Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111154099  559 KQEMTKQKIEYESRIKSLEQrnltlETEMMslHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQF 632
Cdd:pfam20492   1 REEAEREKQELEERLKQYEE-----ETKKA--QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67

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 111154099    60 PMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFD-SNTDVHTVASLLKLYLRELPEPVIPYAKYEDF 138
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDlSEYDVHDVAGLLKLFLRELPEPLITYELYEEF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099   139 LSCAKLLSKEEeaGVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKVEDPLTIMEgT 218
Cdd:smart00324  84 IEAAKLEDETE--RLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-I 160

                          170
                   ....*....|....
gi 111154099   219 VVVQQLMSVMISKH 232
Cdd:smart00324 161 RHQNTVIEFLIENA 174

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111154099  559 KQEMTKQKIEYESRIKSLEQrnltlETEMMslHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQF 632
Cdd:pfam20492   1 REEAEREKQELEERLKQYEE-----ETKKA--QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67

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 111154099  60 PMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVIPYAKYEDFL 139
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 140 SCAKLLSKEEeaGVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKVEDPLTIMEgTV 219
Cdd:cd00159   81 ELAKIEDEEE--RIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLED-IK 157

                        170
                 ....*....|.
gi 111154099 220 VVQQLMSVMIS 230
Cdd:cd00159  158 KLNEIVEFLIE 168

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099   60 PMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFD-SNTDVHTVASLLKLYLRELPEPVIPYAKYEDF 138
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDlEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099  139 LSCAKLLSKEEeaGVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKV 208
Cdd:pfam00620  81 IEAAKLPDEEE--RLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. 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 111154099  37 KGIFGQKLEDTVryeKRYGNRLApMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCG--EKPSFDSNTDVHTV 114
Cdd:cd04386    2 KPVFGTPLEEHL---KRTGREIA-LPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfSLPLDEFYSDPHAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 115 ASLLKLYLRELPEPVIPYAKYEDFLSCAKLLSKEEEagVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQN 194
Cdd:cd04386   78 ASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDER--LQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 111154099 195 LATVFGPNILRPKVEDPLTIME--GTVVVQQLMSVMISKHDCLFPKDA 240
Cdd:cd04386  156 IAIVLAPNLLWAKNEGSLAEMAagTSVHVVAIVELIISHADWFFPGEV 203

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 111154099  56 NRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCG--EKPSFDSN-TDVHTVASLLKLYLRELPEPVIPY 132
Cdd:cd04395   15 NPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGgfDIDLQDPRwRDVNVVSSLLKSFFRKLPEPLFTN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 133 AKYEDFLSCAKLLSKEEEagVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKvEDPL 212
Cdd:cd04395   95 ELYPDFIEANRIEDPVER--LKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRTS-DDNM 171

                        170       180
                 ....*....|....*....|....*
gi 111154099 213 TIMEGTVVVQ-QLMSVMISKHDCLF 236
Cdd:cd04395  172 ETMVTHMPDQcKIVETLIQHYDWFF 196

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099  40 FGQKLEDTVRYEkrygNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEK-----PSFDSNTDVHTV 114
Cdd:cd04398    1 FGVPLEDLILRE----GDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLnvlliSPEDYESDIHSV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 115 ASLLKLYLRELPEPVIPYAKYEDFLSCAKllSKEEEAGVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQN 194
Cdd:cd04398   77 ASLLKLFFRELPEPLLTKALSREFIEAAK--IEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNN 154

                        170
                 ....*....|
gi 111154099 195 LATVFGPNIL 204
Cdd:cd04398  155 LAIIWGPTLM 164

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. 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 111154099  39 IFGQKLEDTVRYE-KRYGNRLAPMLVEQCVDFI-RQRGLKEEGLFRLPGQANLVKELQDAFDC-GEKPSFDSNT--DVHT 113
Cdd:cd04400    1 IFGSPLEEAVELSsHKYNGRDLPSVVYRCIEYLdKNRAIYEEGIFRLSGSASVIKQLKERFNTeYDVDLFSSSLypDVHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 114 VASLLKLYLRELPEPVIPYAKYEDFLSCAKLLSKEEEAgVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQ 193
Cdd:cd04400   81 VAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRSQR-ALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLR 159

                        170
                 ....*....|..
gi 111154099 194 NLATVFGP--NI 203
Cdd:cd04400  160 NVCIVFSPtlNI 171

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 111154099  40 FGQKLED-TVRYEKRYGNRLAPMLVEQCVDFIRQ-RGLKEEGLFRLPGQANLVKELQDAFDCGEKPsfDSNT-DVHTVAS 116
Cdd:cd04389    1 FGSSLEEiMDRQKEKYPELKLPWILTFLSEKVLAlGGFQTEGIFRVPGDIDEVNELKLRVDQWDYP--LSGLeDPHVPAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 117 LLKLYLRELPEPVIPYAKYEDFLScakllSKEEEAGVKELakqVKSLPVVNYNLLKYICRFLDEV--QSYSGVNKMSVQN 194
Cdd:cd04389   79 LLKLWLRELEEPLIPDALYQQCIS-----ASEDPDKAVEI---VQKLPIINRLVLCYLINFLQVFaqPENVAHTKMDVSN 150

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 111154099 195 LATVFGPNILRPKVEDPLTIMEGTVVVQQLMSVMI 229
Cdd:cd04389  151 LAMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099  38 GIFGQKLEDTVRYEkrygNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFD--SNTDVHTVA 115
Cdd:cd04383    1 KLFNGSLEEYIQDS----GQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADdqNDHDINSVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 116 SLLKLYLRELPEPVIPYAKYEDFLSCAKLLSKEEEagVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNL 195
Cdd:cd04383   77 GVLKLYFRGLENPLFPKERFEDLMSCVKLENPTER--VHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNL 154

                        170
                 ....*....|....*..
gi 111154099 196 ATVFGPNILR-PKVEDP 211
Cdd:cd04383  155 AICFGPTLMPvPEGQDQ 171

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 111154099  56 NRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVIPYAKY 135
Cdd:cd04377   12 DRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRELPEPLMTFELY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 136 EDFLSCAKLLSKEEEagVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILR-PKVEDPLTI 214
Cdd:cd04377   92 ENFLRAMELEEKQER--VRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRcPDTADPLQS 169

                 ..
gi 111154099 215 ME 216
Cdd:cd04377  170 LQ 171

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099  58 LAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKP--SFDSNTDVHTVASLLKLYLRELPEPVIP---Y 132
Cdd:cd04387   15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDvsVMLSEMDVNAIAGTLKLYFRELPEPLFTdelY 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111154099 133 AKYEDFLSCAKLLSKEEEagvkeLAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKVED 210
Cdd:cd04387   95 PNFAEGIALSDPVAKESC-----MLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKE 167

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 111154099  60 PMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVIPYAKYEDFL 139
Cdd:cd04378   17 PFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYNDFI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 140 SCAKLLSKEEEAG---------------VKELAKQvksLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNIL 204
Cdd:cd04378   97 ALAKEIQRDTEEDkapntpievnriirkLKDLLRQ---LPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLI 173

                 ....*.
gi 111154099 205 RPKVED 210
Cdd:cd04378  174 RPRPGD 179

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). 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 111154099  39 IFGQKLEDtvrYEKRYGNRLaPMLVEQCVDFIRQRGLKEeGLFRLPGQANLVKELQDAFDCGEKP---SFDSNTDVHTVA 115
Cdd:cd04384    2 VFGCDLTE---HLLNSGQDV-PQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIPdltKDVYIQDIHSVS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 116 SLLKLYLRELPEPVIPYAKYEDFLSCAKLLSKEEEagVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNL 195
Cdd:cd04384   77 SLCKLYFRELPNPLLTYQLYEKFSEAVSAASDEER--LEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNL 154

                        170
                 ....*....|..
gi 111154099 196 ATVFGPNILRPK 207
Cdd:cd04384  155 AIVWAPNLLRSK 166

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. 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 111154099  65 QCVDFIRQRGLKEEGLFRLPGQ----ANLVKELQDAFDCGEkpSFDSNTDVHTVASLLKLYLRELPEPVIPYAKYEDFLS 140
Cdd:cd04380   56 RLVDYLYTRGLAQEGLFEEPGLpsepGELLAEIRDALDTGS--PFNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLE 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 111154099 141 CAKLLSkeeeagvkELAKQV--KSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKVEDP 211
Cdd:cd04380  134 AVANNE--------EDKRQVirISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAG 198

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 111154099  52 KRYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQA----NLVKELQDAFDCGEKPsFDSNTdVHTVASLLKLYLRELPE 127
Cdd:cd04391   15 KKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAqrvkFLCQELEAKFYEGTFL-WDQVK-QHDAASLLKLFIRELPQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 128 PVIPYAKYEDFLSCAKLLSKEEEagVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPK 207
Cdd:cd04391   93 PLLTVEYLPAFYSVQGLPSKKDQ--LQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMIMAPNLFPPR 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 111154099 208 VEDPLTI------MEGTVVVQQLMSVMISKHDCLF--PKDAELQSK 245
Cdd:cd04391  171 GKHSKDNeslqeeVNMAAGCANIMRLLIRYQDLLWtvPSFLINQVR 216

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). 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. 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 111154099  53 RYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVIPY 132
Cdd:cd04408   10 RDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 133 AKYEDFLSCAKLLSKEEEAGVK------ELAKQVKSL----PVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPN 202
Cdd:cd04408   90 QLYDDFIALAKELQRDSEKAAEspsiveNIIRSLKELlgrlPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPT 169

                 ....
gi 111154099 203 ILRP 206
Cdd:cd04408  170 LLRP 173

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. 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 111154099  60 PMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCG--EKPSFDSNTDVHtVASLLKLYLRELPEPVIPYAKYED 137
Cdd:cd04397   28 PALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNptEVPDLSKENPVQ-LAALLKKFLRELPDPLLTFKLYRL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111154099 138 FLSCAKLLSKEEEAGVKELAkqVKSLPVVNYNLLKYICRFLDEVQSYSGV-----NKMSVQNLATVFGPNILRPKVEDPL 212
Cdd:cd04397  107 WISSQKIEDEEERKRVLHLV--YCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKMDIHNLATVITPNILYSKTDNPN 184

                        170       180
                 ....*....|....*....|....*....
gi 111154099 213 TImEGTVVVQQLMSVMISKHD--CLFPKD 239
Cdd:cd04397  185 TG-DEYFLAIEAVNYLIENNEefCEVPDE 212

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.