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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007  58 EENVDKRKKKVEELTMAQNLREASVDLDyfQTSCLHRVINAYGTVLHAEVDEKVKLEMAMERRVYEELAPFSEYE-KNVN 136
Cdd:cd07595   47 GEDKDKRLKKLPEYGLAQSMLESSKELP--DDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEiPNIQ 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 137 KLKDKLNLVSTDLEIAQKDLEKENSMTHQ-----------ESLDAIQMKYEGMKDALVTDIFaSSVSKEFQLNEHMLTSM 205
Cdd:cd07595  125 KQKKRLSKLVLDMDSARSRYNAAHKSSGGqgaaakvdalkDEYEEAELKLEQCRDALATDMY-EFLAKEAEIASYLIDLI 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392926007 206 NLKRDYFKKMYEMYEKAIPEVERMIATALPRPVFGVPLDEH 246
Cdd:cd07595  204 EAQREYHRTALSVLEAVLPELQEQIEQSPSKPVFGQPLEEH 244

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007  257 VLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQfDADEKHYNNDPHAVASTLKAYLRELPDPLTMDSLQSDWV 336
Cdd:pfam00620   3 IVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGP-DVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926007  337 EAINLEGE-ERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTM 397
Cdd:pfam00620  82 EAAKLPDEeERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTL 143

The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007  58 EENVDKRKKKVEELTMAQNLREASVDLDyfQTSCLHRVINAYGTVLHAEVDEKVKLEMAMERRVYEELAPFSEYE-KNVN 136
Cdd:cd07595   47 GEDKDKRLKKLPEYGLAQSMLESSKELP--DDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEiPNIQ 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 137 KLKDKLNLVSTDLEIAQKDLEKENSMTHQ-----------ESLDAIQMKYEGMKDALVTDIFaSSVSKEFQLNEHMLTSM 205
Cdd:cd07595  125 KQKKRLSKLVLDMDSARSRYNAAHKSSGGqgaaakvdalkDEYEEAELKLEQCRDALATDMY-EFLAKEAEIASYLIDLI 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392926007 206 NLKRDYFKKMYEMYEKAIPEVERMIATALPRPVFGVPLDEH 246
Cdd:cd07595  204 EAQREYHRTALSVLEAVLPELQEQIEQSPSKPVFGQPLEEH 244

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 257 VLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDADEKHYnnDPHAVASTLKAYLRELPDPLTMDSLQSDWV 336
Cdd:cd00159    3 IIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDY--DVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 337 EAINLE-GEERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTM-----TGMIYDGMNTHGV 410
Cdd:cd00159   81 ELAKIEdEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLlrppdSDDELLEDIKKLN 160

                 ....*....
gi 392926007 411 KLTEFMISN 419
Cdd:cd00159  161 EIVEFLIEN 169

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007   257 VLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQfDADEKHYNNDPHAVASTLKAYLRELPDPLTMDSLQSDWV 336
Cdd:smart00324   6 IVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGP-DPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEEFI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007   337 EAINLEGE-ERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTMTGMIYDGM-----NTHGV 410
Cdd:smart00324  85 EAAKLEDEtERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVaslkdIRHQN 164

                   ....*....
gi 392926007   411 KLTEFMISN 419
Cdd:smart00324 165 TVIEFLIEN 173

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 257 VLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAAL--DAGQFDADEKHYNndPHAVASTLKAYLRELPDPLTMDSLQSD 334
Cdd:cd04385   18 IVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQLREGEYT--VHDVADVLKRFLRDLPDPLLTSELHAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 335 WVEAINLE-GEERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTM--TGMIYDGMNTHGVK 411
Cdd:cd04385   96 WIEAAELEnKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLfqTDEHSVGQTSHEVK 175

                 ....*...
gi 392926007 412 LTEFMISN 419
Cdd:cd04385  176 VIEDLIDN 183

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 257 VLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQfDADEKHYNndPHAVASTLKAYLRELPDPLTMDSLQSDWV 336
Cdd:cd04402   18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGV-EVDLKAEP--VLLLASVLKDFLRNIPGSLLSSDLYEEWM 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 337 EAINLE-GEERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTM----TGMIYDGMNTHGV- 410
Cdd:cd04402   95 SALDQEnEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLlwppASSELQNEDLKKVt 174

                        170
                 ....*....|....
gi 392926007 411 KLTEFMISNGVRIF 424
Cdd:cd04402  175 SLVQFLIENCQEIF 188

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 238 VFGVPLDEHL-SIQKERISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDA---DEKHynNDPHAVAS 313
Cdd:cd04395    1 TFGVPLDDCPpSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIdlqDPRW--RDVNVVSS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 314 TLKAYLRELPDPLTMDSLQSDWVEAINLEG-EERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIV 392
Cdd:cd04395   79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDpVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 392926007 393 FAPT--------MTGMIYDgMnTHGVKLTEFMI 417
Cdd:cd04395  159 FGPTlvrtsddnMETMVTH-M-PDQCKIVETLI 189

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. 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 up several orders of magnitude.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 237 PVFGVPLDE--HLSIQKERISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDADEKhyNNDPHAVAST 314
Cdd:cd04393    1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSK--EADVCSAASL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 315 LKAYLRELPDPLTMDSLQSDWVEAI-NLEGEERF-SAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIV 392
Cdd:cd04393   79 LRLFLQELPEGLIPASLQIRLMQLYqDYNGEDEFgRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAV 158

                 ...
gi 392926007 393 FAP 395
Cdd:cd04393  159 FGP 161

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 239 FGVPLDEhLSIQKERISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAgqfDADEKHYNNDP-HAVASTLKA 317
Cdd:cd04377    1 FGVSLSS-LTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDT---DPDSVNLEDYPiHVITSVLKQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 318 YLRELPDPLTMDSLQSDWVEAINL-EGEERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLeAKREETS-MNASNLAIVFAP 395
Cdd:cd04377   77 WLRELPEPLMTFELYENFLRAMELeEKQERVRALYSVLEQLPRANLNTLERLIFHLVRV-ALQEEVNrMSANALAIVFAP 155

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 239 FGVPLDEHLSIQKERISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDADEKHYNNDPHAVASTLKAY 318
Cdd:cd04403    1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKWEDIHVITGALKLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 319 LRELPDPLTMDSLQSDWVEAINLEG-EERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTM 397
Cdd:cd04403   81 FRELPEPLFPYSLFNDFVAAIKLSDyEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 239 FGVPLdeHLSIQKER------ISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDADEKHynnDPHAVA 312
Cdd:cd04381    1 FGASL--SLAVERSRchdgidLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEY---EPPTVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 313 STLKAYLRELPDPLTMDSLQSDWVEAINLEGE-ERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAI 391
Cdd:cd04381   76 SLLKQYLRELPEPLLTKELMPRFEEACGRPTEaEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISI 155

                 ....*.
gi 392926007 392 VFAPTM 397
Cdd:cd04381  156 VLSPTV 161

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 239 FGVPLDEHLSIQKERISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDAD--EKHYNnDPHAVASTLK 316
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADisATVYP-DINVITGALK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 317 AYLRELPDPLTMDSLQSDWVEAINLEG-EERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAP 395
Cdd:cd04372   80 LYFRDLPIPVITYDTYPKFIDAAKISNpDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGP 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392926007 396 TMTG----MIYDGMN--THGVKLTEFMISNGVRIF 424
Cdd:cd04372  160 TLMRppedSALTTLNdmRYQILIVQLLITNEDVLF 194

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 239 FGVPLDEHLSIQKE-----RISGVLTKCCDFLRQ-NGMNERGIFRVSGNASKIKRIRAALDAGQFDADEKHynnDPHAVA 312
Cdd:cd04389    1 FGSSLEEIMDRQKEkypelKLPWILTFLSEKVLAlGGFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGLE---DPHVPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 313 STLKAYLRELPDPLTMDSLQSDWVEAinlegEERFSAIDRCLKKMTRGHRQNLIYLMKFL--CDLEAKREETSMNASNLA 390
Cdd:cd04389   78 SLLKLWLRELEEPLIPDALYQQCISA-----SEDPDKAVEIVQKLPIINRLVLCYLINFLqvFAQPENVAHTKMDVSNLA 152

                 ....*
gi 392926007 391 IVFAP 395
Cdd:cd04389  153 MVFAP 157

The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007  58 EENVDKRKKKVEELTMAQNLREASVDLDyfQTSCLHRVINAYGTVLHAEVDEKVKLEMAMERRVYEELAPFSEYE-KNVN 136
Cdd:cd07595   47 GEDKDKRLKKLPEYGLAQSMLESSKELP--DDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEiPNIQ 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 137 KLKDKLNLVSTDLEIAQKDLEKENSMTHQ-----------ESLDAIQMKYEGMKDALVTDIFaSSVSKEFQLNEHMLTSM 205
Cdd:cd07595  125 KQKKRLSKLVLDMDSARSRYNAAHKSSGGqgaaakvdalkDEYEEAELKLEQCRDALATDMY-EFLAKEAEIASYLIDLI 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392926007 206 NLKRDYFKKMYEMYEKAIPEVERMIATALPRPVFGVPLDEH 246
Cdd:cd07595  204 EAQREYHRTALSVLEAVLPELQEQIEQSPSKPVFGQPLEEH 244

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 239 FGVPLDEHLSIQKERISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAG--QFDADEKHynndPHAVASTLK 316
Cdd:cd04378    1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGkdLVELSELS----PHDISSVLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 317 AYLRELPDPLTMDSLQSDWV---------------EAINLEGEERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREE 381
Cdd:cd04378   77 LFLRQLPEPLILFRLYNDFIalakeiqrdteedkaPNTPIEVNRIIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392926007 382 TSMNASNLAIVFAPT------------MTGMIYDGmntHGVKLTEFMISN 419
Cdd:cd04378  157 NKMSPNNLGIVFGPTlirprpgdadvsLSSLVDYG---YQARLVEFLITN 203

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 238 VFGVPLDEHL-------SIQKE--------RISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAG-----QF 297
Cdd:cd04396    1 VFGVSLEESLkyasvaiSIVDEdgeqyvygYIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdygkSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 298 DADEkhYNndPHAVASTLKAYLRELPDPL------------------TMDSLQSDWVEAINLEGEERFSAIDRCLKKMTR 359
Cdd:cd04396   81 DWDG--YT--VHDAASVLRRYLNNLPEPLvpldlyeefrnplrkrprILQYMKGRINEPLNTDIDQAIKEYRDLITRLPN 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926007 360 GHRQNLIYLMKFLCDLEAKREETSMNASNLAIVFAPTMTGMIYDGMNTHGVKLT----EFMISN 419
Cdd:cd04396  157 LNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDHEMDPKEYKLSrlvvEFLIEH 220

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 253 RISGVLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDADekHYNNDPHAVASTLKAYLRELPDPLTMDSLQ 332
Cdd:cd04382   16 MIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPN--LSKVDIHVICGCLKDFLRSLKEPLITFALW 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926007 333 SDWVEAINLEGEERF-SAIDRCLKKMTRGHRQNLIYLMKFLCDLeAKREETSMNASNLAIVFAPTMTG 399
Cdd:cd04382   94 KEFMEAAEILDEDNSrAALYQAISELPQPNRDTLAFLILHLQRV-AQSPECKMDINNLARVFGPTIVG 160

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 238 VFGVPLDEHLSIQKERISG-----VLTKCCDFLRQNGMNERGIFRVSGNASKIKRIRAALDAGQFDADEKHYNNDPHAVA 312
Cdd:cd04391    1 LFGVPLSTLLERDQKKVPGskvplIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDQVKQHDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926007 313 STLKAYLRELPDPL-TMDSLQSdwveAINLEG----EERFSAIDRCLKKMTRGHRQNLIYLMKFLCDLEAKREETSMNAS 387
Cdd:cd04391   81 SLLKLFIRELPQPLlTVEYLPA----FYSVQGlpskKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLW 156

                        170
                 ....*....|
gi 392926007 388 NLAIVFAPTM 397
Cdd:cd04391  157 NVAMIMAPNL 166