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Conserved domains on  [gi|29242797|gb|AAO66337|]
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truncated Rho GTPase-activating protein 4 splice form 2 [Homo sapiens]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166576)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-281 5.09e-113

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: 338.15  E-value: 5.09e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  26 WQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSfrkepsLLSPLHCWAV 105
Cdd:cd07656   1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKREDWS------LLSPVNCWNT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 106 LLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKL 185
Cdd:cd07656  75 LLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGSQLHDELLRVLNELQTAMKTYHTYHAESKSAERKL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 186 REAERQEEKRAGRsvptttagaTEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDV 265
Cdd:cd07656 155 KEAEKQEEKQEQS---------PEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCTKARNEYLLNLAAANATIHKYFVQDL 225

                       250
                ....*....|....*.
gi 29242797 266 LDLMDCCDTGFHLALG 281
Cdd:cd07656 226 SDLIDCMDLGFHNSLS 241
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 503-577 2.00e-27

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


The actual alignment was detected with superfamily member cd04383:

Pssm-ID: 470621  Cd Length: 188  Bit Score: 109.43  E-value: 2.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 503 RLFGGDMEKFIQSSGQPVPLVVESCIRFINLN--------------------------GEDPLVEGCTAHDLDSVAGVLK 556
Cdd:cd04383   1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYglqhqgifrvsgsqvevndiknaferGEDPLADDQNDHDINSVAGVLK 80

                        90       100
                ....*....|....*....|.
gi 29242797 557 LYFRSLEPPLFPPDLFGELLA 577
Cdd:cd04383  81 LYFRGLENPLFPKERFEDLMS 101
 
Name Accession Description Interval E-value
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-281 5.09e-113

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: 338.15  E-value: 5.09e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  26 WQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSfrkepsLLSPLHCWAV 105
Cdd:cd07656   1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKREDWS------LLSPVNCWNT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 106 LLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKL 185
Cdd:cd07656  75 LLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGSQLHDELLRVLNELQTAMKTYHTYHAESKSAERKL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 186 REAERQEEKRAGRsvptttagaTEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDV 265
Cdd:cd07656 155 KEAEKQEEKQEQS---------PEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCTKARNEYLLNLAAANATIHKYFVQDL 225

                       250
                ....*....|....*.
gi 29242797 266 LDLMDCCDTGFHLALG 281
Cdd:cd07656 226 SDLIDCMDLGFHNSLS 241
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 503-577 2.00e-27

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 109.43  E-value: 2.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 503 RLFGGDMEKFIQSSGQPVPLVVESCIRFINLN--------------------------GEDPLVEGCTAHDLDSVAGVLK 556
Cdd:cd04383   1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYglqhqgifrvsgsqvevndiknaferGEDPLADDQNDHDINSVAGVLK 80

                        90       100
                ....*....|....*....|.
gi 29242797 557 LYFRSLEPPLFPPDLFGELLA 577
Cdd:cd04383  81 LYFRGLENPLFPKERFEDLMS 101
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 22-120 5.31e-12

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


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 61.97  E-value: 5.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797     22 KEMRWQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLaerfssrggrlgsSREHQSFRKEPSLLSPL- 100
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKL-------------SKKLRAVRDTEPEYGSLs 67

                           90       100
                   ....*....|....*....|
gi 29242797    101 HCWAVLLQHTRQQSRESAAL 120
Cdd:smart00055  68 KAWEVLLSETDALAKQHLEL 87
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 518-576 4.46e-10

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 58.82  E-value: 4.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797    518 QPVPLVVESCIRFINLNGED-------------------------PLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPPDLF 572
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDtegiyrvsgsksrvkelrdafdsgpDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80


                   ....
gi 29242797    573 GELL 576
Cdd:smart00324  81 EEFI 84
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 31-115 1.15e-08

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: 52.27  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797    31 QLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGrlgssrehqsfRKEPSLLSPLHCWAVLLQHT 110
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKK-----------KPEDDGGTLKKAWDELLTET 69


                  ....*
gi 29242797   111 RQQSR 115
Cdd:pfam00611  70 EQLAK 74
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 521-583 1.27e-08

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 54.09  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797   521 PLVVESCIRFINLNGEDplVEGC---------------------------TAHDLDSVAGVLKLYFRSLEPPLFPPDLFG 573
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLD--TEGIfrvsgsasrikelreafdrgpdvdldlEEEDVHVVASLLKLFLRELPEPLLTFELYE 78

                          90
                  ....*....|
gi 29242797   574 ELLASSGTPS 583
Cdd:pfam00620  79 EFIEAAKLPD 88
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 2-196 6.72e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 6.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797      2 AAHGKLRRERGLQ------AEYETQVKEMRWQLSEQLRCLELQGELRRELLQELAEFMRRRAEVElEYSRGLEKL---AE 72
Cdd:TIGR00618  277 AVLEETQERINRArkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLhsqEI 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797     73 RFSSRGGRLGSSREHqsFRKEPSLLSPLHCWAVLLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDvgrlvkksRDLEQQ 152
Cdd:TIGR00618  356 HIRDAHEVATSIREI--SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF--------RDLQGQ 425

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 29242797    153 LQdeLLEVVSELQTAKKTYQAYHMESVNAEAKLREAERQEEKRA 196
Cdd:TIGR00618  426 LA--HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
 
Name Accession Description Interval E-value
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 26-281 5.09e-113

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: 338.15  E-value: 5.09e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  26 WQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSfrkepsLLSPLHCWAV 105
Cdd:cd07656   1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKREDWS------LLSPVNCWNT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 106 LLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKL 185
Cdd:cd07656  75 LLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGSQLHDELLRVLNELQTAMKTYHTYHAESKSAERKL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 186 REAERQEEKRAGRsvptttagaTEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDV 265
Cdd:cd07656 155 KEAEKQEEKQEQS---------PEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCTKARNEYLLNLAAANATIHKYFVQDL 225

                       250
                ....*....|....*.
gi 29242797 266 LDLMDCCDTGFHLALG 281
Cdd:cd07656 226 SDLIDCMDLGFHNSLS 241
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 27-281 8.83e-91

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: 281.21  E-value: 8.83e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  27 QLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRggrLGSSREHQsFRKEPSLLSPLHCWAVL 106
Cdd:cd07684   2 QLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSK---IRTSREHQ-FKKDQQLLSPVNCWYLV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 107 LQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLR 186
Cdd:cd07684  78 LEQTRRESRDHATLNDIFNNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 187 EAERQEEKRAGRSVPTTTAGAT-EAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDV 265
Cdd:cd07684 158 EAEKQEEKQFNKSGDISSNLLRhEERPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAVSKYYIHDV 237

                       250
                ....*....|....*.
gi 29242797 266 LDLMDCCDTGFHLALG 281
Cdd:cd07684 238 SDLIDCCDLGFHASLA 253
F-BAR_srGAP2 cd07682
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 27-280 4.28e-82

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: 259.24  E-value: 4.28e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  27 QLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGgrlgSSREHQSFRKEPSLLSPLHCWAVL 106
Cdd:cd07682   2 QLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKT----RSTKDQQFKKDQNVLSPVNCWNLL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 107 LQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLR 186
Cdd:cd07682  78 LNQVKRESRDHATLSDIYLNNIIPRFVQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMKTYHMYNADSISAQSKLK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 187 EAERQEEKRAGRSV-----------PTTTAGATEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNA 255
Cdd:cd07682 158 EAEKQEEKQMSRSVrqedrqtprspDSTTNIRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNA 237

                       250       260
                ....*....|....*....|....*
gi 29242797 256 AVSNYYLHDVLDLMDCCDTGFHLAL 280
Cdd:cd07682 238 SVFKYYIHDLSDLIDCCDLGYHASL 262
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 27-280 2.28e-78

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: 249.21  E-value: 2.28e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  27 QLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRggrLGSSREHQSFRKEPSLLSPLHCWAVL 106
Cdd:cd07683   2 QLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAK---TRSTKDHQQYKKDQNLLSPVNCWYLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 107 LQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLR 186
Cdd:cd07683  79 LNQVRRESKDHATLSDIYLNNVIMRFMQISEDSTRMFKKSKEIAFQLHEDLMKVLNELYTVMKTYHMYHTESISAESKLK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 187 EAERQEEKRAGRSVPTTTAGATEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDVL 266
Cdd:cd07683 159 EAEKQEEKQIGRSGDPVFHIRLEDRHQRRSSVKKIEKMKEKRQAKYSENKLKSIKARNEYLLTLEATNASVFKYYIHDLS 238

                       250
                ....*....|....
gi 29242797 267 DLMDCCDTGFHLAL 280
Cdd:cd07683 239 DLIDCCDLGYHASL 252
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 503-577 2.00e-27

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 109.43  E-value: 2.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 503 RLFGGDMEKFIQSSGQPVPLVVESCIRFINLN--------------------------GEDPLVEGCTAHDLDSVAGVLK 556
Cdd:cd04383   1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYglqhqgifrvsgsqvevndiknaferGEDPLADDQNDHDINSVAGVLK 80

                        90       100
                ....*....|....*....|.
gi 29242797 557 LYFRSLEPPLFPPDLFGELLA 577
Cdd:cd04383  81 LYFRGLENPLFPKERFEDLMS 101
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 30-295 1.40e-18

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: 85.83  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  30 EQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSfrkePSLLSPLHCWAVLLQH 109
Cdd:cd07678   5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGNETEMD----RSVRTVWGAWREGTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 110 TRQQSRESAALSEVLAGpLAQRLSHIAEDvgRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQayHMESVNAEAKLREAE 189
Cdd:cd07678  81 TGQGRVTRLEAYRRLRD-EAGKTGRSAKE--QVLKKSTEQLQKAQAELLETVKELSKSKKLYG--QLERVSEVAKEKAAD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 190 RQEE-KRAGRSVPTTtagateagplrKSSLKKggrLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDVLDL 268
Cdd:cd07678 156 VEARlNKSDHGIFHS-----------KASLQK---LSAKFSAQSAEYSQQLQAARNEYLLNLVAANAHLDHYYQEELPAI 221

                       250       260
                ....*....|....*....|....*..
gi 29242797 269 MDCCDTgfhlALGQVLRSYTAAESRTQ 295
Cdd:cd07678 222 MKALDG----DLYERLRDPLTSLSHTE 244
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
 29-296 1.27e-15

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: 77.24  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  29 SEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSFRKEPSLLSPLHCWAVLLQ 108
Cdd:cd07654   4 LEQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLKREWPGSGELKPEDDRSGYTVWGAWLEGLDAVA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 109 HTRQQSRESAALSEVLAGPLAQRLSHIAedvgrlVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLREA 188
Cdd:cd07654  84 QSRQNRCEAYRRYISEPAKTGRSAKEQQ------LKKCTEQLQRAQAEVQQTVRELSKSRKTYFEREQVAHLAREKAADV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 189 ERQEeKRAGRSVPTTtagateagplrKSSLKKggrLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDVLDL 268
Cdd:cd07654 158 QARE-ARSDLSIFQS-----------RTSLQK---ASVKLSARKAECSSKATAARNDYLLNLAATNAHQDRYYQTDLPAI 222

                       250       260       270
                ....*....|....*....|....*....|
gi 29242797 269 MDCCDTGF--HLALGQVLRSYTAAESRTQA 296
Cdd:cd07654 223 IKALDGELydHLKDFLISLSHTELETAQVI 252
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 30-302 1.33e-13

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: 71.31  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  30 EQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSFRkepsllSPLHCWAVLLQH 109
Cdd:cd07677   5 EQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLKSDWRGMKADERADYR------SMYTVWKSFLEG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 110 TRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYqayhMESVNAEAKLREAE 189
Cdd:cd07677  79 TMQVAQSRINICENYKNLISEPARTVRLYKEQQLKRCVDQLTKIQAELQETVKDLAKGKKKY----FETEQMAHAVREKA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 190 RQEEKRAGRSVPTTTAgateagpLRKSSLKkggrlvekRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDVLDLM 269
Cdd:cd07677 155 DIEAKSKLSLFQSRIS-------LQKASVK--------LKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIM 219

                       250       260       270
                ....*....|....*....|....*....|...
gi 29242797 270 DCCDTGFHlalgQVLRSYTAAESRTQASQVQGL 302
Cdd:cd07677 220 KALDGNVY----DHLKDYLMAFSRTELETCQAV 248
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 22-120 5.31e-12

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


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 61.97  E-value: 5.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797     22 KEMRWQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLaerfssrggrlgsSREHQSFRKEPSLLSPL- 100
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKL-------------SKKLRAVRDTEPEYGSLs 67

                           90       100
                   ....*....|....*....|
gi 29242797    101 HCWAVLLQHTRQQSRESAAL 120
Cdd:smart00055  68 KAWEVLLSETDALAKQHLEL 87
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 518-576 4.46e-10

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 58.82  E-value: 4.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797    518 QPVPLVVESCIRFINLNGED-------------------------PLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPPDLF 572
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDtegiyrvsgsksrvkelrdafdsgpDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80


                   ....
gi 29242797    573 GELL 576
Cdd:smart00324  81 EEFI 84
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 31-115 1.15e-08

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: 52.27  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797    31 QLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGrlgssrehqsfRKEPSLLSPLHCWAVLLQHT 110
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKK-----------KPEDDGGTLKKAWDELLTET 69


                  ....*
gi 29242797   111 RQQSR 115
Cdd:pfam00611  70 EQLAK 74
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 521-583 1.27e-08

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 54.09  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797   521 PLVVESCIRFINLNGEDplVEGC---------------------------TAHDLDSVAGVLKLYFRSLEPPLFPPDLFG 573
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLD--TEGIfrvsgsasrikelreafdrgpdvdldlEEEDVHVVASLLKLFLRELPEPLLTFELYE 78

                          90
                  ....*....|
gi 29242797   574 ELLASSGTPS 583
Cdd:pfam00620  79 EFIEAAKLPD 88
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 34-274 1.61e-07

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: 51.96  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  34 CLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSsrggrlgssrehqsfrkePSLLSPLHCWAVLLQHTRQQ 113
Cdd:cd07610   4 LLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFS------------------KKPESGKTSLGTSWNSLREE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 114 SRESAALSEVlagpLAQRLSHIAEDVGRLVKKsrDLEQQLqdellevVSELQTAKKTYQayhmesvnaeaKLREAERQEE 193
Cdd:cd07610  66 TESAATVHEE----LSEKLSQLIREPLEKVKE--DKEQAR-------KKELAEGEKLKK-----------KLQELWAKLA 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 194 KRAGRSVptttagateagplrKSSLKKGgrlvEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDVLDLMDCCD 273
Cdd:cd07610 122 KKADEEY--------------REQVEKL----NPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQ 183


                .
gi 29242797 274 T 274
Cdd:cd07610 184 Q 184
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 505-574 1.92e-06

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 48.94  E-value: 1.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 505 FGGDMEKFIQSSGQPVPLVVESCIRFINLNG------------------------EDPLVEGCTA-----HDLDSVAGVL 555
Cdd:cd04398   1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGlnlegiyrlsgnvsrvnklkelfdKDPLNVLLISpedyeSDIHSVASLL 80

                        90
                ....*....|....*....
gi 29242797 556 KLYFRSLEPPLFPPDLFGE 574
Cdd:cd04398  81 KLFFRELPEPLLTKALSRE 99
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 521-576 2.26e-06

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 48.07  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 521 PLVVESCIRFINLNGEDplVEGC--------------------------TAHDLDSVAGVLKLYFRSLEPPLFPPDLFGE 574
Cdd:cd00159   1 PLIIEKCIEYLEKNGLN--TEGIfrvsgsaskieelkkkfdrgediddlEDYDVHDVASLLKLYLRELPEPLIPFELYDE 78


                ..
gi 29242797 575 LL 576
Cdd:cd00159  79 FI 80
F-BAR_Fer cd07686
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine ...
 35-188 1.33e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) 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. Fer (Fes related) is a cytoplasmic (or nonreceptor) tyrosine kinase expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells. 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.


Pssm-ID: 153370 [Multi-domain]  Cd Length: 234  Bit Score: 46.98  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  35 LELQG-ELRreLLQELAEFMRRRAEVELEYSRGLEKLAERFSsrggrlgssREHQSFRKEPSLLSplHCWAVLLQHTRQQ 113
Cdd:cd07686  11 LKLQDwELR--LLETVKKFMALRVKSDKEYASTLQNLCNQVD---------KESTSQLDYVSNVS--KSWLHMVQQTEQL 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29242797 114 SRESAALSEVL-AGPLaQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVV-SELQTAKKTYQAYHMESVNAEAKLREA 188
Cdd:cd07686  78 SKIMKTHAEELnSGPL-HRLTMMIKDKQQVKKSYIGVHQQIEAEMYKVTkTELEKLKCSYRQLTKEVNSAKEKYKDA 153
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 47-194 2.80e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 46.18  E-value: 2.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  47 QELAEFMRRRAEVELEYSRGLEKLAERFSSrGGRLGSsrehqsfrkepslLSPlhCWAVLLQHTRQqsresaaLSEVLAg 126
Cdd:cd07648  22 KELADFLRERATIEETYSKALNKLAKQASN-SSQLGT-------------FAP--LWLVLRVSTEK-------LSELHL- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 127 PLAQRLSHIAEDVGR----LVKKSRDLEQQLQDElLEVVSELQT-------AKKTYQAYHMESV---NAEAKLREAERQE 192
Cdd:cd07648  78 QLVQKLQELIKDVQKygeeQHKKHKKVKEEESGT-AEAVQAIQTttaalqkAKEAYHARCLELErlrRENASPKEIEKAE 156


                ..
gi 29242797 193 EK 194
Cdd:cd07648 157 AK 158
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 47-259 1.42e-04

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: 43.89  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  47 QELAEFMRRRAEVELEYSRGLEKLAERfSSRGGRLGSsrehqsfrkepslLSPLhcWAVLLQHTrqqsresaalsEVLAG 126
Cdd:cd07673  29 KELSDFIRERATIEEAYSRSMTKLAKS-ASNYSQLGT-------------FAPV--WDVFKTST-----------EKLAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 127 ---PLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLREAER-QEEKRAGRSVPT 202
Cdd:cd07673  82 chlELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERlKKEGATQREIEK 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 29242797 203 TTAGATEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSN 259
Cdd:cd07673 162 AAVKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEIIGSYSN 218
F-BAR_Fes cd07685
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) tyrosine ...
 37-194 5.18e-04

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: 42.24  E-value: 5.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  37 LQGELRreLLQELAEFMRRRAEVELEYSRGLEKLAERFSSrggrlGSSREHQSFRKEPSLLSplHCWAVLLQHTRQQSRE 116
Cdd:cd07685  14 QDSELR--LMEVMKKWMSQRAKSDREYSGMLHHMSAQVEK-----LDRSQHGALSMLSSPIS--QSWAVLVSQTETLSQV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 117 SAALSE-VLAGPLAqRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVS-ELQTAKKTYQAYHMESVNAEAKLREAERQEEK 194
Cdd:cd07685  85 LRKHAEdLNAGPLS-KLSLLIRDKQQLRKTFSEQWQLLKQEYTKTTQqDIEKLKSQYRSLAKDSAQAKRKYQEASKDKDR 163
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 40-295 6.61e-04

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: 41.60  E-value: 6.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  40 ELRreLLQELAEFMRRRAEVELEYSRGLEKLAerfsSRGGRLGSSREhqsfrkepSLLSP-LHCWAVLLQHTRQQSRESA 118
Cdd:cd07657  17 ELR--LLETMKKYMAKRAKSDREYASTLGSLA----NQGLKIEAGDD--------LQGSPiSKSWKEIMDSTDQLSKLIK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 119 ALSEVLAGPLAQRLSHIAEDvGRLVKKSRDLE-QQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLREAerqeekrag 197
Cdd:cd07657  83 QHAEALESGTLDKLTLLIKD-KRKAKKAYQEErQQIDEQYKKLTDEVEKLKSEYQKLLEDYKAAKSKFEEA--------- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 198 rsvptttagateagplrKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYY---LHDVLDLMDCCDT 274
Cdd:cd07657 153 -----------------VVKGGRGGRKLDKARDKYQKACRKLHLCHNDYVLALLEAQEHEEDYRtllLPGLLNSLQSLQE 215

                       250       260
                ....*....|....*....|.
gi 29242797 275 GFHLALGQVLRSYTAAESRTQ 295
Cdd:cd07657 216 EFITQWKKILQEYLRYSDLTT 236
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 515-582 6.80e-04

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 40.90  E-value: 6.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 515 SSGQPVPLVVESCIRFINLNGEDP----LVEGCTAH--------------DLDS-------VAGVLKLYFRSLEPPLFPP 569
Cdd:cd04373  10 TSEKPIPIFLEKCVEFIEATGLETegiyRVSGNKTHldslqkqfdqdhnlDLVSkdftvnaVAGALKSFFSELPDPLIPY 89

                        90
                ....*....|...
gi 29242797 570 DLFGELLASSGTP 582
Cdd:cd04373  90 SMHLELVEAAKIN 102
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 47-193 2.25e-03

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: 40.31  E-value: 2.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  47 QELAEFMRRRAEVELEYSRGLEKLAeRFSSRGGRLGSsrehqsfrkepslLSPLhcWAVLlqhtrQQSRESAALSEVlag 126
Cdd:cd07674  22 KELADFVRERAAIEETYSKSMSKLS-KMASNGSPLGT-------------FAPM--WEVF-----RVSSDKLALCHL--- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29242797 127 PLAQRLSHIAEDVGRLVKKSRDLEQQLQDEL---LEVVSELQTA----KKTYQAYHMESVNAEAKLREAERQEE 193
Cdd:cd07674  78 ELMRKLNDLIKDINRYGDEQVKIHKKTKEEAigtLEAVQSLQVQsqhlQKSRENYHSKCVEQERLRREGVPQKE 151
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 547-575 2.98e-03

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 39.14  E-value: 2.98e-03
                        10        20
                ....*....|....*....|....*....
gi 29242797 547 DLDSVAGVLKLYFRSLEPPLFPPDLFGEL 575
Cdd:cd04387  69 DVNAIAGTLKLYFRELPEPLFTDELYPNF 97
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 44-261 3.79e-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: 39.54  E-value: 3.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  44 ELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGrlgssrehqsfRKEPSLLSPLHCWAVLLQHTRQQSRESAALSEV 123
Cdd:cd07653  19 DFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKKK-----------EEDEYSFSSVKAFRSILNEVNDIAGQHELIAEN 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 124 LAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLREAERQEEkragrsvptt 203
Cdd:cd07653  88 LNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMN---------- 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 29242797 204 tagATEAGplrksslkkggrlVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYY 261
Cdd:cd07653 158 ---LTKAD-------------VEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHY 199
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 46-173 4.27e-03

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: 39.21  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  46 LQELAEFMRRRAEVELEYSRGLEKLAeRFSsrggrLGSSRehqsfrkEPSLLSPLHcwaVLLQHTRQQSRESAALSEVLA 125
Cdd:cd07651  21 LEELRSFYKERASIEEEYAKRLEKLS-RKS-----LGGSE-------EGGLKNSLD---TLRLETESMAKSHLKFAKQIR 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 29242797 126 GPLAQRLSHIAedvGRLVKKSRDLEQQLQDEL---LEVVSELQTAKKTYQA 173
Cdd:cd07651  85 QDLEEKLAAFA---SSYTQKRKKIQSHMEKLLkkkQDQEKYLEKAREKYEA 132
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 48-275 5.76e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 38.87  E-value: 5.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797  48 ELAEFMRRRAEVELEYSRGLEKLA----ERFSSRGGRlgssreHQSFrkepsllsplhcwavllqhtrqqsreSAALSEV 123
Cdd:cd07652  23 EFATFLKKRAAIEEEHARGLKKLArttlDTYKRPDHK------QGSF--------------------------SNAYHSS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 124 LagplaqrlsHIAEDVG----RLVKKSrdleQQLQDELLEVVSELQTAKKTYQAYHmesVNAEAKLREAERQEEKRAGR- 198
Cdd:cd07652  71 L---------EFHEKLAdnglRFAKAL----NEMSDELSSLAKTVEKSRKSIKETG---KRAEKKVQDAEAAAEKAKARy 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797 199 ------------SVPTTTAGATEAGPlrKSSLKKGGRLVEKRQAK---FMEHKLKCTKARNEyLLSLASVNAAvsnyylH 263
Cdd:cd07652 135 dsladdlervktGDPGKKLKFGLKGN--KSAAQHEDELLRKVQAAdqdYASKVNAAQALRQE-LLSRHRPEAV------K 205

                       250
                ....*....|..
gi 29242797 264 DVLDLMDCCDTG 275
Cdd:cd07652 206 DLFDLILEIDAA 217
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 2-196 6.72e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 6.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797      2 AAHGKLRRERGLQ------AEYETQVKEMRWQLSEQLRCLELQGELRRELLQELAEFMRRRAEVElEYSRGLEKL---AE 72
Cdd:TIGR00618  277 AVLEETQERINRArkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLhsqEI 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29242797     73 RFSSRGGRLGSSREHqsFRKEPSLLSPLHCWAVLLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDvgrlvkksRDLEQQ 152
Cdd:TIGR00618  356 HIRDAHEVATSIREI--SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF--------RDLQGQ 425

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 29242797    153 LQdeLLEVVSELQTAKKTYQAYHMESVNAEAKLREAERQEEKRA 196
Cdd:TIGR00618  426 LA--HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
 
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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