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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1351 FGKLMITSE--QGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVNAVATALKDFFS 1428
Cdd:cd04373    1 FGVPLANVVtsEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1429 KRLPPLFSKDIIKELEEIAGsrgvgnsklnvevKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDS 1508
Cdd:cd04373   81 ELPDPLIPYSMHLELVEAAK-------------INDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24642826 1509 KNLAICWWPTLIPIDFTDMGHFEqlrpyLEDIVQTMIDQFPYL 1551
Cdd:cd04373  148 ENLSICFWPTLMRPDFTSMEALS-----ATRIYQTIIETFIQQ 185

p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics. The RhoGAP-FF1 region contains the FF domain that has been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAPFF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826    254 ESAKSRKELLDTRSEAVTRLIRNQITDYHVLWSQGSKMLSQYREWNEFLNIFGHEAGQKLFRRHMKKLRDDHLNKKLHQY 333
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIRSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1351 FGKLMITSE--QGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVNAVATALKDFFS 1428
Cdd:cd04373    1 FGVPLANVVtsEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1429 KRLPPLFSKDIIKELEEIAGsrgvgnsklnvevKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDS 1508
Cdd:cd04373   81 ELPDPLIPYSMHLELVEAAK-------------INDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24642826 1509 KNLAICWWPTLIPIDFTDMGHFEqlrpyLEDIVQTMIDQFPYL 1551
Cdd:cd04373  148 ENLSICFWPTLMRPDFTSMEALS-----ATRIYQTIIETFIQQ 185

pseudoGTPase domain found in the family of p190RhoGAP; This family includes two p190RhoGAP proteins, A and B, which are Rho family GTPase-activating proteins (GAPs) that act as key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Rho family is one of five Ras superfamily subgroups (Ras, Rho, Rab, Ran and Arf). Each contains five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases consist of a GTPase fold lacking one or more of these G motifs. This model corresponds to the GTPase-like domain called pseudoGTPase domain that is located at the middle region of p190RhoGAP proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826  598 LNLLIVGSEHLASDLLNDIRICTGSkGEYIYENQTYYLNYRIANGDME----AFKAIDVYSSGLICVYSNQQSFETLKDN 673
Cdd:cd22207    1 LNLVLLGSDGLADELANEIRALCED-DEYELDGVVYSLDLRTIDGDVSlpqnSFQTTDFKPHGCLCVYSSRESLEYIKTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826  674 LERTLLCNLELEDK--FENLPIVLVYQPQ-DLKENEVEYLRNEGMRLSEMLHCDFIDHTQN--------HQKYVYDILNI 742
Cdd:cd22207   80 LEKTLLSDLEEEDKlpFQGLPIVLLFARDpSISEKEVSQLREEGQELADRLQCVFIDVPSSgeamgrkfHESQIDDALRS 159

                 ....*.
gi 24642826  743 VILSLK 748
Cdd:cd22207  160 LIESIK 165

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 24642826    1361 GEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVNAVATALKDFFSKrLP-PLFSKDI 1439
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRE-LPePLITYEL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826    1440 IKELEEIAgsrgvgnsKLNVEVKtdrscRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWWPTL 1519
Cdd:smart00324   80 YEEFIEAA--------KLEDETE-----RLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTL 146

                           170       180
                    ....*....|....*....|....*...
gi 24642826    1520 IPIDFTDMGhFEQLRPYLEDIVQTMIDQ 1547
Cdd:smart00324  147 LRPPDGEVA-SLKDIRHQNTVIEFLIEN 173

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826  148 DGFVVVFDVSpvpnrsVEKQVEFVQNVIATILKNKK---PLVLVTTKNDDAYELYV--REAEKISQRKDYKstvqLIETS 222
Cdd:cd00154   74 HGAILVYDVT------NRESFENLDKWLNELKEYAPpniPIILVGNKSDLEDERQVstEEAQQFAKENGLL----FFETS 143

                         90
                 ....*....|....*.
gi 24642826  223 AHESINIDLAFLLLAQ 238
Cdd:cd00154  144 AKTGENVDEAFESLAR 159

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826    148 DGFVVVFDVSpvpNR-SVEKqvefVQNVIATILKNKK---PLVLVTTKNDDAYELYVR--EAEKISQRKDykstVQLIET 221
Cdd:pfam00071   73 DGFLLVYDIT---SRdSFEN----VKKWVEEILRHADenvPIVLVGNKCDLEDQRVVSteEGEALAKELG----LPFMET 141

                           90
                   ....*....|....*....
gi 24642826    222 SAHESINIDLAFLLLAQMI 240
Cdd:pfam00071  142 SAKTNENVEEAFEELAREI 160

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1351 FGKLMITSE--QGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVNAVATALKDFFS 1428
Cdd:cd04373    1 FGVPLANVVtsEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1429 KRLPPLFSKDIIKELEEIAGsrgvgnsklnvevKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDS 1508
Cdd:cd04373   81 ELPDPLIPYSMHLELVEAAK-------------INDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24642826 1509 KNLAICWWPTLIPIDFTDMGHFEqlrpyLEDIVQTMIDQFPYL 1551
Cdd:cd04373  148 ENLSICFWPTLMRPDFTSMEALS-----ATRIYQTIIETFIQQ 185

pseudoGTPase domain found in the family of p190RhoGAP; This family includes two p190RhoGAP proteins, A and B, which are Rho family GTPase-activating proteins (GAPs) that act as key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Rho family is one of five Ras superfamily subgroups (Ras, Rho, Rab, Ran and Arf). Each contains five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases consist of a GTPase fold lacking one or more of these G motifs. This model corresponds to the GTPase-like domain called pseudoGTPase domain that is located at the middle region of p190RhoGAP proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826  598 LNLLIVGSEHLASDLLNDIRICTGSkGEYIYENQTYYLNYRIANGDME----AFKAIDVYSSGLICVYSNQQSFETLKDN 673
Cdd:cd22207    1 LNLVLLGSDGLADELANEIRALCED-DEYELDGVVYSLDLRTIDGDVSlpqnSFQTTDFKPHGCLCVYSSRESLEYIKTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826  674 LERTLLCNLELEDK--FENLPIVLVYQPQ-DLKENEVEYLRNEGMRLSEMLHCDFIDHTQN--------HQKYVYDILNI 742
Cdd:cd22207   80 LEKTLLSDLEEEDKlpFQGLPIVLLFARDpSISEKEVSQLREEGQELADRLQCVFIDVPSSgeamgrkfHESQIDDALRS 159

                 ....*.
gi 24642826  743 VILSLK 748
Cdd:cd22207  160 LIESIK 165

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 24642826    1361 GEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVNAVATALKDFFSKrLP-PLFSKDI 1439
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRE-LPePLITYEL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826    1440 IKELEEIAgsrgvgnsKLNVEVKtdrscRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWWPTL 1519
Cdd:smart00324   80 YEEFIEAA--------KLEDETE-----RLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTL 146

                           170       180
                    ....*....|....*....|....*...
gi 24642826    1520 IPIDFTDMGhFEQLRPYLEDIVQTMIDQ 1547
Cdd:smart00324  147 LRPPDGEVA-SLKDIRHQNTVIEFLIEN 173

p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics. The RhoGAP-FF1 region contains the FF domain that has been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAPFF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826    254 ESAKSRKELLDTRSEAVTRLIRNQITDYHVLWSQGSKMLSQYREWNEFLNIFGHEAGQKLFRRHMKKLRDDHLNKKLHQY 333
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIRSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80

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 24642826 1363 IPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLfqrfEEDTNTEIDALDI------PVNAVATALKDFFSKRLPPLFS 1436
Cdd:cd04395   18 VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISAL----QEELNRGGFDIDLqdprwrDVNVVSSLLKSFFRKLPEPLFT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1437 KDIIKELeeIAGSRgvgnsklnvevKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWW 1516
Cdd:cd04395   94 NELYPDF--IEANR-----------IEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFG 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24642826 1517 PTLIPIDFTDMGHFEQLRPYLEDIVQTMIDQFPYLF 1552
Cdd:cd04395  161 PTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF 196

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 24642826 1355 MITSEQGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTN-TEIDALDIP-VNAVATALKDFFsKRLP 1432
Cdd:cd04372    8 LVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEkADISATVYPdINVITGALKLYF-RDLP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1433 -PLFSKDiikeleeiAGSRGVGNSKLnvevkTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNL 1511
Cdd:cd04372   87 iPVITYD--------TYPKFIDAAKI-----SNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24642826 1512 AICWWPTLI-PIDFTDMGHFEQLRpYLEDIVQTMIDQFPYLF 1552
Cdd:cd04372  154 GIVFGPTLMrPPEDSALTTLNDMR-YQILIVQLLITNEDVLF 194

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 24642826 1362 EIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDML---FQRFEEDTNTEIDALDIpvNAVATALKDFFSKRLPPLFSKD 1438
Cdd:cd04383   17 AIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIknaFERGEDPLADDQNDHDI--NSVAGVLKLYFRGLENPLFPKE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1439 IIKELEEIAgsrgvgnsklNVEVKTDRSCRLialKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWWPT 1518
Cdd:cd04383   95 RFEDLMSCV----------KLENPTERVHQI---REILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPT 161

                 ....
gi 24642826 1519 LIPI 1522
Cdd:cd04383  162 LMPV 165

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 24642826 1362 EIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVnaVATALKDFFsKRLP-PLFSKDII 1440
Cdd:cd04381   19 DLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYEPPT--VASLLKQYL-RELPePLLTKELM 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24642826 1441 KELEEIAGsrgvgnsklnvevKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWWPTL 1519
Cdd:cd04381   96 PRFEEACG-------------RPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPTV 161

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 24642826 1362 EIPIFLNKCVEFIEKEGLdSEGIYRVPGSRAHVDMLFQRFEE----DTNTEIDALDIpvNAVATALKDFFsKRLP-PLFS 1436
Cdd:cd04384   17 DVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSeqipDLTKDVYIQDI--HSVSSLCKLYF-RELPnPLLT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1437 KDIIKELEEIagsrgvgnsklnVEVKTDrSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWW 1516
Cdd:cd04384   93 YQLYEKFSEA------------VSAASD-EERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24642826 1517 PTLIPIDFTDMGHFEQLRPYLEDIVQTMIDQF 1548
Cdd:cd04384  160 PNLLRSKQIESACFSGTAAFMEVRIQSVVVEF 191

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. 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 24642826 1358 SEQGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDT-NTEIDALDIP-VNAVATALKDFFsKRLP-PL 1434
Cdd:cd04379   13 GESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSaAVELSEELYPdINVITGVLKDYL-RELPePL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1435 FSKDIIKELEEIagsrgvgnskLNVEVKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAIC 1514
Cdd:cd04379   92 ITPQLYEMVLEA----------LAVALPNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAVC 161

                 ....*..
gi 24642826 1515 WWPTLIP 1521
Cdd:cd04379  162 FGPVLMF 168

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 24642826 1360 QGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFeEDTNTEIDALDIPVNAVATALKDFFsKRLP-PL---- 1434
Cdd:cd04408   13 PEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAF-ENGRDLVDLSGHSPHDITSVLKHFL-KELPePVlpfq 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1435 -------FSKDIIKELEEIAGSRGVGNSKLNvevktdrscrliALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMD 1507
Cdd:cd04408   91 lyddfiaLAKELQRDSEKAAESPSIVENIIR------------SLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMS 158

                        170       180
                 ....*....|....*....|.
gi 24642826 1508 SKNLAICWWPTLI-PIDFTDM 1527
Cdd:cd04408  159 PNNLGIVFGPTLLrPLVGGDV 179

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 24642826 1362 EIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFE--EDTNTEIDAlDIPvnAVATALKdFFSKRLP-PLFSKD 1438
Cdd:cd04393   19 GVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDsgEEVDLSKEA-DVC--SAASLLR-LFLQELPeGLIPAS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1439 IIKELEEIAgSRGVGNsklnvevktDRSCRliALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWWPT 1518
Cdd:cd04393   95 LQIRLMQLY-QDYNGE---------DEFGR--KLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFGPD 162

                        170
                 ....*....|.
gi 24642826 1519 L--IPIDFTDM 1527
Cdd:cd04393  163 VfhVYTDVEDM 173

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 24642826 1359 EQGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFeeDTNTEiDAL----DIPVNAVATALKDFFSKRLPPL 1434
Cdd:cd04387   12 ERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAF--DTNNK-DVSvmlsEMDVNAIAGTLKLYFRELPEPL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642826 1435 FSKDIIKELEEiagsrGVGNSklnvevktDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAIC 1514
Cdd:cd04387   89 FTDELYPNFAE-----GIALS--------DPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATV 155