGnetEMDRSVRTVWGAWREGTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  93 TVAGGQTRLQASDRYRDLAGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARL 172
Cdd:cd07678   81 TGQGRVTRLEAYRRLRDEAGKTGRSAKEQVLKKSTEQLQKAQAELLETVKELSKSKKLYGQLERVSEVAKEKAADVEARL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 173 NRSDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTSL 252
Cdd:cd07678  161 NKSDHGIFHSKASLQKLSAKFSAQSAEYSQQLQAARNEYLLNLVAANAHLDHYYQEELPAIMKALDGDLYERLRDPLTSL 240

                        250       260
                 ....*....|....*....|...
gi 767937894 253 SHTELEAAEVILEHAHRGEQTTS 275
Cdd:cd07678  241 SHTELEACEVTQEHFHRIEQATS 263
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 21-102 4.59e-11

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: 58.82  E-value: 4.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894   21 QLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKreghRSGEMDSRGRTVFGAWRCLLDATVAGGQTR 100
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLK----KKKKPEDDGGTLKKAWDELLTETEQLAKQH 76


                  ..
gi 767937894  101 LQ 102
Cdd:pfam00611  77 LK 78
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 20-102 1.15e-06

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: 46.57  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894    20 EQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGpflKREGHRSGEMdsRGRTVFGAWRCLLDATVAGGQT 99
Cdd:smart00055   9 DGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK---KLRAVRDTEP--EYGSLSKAWEVLLSETDALAKQ 83


                   ...
gi 767937894   100 RLQ 102
Cdd:smart00055  84 HLE 86
 
Name Accession Description Interval E-value
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 16-275 2.55e-139

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


Pssm-ID: 153362 [Multi-domain]  Cd Length: 263  Bit Score: 401.31  E-value: 2.55e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  16 LRFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSG---EMDSRGRTVFGAWRCLLDA 92
Cdd:cd07678    1 LRFLEQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGnetEMDRSVRTVWGAWREGTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  93 TVAGGQTRLQASDRYRDLAGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARL 172
Cdd:cd07678   81 TGQGRVTRLEAYRRLRDEAGKTGRSAKEQVLKKSTEQLQKAQAELLETVKELSKSKKLYGQLERVSEVAKEKAADVEARL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 173 NRSDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTSL 252
Cdd:cd07678  161 NKSDHGIFHSKASLQKLSAKFSAQSAEYSQQLQAARNEYLLNLVAANAHLDHYYQEELPAIMKALDGDLYERLRDPLTSL 240

                        250       260
                 ....*....|....*....|...
gi 767937894 253 SHTELEAAEVILEHAHRGEQTTS 275
Cdd:cd07678  241 SHTELEACEVTQEHFHRIEQATS 263
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
 16-275 7.77e-126

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


Pssm-ID: 153338 [Multi-domain]  Cd Length: 264  Bit Score: 366.91  E-value: 7.77e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  16 LRFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSG----EMDSRGRTVFGAWRCLLD 91
Cdd:cd07654    1 LRHLEQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLKREWPGSGelkpEDDRSGYTVWGAWLEGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  92 ATVAGGQTRLQASDRYRDLAGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQAR 171
Cdd:cd07654   81 AVAQSRQNRCEAYRRYISEPAKTGRSAKEQQLKKCTEQLQRAQAEVQQTVRELSKSRKTYFEREQVAHLAREKAADVQAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 172 LNRSDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTS 251
Cdd:cd07654  161 EARSDLSIFQSRTSLQKASVKLSARKAECSSKATAARNDYLLNLAATNAHQDRYYQTDLPAIIKALDGELYDHLKDFLIS 240

                        250       260
                 ....*....|....*....|....
gi 767937894 252 LSHTELEAAEVILEHAHRGEQTTS 275
Cdd:cd07654  241 LSHTELETAQVIQETFQRLLETSS 264
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 20-263 1.17e-48

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


Pssm-ID: 153361 [Multi-domain]  Cd Length: 260  Bit Score: 168.00  E-value: 1.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  20 EQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREgHRSGEMDSRG--RTVFGAWRCLLDATVAGG 97
Cdd:cd07677    5 EQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLKSD-WRGMKADERAdyRSMYTVWKSFLEGTMQVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  98 QTRLQASDRYRDL---AGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAaDVQARlnr 174
Cdd:cd07677   84 QSRINICENYKNLisePARTVRLYKEQQLKRCVDQLTKIQAELQETVKDLAKGKKKYFETEQMAHAVREKA-DIEAK--- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 175 SDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTSLSH 254
Cdd:cd07677  160 SKLSLFQSRISLQKASVKLKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKALDGNVYDHLKDYLMAFSR 239


                 ....*....
gi 767937894 255 TELEAAEVI 263
Cdd:cd07677  240 TELETCQAV 248
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 17-234 5.23e-12

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


Pssm-ID: 153340 [Multi-domain]  Cd Length: 241  Bit Score: 65.81  E-value: 5.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  17 RFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGH-RSGEMDSRGRTVFGAWRCLLDatva 95
Cdd:cd07656    2 QLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNeKSKREDWSLLSPVNCWNTLLV---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  96 ggQTRlqasDRYRDLAGGTGRSAKEQVLRKGT--ENLQR-----------AQAEVLQSVRELSRSRKLYGQR--ERVWAL 160
Cdd:cd07656   78 --QTK----QESRDHSTLSDIYSNNLVQRLGQmsEDLQRiskkcreigsqLHDELLRVLNELQTAMKTYHTYhaESKSAE 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767937894 161 AQEKAADVQARLNRSDHGIFHSRTSLQKLSTKL-SAQSAQYSQ-QLQA--ARNEYLLNLVATNAHLDHYYQEELPALL 234
Cdd:cd07656  152 RKLKEAEKQEEKQEQSPEKKLERSRSSKKIEKEvEKRQAKYSEaKLKCtkARNEYLLNLAAANATIHKYFVQDLSDLI 229
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 21-102 4.59e-11

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: 58.82  E-value: 4.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894   21 QLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKreghRSGEMDSRGRTVFGAWRCLLDATVAGGQTR 100
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLK----KKKKPEDDGGTLKKAWDELLTETEQLAKQH 76


                  ..
gi 767937894  101 LQ 102
Cdd:pfam00611  77 LK 78
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 17-234 6.86e-11

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating 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. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP1, also called Rho GTPase-Activating Protein 13 (ARHGAP13), is a Cdc42- and RhoA-specific GAP and is expressed later in the development of CNS (central nervous system) tissues. It is an important downstream signaling molecule of Robo1. srGAP1 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153367 [Multi-domain]  Cd Length: 253  Bit Score: 62.39  E-value: 6.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  17 RFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKR----EGHRSGEMDSRGRTVFGAWRCLLDA 92
Cdd:cd07683    2 QLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAKtrstKDHQQYKKDQNLLSPVNCWYLLLNQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  93 TVAGGQTRLQASDRYRDLAGGTGRSAKE---QVLRKGTENLQRAQAEVLQSVRELSRSRKLYG--QRERVWALAQEKAAD 167
Cdd:cd07683   82 VRRESKDHATLSDIYLNNVIMRFMQISEdstRMFKKSKEIAFQLHEDLMKVLNELYTVMKTYHmyHTESISAESKLKEAE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 168 VQA--RLNRSDHGIFHSRTS-----------LQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALL 234
Cdd:cd07683  162 KQEekQIGRSGDPVFHIRLEdrhqrrssvkkIEKMKEKRQAKYSENKLKSIKARNEYLLTLEATNASVFKYYIHDLSDLI 241
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 21-237 3.75e-09

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: 57.26  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  21 QLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSGEMDSRGRtvfgAWRCLLDATVA-GGQT 99
Cdd:cd07653    6 QFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKKKEEDEYSFSSVK----AFRSILNEVNDiAGQH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 100 RLQASDRYRDLAGGTGRSAKE--QVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARLNrsdh 177
Cdd:cd07653   82 ELIAENLNSNVCKELKTLISElrQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMN---- 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 178 gifHSRTSLQklstKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKAL 237
Cdd:cd07653  158 ---LTKADVE----KAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKL 210
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 17-234 6.37e-08

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


Pssm-ID: 153368 [Multi-domain]  Cd Length: 253  Bit Score: 53.55  E-value: 6.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  17 RFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPF---LKREGHRSGEMDSRGRTVFGAWRCLLDAT 93
Cdd:cd07684    2 QLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFsskIRTSREHQFKKDQQLLSPVNCWYLVLEQT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  94 VAGGQTRLQASDRYRDLAGGTGRSAKEQVLR---KGTENLQRAQAEVLQSVRELSRSRKLY---------GQRERVWALA 161
Cdd:cd07684   82 RRESRDHATLNDIFNNNVIVRLSQISEDVIRlfkKSKEIGLQMHEELLKVTNELYTVMKTYhmyhaesisAESKLKEAEK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 162 QE-----KAADVQARLNRSDHGIfHSRTSLQKLSTKLSAQSAQYSQ---QLQAARNEYLLNLVATNAHLDHYYQEELPAL 233
Cdd:cd07684  162 QEekqfnKSGDISSNLLRHEERP-QRRSSVKKIEKMKEKRQAKYSEnklKCTKARNDYLLNLAATNAAVSKYYIHDVSDL 240


                 .
gi 767937894 234 L 234
Cdd:cd07684  241 I 241
F-BAR_srGAP2 cd07682
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 17-235 6.32e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating 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. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP2 is expressed in zones of neuronal differentiation. It plays a role in the regeneration of neurons and axons. srGAP2 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153366 [Multi-domain]  Cd Length: 263  Bit Score: 50.85  E-value: 6.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  17 RFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSGEMDSRGRTVFG---AWRCLLDAT 93
Cdd:cd07682    2 QLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSpvnCWNLLLNQV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  94 VAGGQTRLQASD--------RYRDLAGGTGRsakeqVLRKGTENLQRAQAEVLQSVRELSRSRKLY---------GQRER 156
Cdd:cd07682   82 KRESRDHATLSDiylnniipRFVQISEDSGR-----LFKKSKEVGLQLQEDLMKVLNELYTVMKTYhmynadsisAQSKL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 157 VWALAQE----------------KAADVQARLNRSDHGIfhSRTSLQKLSTKLSAQSAQYSQ-QLQA--ARNEYLLNLVA 217
Cdd:cd07682  157 KEAEKQEekqmsrsvrqedrqtpRSPDSTTNIRIEEKHV--RRSSVKKIEKMKEKRQAKYTEnKLKAikARNEYLLALEA 234

                        250
                 ....*....|....*...
gi 767937894 218 TNAHLDHYYQEELPALLK 235
Cdd:cd07682  235 TNASVFKYYIHDLSDLID 252
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 20-102 1.15e-06

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: 46.57  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894    20 EQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGpflKREGHRSGEMdsRGRTVFGAWRCLLDATVAGGQT 99
Cdd:smart00055   9 DGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK---KLRAVRDTEP--EYGSLSKAWEVLLSETDALAKQ 83


                   ...
gi 767937894   100 RLQ 102
Cdd:smart00055  84 HLE 86
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 25-237 4.26e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer (Fes related) tyrosine kinases; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), and Fer (Fes related) are cytoplasmic (or nonreceptor) tyrosine kinases that play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Although Fes and Fer show redundancy in their biological functions, they show differences in their expression patterns. Fer is ubiquitously expressed while Fes is expressed predominantly in myeloid and endothelial cells. Fes and Fer contain an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling.


Pssm-ID: 153341 [Multi-domain]  Cd Length: 237  Bit Score: 47.76  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  25 LQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGhrsgEMDSRGRTVFGAWRCLLDATvagGQTRLQAS 104
Cdd:cd07657   10 LLKRQDAELRLLETMKKYMAKRAKSDREYASTLGSLANQGLKIEA----GDDLQGSPISKSWKEIMDST---DQLSKLIK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 105 DRYRDLAGGTGRSA------KEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARLNRSDHG 178
Cdd:cd07657   83 QHAEALESGTLDKLtllikdKRKAKKAYQEERQQIDEQYKKLTDEVEKLKSEYQKLLEDYKAAKSKFEEAVVKGGRGGRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767937894 179 IFHSRTSLQKLSTKLsaqsaqysqqlQAARNEYLLNLVATNAHLDHYYQEELPALLKAL 237
Cdd:cd07657  163 LDKARDKYQKACRKL-----------HLCHNDYVLALLEAQEHEEDYRTLLLPGLLNSL 210
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 25-258 2.90e-04

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: 41.94  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  25 LQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKreghrsgeMDSRGRTVFG-AWRCLldatvagGQTRLQA 103
Cdd:cd07610    5 LEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSK--------KPESGKTSLGtSWNSL-------REETESA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 104 SDRYRDLAggtgrSAKEQVLRKGTENLQRAQAEvlQSVRELSRSRKLYGQRERVWALAQEKAADVqarlnrsdhgifhsr 183
Cdd:cd07610   70 ATVHEELS-----EKLSQLIREPLEKVKEDKEQ--ARKKELAEGEKLKKKLQELWAKLAKKADEE--------------- 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767937894 184 tslqklstklsaqSAQYSQQLQAARNEYLLNLVATNAHLDHYYqEELPALLKALVSELSEHLRDPLTSLSHTELE 258
Cdd:cd07610  128 -------------YREQVEKLNPAQSEYEEEKLNKIQAEQERE-EERLEILKDNLKNYINAIKEIPQKIQQELEQ 188
F-BAR_Fes cd07685
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) tyrosine ...
 23-239 4.16e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) tyrosine kinase; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), is a cytoplasmic (or nonreceptor) tyrosine kinase whose gene was first isolated from tumor-causing retroviruses. It is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells, and plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. Fes kinase has also been implicated as a tumor suppressor in colorectal cancer. It contains an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling.


Pssm-ID: 153369 [Multi-domain]  Cd Length: 237  Bit Score: 38.78  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894  23 SILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSGEMDSRGRTVFGAWRCLLDATVAGGQTRLQ 102
Cdd:cd07685    8 AALLRLQDSELRLMEVMKKWMSQRAKSDREYSGMLHHMSAQVEKLDRSQHGALSMLSSPISQSWAVLVSQTETLSQVLRK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937894 103 ASDRYRD--LAGGTGRSAKEQVLRKG-TENLQRAQAEVLQSVR-ELSRSRKLYGQRERVWALAQEKaadvqarlnrsdhg 178
Cdd:cd07685   88 HAEDLNAgpLSKLSLLIRDKQQLRKTfSEQWQLLKQEYTKTTQqDIEKLKSQYRSLAKDSAQAKRK-------------- 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767937894 179 ifHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVS 239
Cdd:cd07685  154 --YQEASKDKDRDKAKEKYVKSLWKLYALHNEYVLAVRAAQLHHQHHYQRILPGLLESLQS 212
 
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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