protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568915030  33 HAIWVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLK 87
Cdd:cd20857    6 HNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLK 60

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 568915030   109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISvnMYEDINIITGALKLYFRDLPIPLITYDAYP 188
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDL--SEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030   189 KFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDpMAALNDI 268
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE-VASLKDI 160

                          170
                   ....*....|....
gi 568915030   269 RYQRLVVELLIKNE 282
Cdd:smart00324 161 RHQNTVIEFLIENA 174

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568915030  33 HAIWVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLK 87
Cdd:cd20857    6 HNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLK 60

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568915030    33 HAIWVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDC 82
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50

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 568915030   109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISvnMYEDINIITGALKLYFRDLPIPLITYDAYP 188
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDL--SEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030   189 KFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDpMAALNDI 268
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE-VASLKDI 160

                          170
                   ....*....|....
gi 568915030   269 RYQRLVVELLIKNE 282
Cdd:smart00324 161 RHQNTVIEFLIENA 174

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISvnmYEDINIITGALKLYFRDLPIPLITYDAYP 188
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLE---DYDVHDVASLLKLYLRELPEPLIPFELYD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 189 KFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDpMAALNDI 268
Cdd:cd00159   78 EFIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSD-DELLEDI 156

                        170
                 ....*....|...
gi 568915030 269 RYQRLVVELLIKN 281
Cdd:cd00159  157 KKLNEIVEFLIEN 169

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKAD-ISVNMYE-DINIITGALKLYFRDLPIPLITYDA 186
Cdd:cd04398   17 PNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLlISPEDYEsDIHSVASLLKLFFRELPEPLLTKAL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 187 YPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDpmaaLN 266
Cdd:cd04398   97 SREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWGPTLMNAAPDN----AA 172

                        170       180
                 ....*....|....*....|
gi 568915030 267 DIRYQRLVVELLIKNEDILF 286
Cdd:cd04398  173 DMSFQSRVIETLLDNAYQIF 192

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDIniiTGALKLYFRDLPIPLITYDAYP 188
Cdd:cd04378   17 PFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDI---SSVLKLFLRQLPEPLILFRLYN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 189 KFI----ESAKIMDPDEQLET----------LHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLM 254
Cdd:cd04378   94 DFIalakEIQRDTEEDKAPNTpievnriirkLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLI 173

                        170       180       190
                 ....*....|....*....|....*....|
gi 568915030 255 RSPELD---PMAALNDIRYQRLVVELLIKN 281
Cdd:cd04378  174 RPRPGDadvSLSSLVDYGYQARLVEFLITN 203

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 568915030  97 LTTLVKAHITKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEkaDISVNMYE-DINIITGALKLYFR 175
Cdd:cd04387    5 ISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNK--DVSVMLSEmDVNAIAGTLKLYFR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 176 DLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMR 255
Cdd:cd04387   83 ELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLR 162

                 ....*
gi 568915030 256 SPELD 260
Cdd:cd04387  163 PSEKE 167

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEkADIsVNMYEDINIITGALKLYFRDLPIPLITYDAYP 188
Cdd:cd04373   16 PIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHN-LDL-VSKDFTVNAVAGALKSFFSELPDPLIPYSMHL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 189 KFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRsPELDPMAALNDI 268
Cdd:cd04373   94 ELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR-PDFTSMEALSAT 172

                        170
                 ....*....|...
gi 568915030 269 RYQRLVVELLIKN 281
Cdd:cd04373  173 RIYQTIIETFIQQ 185

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 568915030 106 TKRPMV---VDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVnmyEDINIITGALKLYFRDLPIPLI 182
Cdd:cd04382   12 STSPMIpalIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSK---VDIHVICGCLKDFLRSLKEPLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 183 TYDAYPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTlHEKENLMSAENLGIVFGPTLM--RSPELD 260
Cdd:cd04382   89 TFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLARVFGPTIVgySVPNPD 167

                        170       180
                 ....*....|....*....|
gi 568915030 261 PMAALNDIRYQRLVVELLIK 280
Cdd:cd04382  168 PMTILQDTVRQPRVVERLLE 187

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDIniiTGALKLYFRDLPIPLITYDAYP 188
Cdd:cd04408   17 PFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDI---TSVLKHFLKELPEPVLPFQLYD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 189 KFIESAKIM--DPDEQLET---LHEALRS-------LPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRS 256
Cdd:cd04408   94 DFIALAKELqrDSEKAAESpsiVENIIRSlkellgrLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRP 173

                        170       180
                 ....*....|....*....|....*..
gi 568915030 257 PELD--PMAALNDIRYQRLVVELLIKN 281
Cdd:cd04408  174 LVGGdvSMICLLDTGYQAQLVEFLISN 200

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 568915030  91 KVYSCDLTTLVKAHITKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRdGEKADISVNMYEDINIITGAL 170
Cdd:cd04383    1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFER-GEDPLADDQNDHDINSVAGVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 171 KLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFG 250
Cdd:cd04383   80 KLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFG 159

                 ....*...
gi 568915030 251 PTLMRSPE 258
Cdd:cd04383  160 PTLMPVPE 167

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP 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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADIsvnmyED--INIITGALKLYFRDLPIPLITYDA 186
Cdd:cd04407   16 PIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKL-----ENypIHAITGLLKQWLRELPEPLMTFAQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 187 YPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPE-LDPMAAL 265
Cdd:cd04407   91 YNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRCPDsSDPLTSM 170

                        170
                 ....*....|....*
gi 568915030 266 NDIRYQRLVVELLIK 280
Cdd:cd04407  171 KDVAKTTTCVEMLIK 185

protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; Alpha-chimaerin, also called A-chimaerin, N-chimaerin (CHN), alpha-chimerin, N-chimerin (NC), or Rho GTPase-activating protein 2 (ARHGAP2), is a GTPase-activating protein (GAP) for p21-rac and a phorbol ester receptor. It is involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance. Alpha-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568915030  33 HAIWVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKP 84
Cdd:cd20856    6 HNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKP 57

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. 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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRdGEkaDISVNMYEDINIITGALKLYFRDLPIPLITYDAYP 188
Cdd:cd04404   24 PPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNM-GE--PVDFDQYEDVHLPAVILKTFLRELPEPLLTFDLYD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 189 KFIESAKImDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELD-PMAALND 267
Cdd:cd04404  101 DIVGFLNV-DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPNLLWAKDASmSLSAINP 179

                        170
                 ....*....|....*....
gi 568915030 268 IryqRLVVELLIKNEDILF 286
Cdd:cd04404  180 I---NTFTKFLLDHQDEIF 195

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP 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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEkadiSVNMYE-DINIITGALKLYFRDLPIPLITYDAY 187
Cdd:cd04406   16 PLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAN----SVNLDDyNIHVIASVFKQWLRDLPNPLMTFELY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 188 PKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPE-LDPMAALN 266
Cdd:cd04406   92 EEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRCPDtTDPLQSVQ 171

                        170
                 ....*....|...
gi 568915030 267 DIRYQRLVVELLI 279
Cdd:cd04406  172 DISKTTTCVELIV 184

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. 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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEkadisVNMYEDINI--ITGALKLYFRDLPIPLITYDA 186
Cdd:cd04376   10 PRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGID-----VVLDENHSVhdVAALLKEFFRDMPDPLLPREL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 187 YPKFIESAKiMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKE-----------NLMSAENLGIVFGPTLMR 255
Cdd:cd04376   85 YTAFIGTAL-LEPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLH 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568915030 256 -----SPELDPMAA-LNDIRYQRLVVELLIKNEDILF 286
Cdd:cd04376  164 kqksgEREFVQASLrIEESTAIINVVQTMIDNYEELF 200

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGekadiSVNMYE-DINIITGALKLYFRDLPIPLITYDAY 187
Cdd:cd04381   21 PLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRE-----SPNLEEyEPPTVASLLKQYLRELPEPLLTKELM 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915030 188 PKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPEL 259
Cdd:cd04381   96 PRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPTVQISNRL 167

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 568915030 109 PMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDrDGEKADISVNmyEDINIITGALKLYFRDLPIPLITYDAYP 188
Cdd:cd04393   21 PAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLD-SGEEVDLSKE--ADVCSAASLLRLFLQELPEGLIPASLQI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915030 189 KFIE-SAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMR-SPELDPMAALN 266
Cdd:cd04393   98 RLMQlYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFGPDVFHvYTDVEDMKEQE 177

                        170
                 ....*....|..
gi 568915030 267 DIryQRLVVELL 278
Cdd:cd04393  178 IC--SRIMAKLL 187

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A 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 568915030 110 MVVDMCiREIESRgLNSEGLYRVSGFSDLIEDVKMAFDrDGEKADISVNMYEdiniITGALKLYFRDLPIPLITYDAYPK 189
Cdd:cd04394   23 FLVDAC-TFLLDH-LSTEGLFRKSGSVVRQKELKAKLE-GGEACLSSALPCD----VAGLLKQFFRELPEPLLPYDLHEA 95