LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112548  24 CIKCWESVPSTSQVWFGGKCWHSDCFKCVNCNKKLdpSSEDFSQDDQKqIFCKLC 78
Cdd:cd08368   1 CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPL--GGDSFYEKDGK-PYCEKC 52

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 19112548 761 PTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSE-DISAVTSVFKQYLRNLPNPIITYDQYFPFI 839
Cdd:cd00159   1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDyDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 840 TAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSR-DVIDMTVKN 918
Cdd:cd00159  81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDeLLEDIKKLN 160

                ....*....
gi 19112548 919 YSLAFLIDH 927
Cdd:cd00159 161 EIVEFLIEN 169

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112548  24 CIKCWESVPSTSQVWFGGKCWHSDCFKCVNCNKKLdpSSEDFSQDDQKqIFCKLC 78
Cdd:cd08368   1 CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPL--GGDSFYEKDGK-PYCEKC 52

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 19112548     24 CIKCWESVPSTSQVW-FGGKCWHSDCFKCVNCNKKLdpsSEDFSQDDQKQIFCKLC 78
Cdd:smart00132   2 CAGCGKPIYGTERVLrALGKVWHPECFKCATCGKPL---SGDTFFEKDGKLYCKDC 54

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 19112548 761 PTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSE-DISAVTSVFKQYLRNLPNPIITYDQYFPFI 839
Cdd:cd00159   1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDyDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 840 TAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSR-DVIDMTVKN 918
Cdd:cd00159  81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDeLLEDIKKLN 160

                ....*....
gi 19112548 919 YSLAFLIDH 927
Cdd:cd00159 161 EIVEFLIEN 169

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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLR-NEDTVLDPSEDISAVTSVFKQYLRNLPNPIITYDQYFPF 838
Cdd:cd04377  15 VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDtDPDSVNLEDYPIHVITSVLKQWLRELPEPLMTFELYENF 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 839 ITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNS 908
Cdd:cd04377  95 LRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRCPDTA 164

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 19112548 759 RVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKI-VALLRNEDTVlDPSE----DISAVTSVFKQYLRNLPNPIITYD 833
Cdd:cd04372  15 QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVkMAFDRDGEKA-DISAtvypDINVITGALKLYFRDLPIPVITYD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 834 QYFPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDVI- 912
Cdd:cd04372  94 TYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALTTl 173

                       170       180
                ....*....|....*....|.
gi 19112548 913 -DMTVKNYSLAFLIDHVHEVF 932
Cdd:cd04372 174 nDMRYQILIVQLLITNEDVLF 194

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 19112548 759 RVPTLIVSCINFIESYGMDFEGLYR---KSGATSQMKKIVALLRNEDTVLDPS-EDISAVTSVFKQYLRNLPNPIITYDQ 834
Cdd:cd04395  17 YVPLIVEVCCNIVEARGLETVGIYRvpgNNAAISALQEELNRGGFDIDLQDPRwRDVNVVSSLLKSFFRKLPEPLFTNEL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 835 YFPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRD--VI 912
Cdd:cd04395  97 YPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRTSDDNMEtmVT 176

                ...
gi 19112548 913 DMT 915
Cdd:cd04395 177 HMP 179

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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDT--VLDPSE----DISAVTSVFKQYLRNLPNPIITYD 833
Cdd:cd04398  16 VPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLnvLLISPEdyesDIHSVASLLKLFFRELPEPLLTKA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 834 QYFPFITAANC--ASF-QDKLDGfimVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIrdPDNSRD 910
Cdd:cd04398  96 LSREFIEAAKIedESRrRDALHG---LINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWGPTLM--NAAPDN 170

                       170       180
                ....*....|....*....|..
gi 19112548 911 VIDMTVKNYSLAFLIDHVHEVF 932
Cdd:cd04398 171 AADMSFQSRVIETLLDNAYQIF 192

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 759 RVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTV-LDPS--EDISAVTSVFKQYLRNLPNPIITYDQY 835
Cdd:cd04403  15 TVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLdLDDSkwEDIHVITGALKLFFRELPEPLFPYSLF 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112548 836 FPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDV 911
Cdd:cd04403  95 NDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQETGNI 170

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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNE-DTVLDPSEDISAVTSVFKQYLRNLPNPIITYDQYFPF 838
Cdd:cd04406  15 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDaNSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEF 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 839 ITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNS 908
Cdd:cd04406  95 LRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRCPDTT 164

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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSE----DIsavTSVFKQYLRNLPNPIITYDQY 835
Cdd:cd04378  16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSElsphDI---SSVLKLFLRQLPEPLILFRLY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 836 FPFITAA------NCASFQDKLDGFIM--------VIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTL 901
Cdd:cd04378  93 NDFIALAkeiqrdTEEDKAPNTPIEVNriirklkdLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTL 172

                       170       180
                ....*....|....*....|....*....
gi 19112548 902 IRDPDNSRDVidmtvknySLAFLIDHVHE 930
Cdd:cd04378 173 IRPRPGDADV--------SLSSLVDYGYQ 193

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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLrNEDTVLDPSE---DISAVTSVFKQYLRNLPNPIITYDQYF 836
Cdd:cd04373  15 IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQF-DQDHNLDLVSkdfTVNAVAGALKSFFSELPDPLIPYSMHL 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 837 PFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRdPD 906
Cdd:cd04373  94 ELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR-PD 162

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 19112548 760 VPTLIVSCINFIESYGMDFE-GLYRKSGATSQMKKIVALLRNE---DTVLDPSE-DISAVTSVFKQYLRNLPNPIITYDQ 834
Cdd:cd04400  22 LPSVVYRCIEYLDKNRAIYEeGIFRLSGSASVIKQLKERFNTEydvDLFSSSLYpDVHTVAGLLKLYLRELPTLILGGEL 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112548 835 YFPFITAANC-ASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTL 901
Cdd:cd04400 102 HNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169

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 19112548 759 RVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALL--RNEDTVLDPSE-DISAVTSVFKQYLRNLPNPIITYDQY 835
Cdd:cd04387  15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFdtNNKDVSVMLSEmDVNAIAGTLKLYFRELPEPLFTDELY 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112548 836 FPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDV 911
Cdd:cd04387  95 PNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKESKI 170

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 19112548 760 VPTLIVSCINFIESYgMDFEGLYRKSGATSQMKKIVALLRNEDTVLDpSEDISAVTSVFKQYLRNLPNPIITYDQYFPFI 839
Cdd:cd04394  20 VPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEACLS-SALPCDVAGLLKQFFRELPEPLLPYDLHEALL 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112548 840 TAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTL 901
Cdd:cd04394  98 KAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNL 159

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 19112548 758 LRVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSE----DISAVTSVFKQYLRNLPNPIITYD 833
Cdd:cd04379  16 RDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEelypDINVITGVLKDYLRELPEPLITPQ 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112548 834 QYFPFITAANCASFQDKL---DGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLI 902
Cdd:cd04379  96 LYEMVLEALAVALPNDVQtntHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAVCFGPVLM 167

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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIV-ALLRNEDTVLDPSE--DISAVTSVFKQYLRNLPNPIITYDQYF 836
Cdd:cd04383  18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKnAFERGEDPLADDQNdhDINSVAGVLKLYFRGLENPLFPKERFE 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112548 837 PFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDV 911
Cdd:cd04383  98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPVPEGQDQV 172

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. 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 19112548 760 VPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSE----DISavtSVFKQYLRNLPNPIITYDQY 835
Cdd:cd04409  16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSElsphDIS---NVLKLYLRQLPEPLILFRLY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 836 FPFITAAN----------------------CASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNL 893
Cdd:cd04409  93 NEFIGLAKesqhvnetqeakknsdkkwpnmCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNL 172

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19112548 894 AVVFSPTLIRdPDNSrdviDMTVknySLAFLIDHVHE 930
Cdd:cd04409 173 GIIFGPTLIR-PRPT----DATV---SLSSLVDYPHQ 201

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 759 RVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLR---------NED--TVLDpsedisaVTSVFKQYLRNLPN 827
Cdd:cd04396  31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFStppdygksfDWDgyTVHD-------AASVLRRYLNNLPE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112548 828 PIITYDQY---------FPFITAANCASFQDKLDGFI--------MVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTS 890
Cdd:cd04396 104 PLVPLDLYeefrnplrkRPRILQYMKGRINEPLNTDIdqaikeyrDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTA 183

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19112548 891 KNLAVVFSPTLIRDPDNsrdviDMTVKNYSLA-----FLIDH 927
Cdd:cd04396 184 SNLAAIFQPGILSHPDH-----EMDPKEYKLSrlvveFLIEH 220