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Conserved domains on  [gi|1869284279|ref|NP_001372156|]
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SLIT-ROBO Rho GTPase-activating protein 2B isoform 6 [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 ...
 26-268 3.67e-152

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 cd07682:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 263  Bit Score: 432.19  E-value: 3.67e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  26 AQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVNCWNLLLNQ 105
Cdd:cd07682     1 AQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 106 VKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKK---------------------VMKTYHMYNADSISAQSKLKEAE 164
Cdd:cd07682    81 VKRESRDHATLSDIYLNNIIPRFVQISEDSGRLFKKskevglqlqedlmkvlnelytVMKTYHMYNADSISAQSKLKEAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 165 KQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 244
Cdd:cd07682   161 KQEEKQMSRSVRQEDRQTPRSPDSTTNIRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 240

                         250       260
                  ....*....|....*....|....
gi 1869284279 245 KYYIHDLSDLIDqCCDLGYHASLN 268
Cdd:cd07682   241 KYYIHDLSDLID-CCDLGYHASLN 263
 
Name Accession Description Interval E-value
F-BAR_srGAP2 cd07682
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-268 3.67e-152

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: 432.19  E-value: 3.67e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  26 AQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVNCWNLLLNQ 105
Cdd:cd07682     1 AQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 106 VKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKK---------------------VMKTYHMYNADSISAQSKLKEAE 164
Cdd:cd07682    81 VKRESRDHATLSDIYLNNIIPRFVQISEDSGRLFKKskevglqlqedlmkvlnelytVMKTYHMYNADSISAQSKLKEAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 165 KQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 244
Cdd:cd07682   161 KQEEKQMSRSVRQEDRQTPRSPDSTTNIRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 240

                         250       260
                  ....*....|....*....|....
gi 1869284279 245 KYYIHDLSDLIDqCCDLGYHASLN 268
Cdd:cd07682   241 KYYIHDLSDLID-CCDLGYHASLN 263
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 31-113 2.29e-13

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: 64.98  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  31 QMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFkkdqnvlSPVNCWNLLLNQVKRES 110
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGG-------TLKKAWDELLTETEQLA 73


                  ...
gi 1869284279 111 RDH 113
Cdd:pfam00611  74 KQH 76
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 27-116 1.86e-09

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: 54.27  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279   27 QLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAErflaktcstKDQQFKKDQNVLSPVN-CWNLLLNQ 105
Cdd:smart00055   6 ELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK---------KLRAVRDTEPEYGSLSkAWEVLLSE 76

                           90
                   ....*....|.
gi 1869284279  106 VKRESRDHTTL 116
Cdd:smart00055  77 TDALAKQHLEL 87
 
Name Accession Description Interval E-value
F-BAR_srGAP2 cd07682
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-268 3.67e-152

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: 432.19  E-value: 3.67e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  26 AQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVNCWNLLLNQ 105
Cdd:cd07682     1 AQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 106 VKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKK---------------------VMKTYHMYNADSISAQSKLKEAE 164
Cdd:cd07682    81 VKRESRDHATLSDIYLNNIIPRFVQISEDSGRLFKKskevglqlqedlmkvlnelytVMKTYHMYNADSISAQSKLKEAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 165 KQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 244
Cdd:cd07682   161 KQEEKQMSRSVRQEDRQTPRSPDSTTNIRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 240

                         250       260
                  ....*....|....*....|....
gi 1869284279 245 KYYIHDLSDLIDqCCDLGYHASLN 268
Cdd:cd07682   241 KYYIHDLSDLID-CCDLGYHASLN 263
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-268 1.51e-110

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: 325.87  E-value: 1.51e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  26 AQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKD-QQFKKDQNVLSPVNCWNLLLN 104
Cdd:cd07683     1 AQLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAKTRSTKDhQQYKKDQNLLSPVNCWYLLLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 105 QVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKK---------------------VMKTYHMYNADSISAQSKLKEA 163
Cdd:cd07683    81 QVRRESKDHATLSDIYLNNVIMRFMQISEDSTRMFKKskeiafqlhedlmkvlnelytVMKTYHMYHTESISAESKLKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 164 EKQEEKQIGksvkqedrqtpRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASV 243
Cdd:cd07683   161 EKQEEKQIG-----------RSGDPVFHIRLEDRHQRRSSVKKIEKMKEKRQAKYSENKLKSIKARNEYLLTLEATNASV 229

                         250       260
                  ....*....|....*....|....*
gi 1869284279 244 FKYYIHDLSDLIDqCCDLGYHASLN 268
Cdd:cd07683   230 FKYYIHDLSDLID-CCDLGYHASLN 253
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-268 1.26e-103

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: 307.72  E-value: 1.26e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  26 AQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFkkDQNVLSPVNCWNLLLNQ 105
Cdd:cd07656     1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKRE--DWSLLSPVNCWNTLLVQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 106 VKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKK---------------------VMKTYHMYNADSISAQSKLKEAE 164
Cdd:cd07656    79 TKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKcreigsqlhdellrvlnelqtAMKTYHTYHAESKSAERKLKEAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 165 KQEEKQIGksvkqedrqtprspdstanvRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVF 244
Cdd:cd07656   159 KQEEKQEQ--------------------SPEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCTKARNEYLLNLAAANATIH 218

                         250       260
                  ....*....|....*....|....
gi 1869284279 245 KYYIHDLSDLIDqCCDLGYHASLN 268
Cdd:cd07656   219 KYFVQDLSDLID-CMDLGFHNSLS 241
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 27-267 9.59e-97

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: 290.84  E-value: 9.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  27 QLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVNCWNLLLNQV 106
Cdd:cd07684     2 QLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRTSREHQFKKDQQLLSPVNCWYLVLEQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 107 KRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKK---------------------VMKTYHMYNADSISAQSKLKEAEK 165
Cdd:cd07684    82 RRESRDHATLNDIFNNNVIVRLSQISEDVIRLFKKskeiglqmheellkvtnelytVMKTYHMYHAESISAESKLKEAEK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 166 QEEKQIGKSvkqedrqtprSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFK 245
Cdd:cd07684   162 QEEKQFNKS----------GDISSNLLRHEERPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAVSK 231

                         250       260
                  ....*....|....*....|..
gi 1869284279 246 YYIHDLSDLIDqCCDLGYHASL 267
Cdd:cd07684   232 YYIHDVSDLID-CCDLGFHASL 252
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 31-268 4.73e-17

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: 78.92  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  31 QMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKdqqfkkdqnvlspvNCWNLLLNQVKRES 110
Cdd:cd07610     1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGK--------------TSLGTSWNSLREET 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 111 RDHTTLSDIYLNNIiprfVQVSEDSGRLFKKVMKTYHM-YNADSISAQSKLKEAEKQEEKQigksvkqedrqtprspdst 189
Cdd:cd07610    67 ESAATVHEELSEKL----SQLIREPLEKVKEDKEQARKkELAEGEKLKKKLQELWAKLAKK------------------- 123

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1869284279 190 anvrieekhvRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDlIDQCCDLGYHASLN 268
Cdd:cd07610   124 ----------ADEEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKE-IPQKIQQELEQSIN 191
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 31-113 2.29e-13

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: 64.98  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  31 QMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFkkdqnvlSPVNCWNLLLNQVKRES 110
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGG-------TLKKAWDELLTETEQLA 73


                  ...
gi 1869284279 111 RDH 113
Cdd:pfam00611  74 KQH 76
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
 29-284 1.26e-11

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: 64.53  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  29 TEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVncWNLLLNQVKR 108
Cdd:cd07654     4 LEQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLKREWPGSGELKPEDDRSGYTV--WGAWLEGLDA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 109 ESRDHTTLSDIYLNNIiprfvqvsEDSGRLFKKVMKTYHMYNADSIS-AQSKLKEAEKQEEKqiGKSVKQEDRQTPRSP- 186
Cdd:cd07654    82 VAQSRQNRCEAYRRYI--------SEPAKTGRSAKEQQLKKCTEQLQrAQAEVQQTVRELSK--SRKTYFEREQVAHLAr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 187 DSTANVRIEEKHVRRS---SVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIdQCCDLGY 263
Cdd:cd07654   152 EKAADVQAREARSDLSifqSRTSLQKASVKLSARKAECSSKATAARNDYLLNLAATNAHQDRYYQTDLPAII-KALDGEL 230

                         250       260
                  ....*....|....*....|.
gi 1869284279 264 HASLNRALRTFLSAELNLEQS 284
Cdd:cd07654   231 YDHLKDFLISLSHTELETAQV 251
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 30-303 6.04e-10

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: 59.76  E-value: 6.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  30 EQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVncWNLLLNQVKRE 109
Cdd:cd07677     5 EQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLKSDWRGMKADERADYRSMYTV--WKSFLEGTMQV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 110 SRDHTTLSDIYLNniiprFVQVSEDSGRLFKKvmKTYHMYNADSISAQSKLKEAEKQEEKqiGKSVKQEDRQTPRSPDST 189
Cdd:cd07677    83 AQSRINICENYKN-----LISEPARTVRLYKE--QQLKRCVDQLTKIQAELQETVKDLAK--GKKKYFETEQMAHAVREK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 190 ANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIdQCCDLGYHASLNR 269
Cdd:cd07677   154 ADIEAKSKLSLFQSRISLQKASVKLKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIM-KALDGNVYDHLKD 232

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1869284279 270 ALRTFLSAELnleqskhEGLDAIENAVENLDATS 303
Cdd:cd07677   233 YLMAFSRTEL-------ETCQAVQNTFQFLLETS 259
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 27-116 1.86e-09

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: 54.27  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279   27 QLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAErflaktcstKDQQFKKDQNVLSPVN-CWNLLLNQ 105
Cdd:smart00055   6 ELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK---------KLRAVRDTEPEYGSLSkAWEVLLSE 76

                           90
                   ....*....|.
gi 1869284279  106 VKRESRDHTTL 116
Cdd:smart00055  77 TDALAKQHLEL 87
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 30-280 2.83e-09

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: 57.71  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  30 EQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVNCWnlllnqvkRE 109
Cdd:cd07678     5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGNETEMDRSVRTVWGAW--------RE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 110 SRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKVMKTYHMYNAdsISAQSKLKEAEKQEEKQiGKSVKQEDRQTPRSPDST 189
Cdd:cd07678    77 GTAATGQGRVTRLEAYRRLRDEAGKTGRSAKEQVLKKSTEQL--QKAQAELLETVKELSKS-KKLYGQLERVSEVAKEKA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 190 ANVRIEEKHVRRS---SVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIdQCCDLGYHAS 266
Cdd:cd07678   154 ADVEARLNKSDHGifhSKASLQKLSAKFSAQSAEYSQQLQAARNEYLLNLVAANAHLDHYYQEELPAIM-KALDGDLYER 232

                         250
                  ....*....|....
gi 1869284279 267 LNRALRTFLSAELN 280
Cdd:cd07678   233 LRDPLTSLSHTELE 246
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 27-257 5.72e-03

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: 38.39  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279  27 QLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKtcstkdqQFKKDQNVLSPVNCWNLLLNQV 106
Cdd:cd07653     2 ELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPK-------KKEEDEYSFSSVKAFRSILNEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284279 107 KRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKVMKtyhmynaDSISAQSKLKEAEKQEEKQIGKSVKQEdRQTPRSP 186
Cdd:cd07653    75 NDIAGQHELIAENLNSNVCKELKTLISELRQERKKHLS-------EGSKLQQKLESSIKQLEKSKKAYEKAF-KEAEKAK 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1869284279 187 DSTANVRIEEKHVRrssvKKIEKMKEKRQAKYTEnklkAIKARNEYLLALEATNASVFKYYIHDLSDLIDQ 257
Cdd:cd07653   147 QKYEKADADMNLTK----ADVEKAKANANLKTQA----AEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDK 209
 
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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