PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849  167 QLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIALESAVYNSGCLRVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVL 246
Cdd:cd06718     1 RRVELIKPPGKPLGFYIRDGNGVERVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLII 80

                  ....
gi 386766849  247 AIRQ 250
Cdd:cd06718    81 TVKP 84

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849   957 PIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEHvpDINVITGVLKDYLRELPEPLFTRCLFQ 1036
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEE--DVHVVASLLKLFLRELPEPLLTFELYE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766849  1037 MTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1105
Cdd:pfam00620   79 EFIEAAKL---PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLL 144

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849  167 QLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIALESAVYNSGCLRVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVL 246
Cdd:cd06718     1 RRVELIKPPGKPLGFYIRDGNGVERVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLII 80

                  ....
gi 386766849  247 AIRQ 250
Cdd:cd06718    81 TVKP 84

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849  793 LWIHLLAGRGLRTAPEGAagtatqgqTRDLYCVIECDRVHKARTVVRSGDLQFDWDESFELDLV--GNKQLDVLVYSWDP 870
Cdd:cd00030     1 LRVTVIEARNLPAKDLNG--------KSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEVWDKDR 72

                          90       100
                  ....*....|....*....|....
gi 386766849  871 QHRHKLCYRGAISLSSILRQSPLH 894
Cdd:cd00030    73 FSKDDFLGEVEIPLSELLDSGKEG 96

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849    795 IHLLAGRGLRTAPegaagtatQGQTRDLYCVIECD--RVHKARTVVRSGDLQFDWDESFELDLV--GNKQLDVLVYSWDP 870
Cdd:smart00239    4 VKIISARNLPPKD--------KGGKSDPYVKVSLDgdPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDKDR 75

                            90       100
                    ....*....|....*....|....*.
gi 386766849    871 QHRHKLCYRGAISLSSILRQSPLHQL 896
Cdd:smart00239   76 FGRDDFIGQVTIPLSDLLLGGRHEKL 101

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849  179 LGLYIREGNGadrtdGVFISRIALESAVYNSGcLRVGDEILAVNLVDVTHMSLDDVVIIMsiprrlvlairqrRGNRGTg 258
Cdd:COG0793    62 LGAELGEEDG-----KVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLL-------------RGKAGT- 121

                          90       100
                  ....*....|....*....|....*.
gi 386766849  259 spgpP---TLSRPEQKPPPVVVIKRD 281
Cdd:COG0793   122 ----KvtlTIKRPGEGEPITVTLTRA 143

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849   957 PIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEHvpDINVITGVLKDYLRELPEPLFTRCLFQ 1036
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEE--DVHVVASLLKLFLRELPEPLLTFELYE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766849  1037 MTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1105
Cdd:pfam00620   79 EFIEAAKL---PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLL 144

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 386766849  957 PIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEhvpDINVITGVLKDYLRELPEPLFTRCLFQ 1036
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDY---DVHDVASLLKLYLRELPEPLIPFELYD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1037 MTVDAlaVCLPDDPEGNAKLMlSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLMlHSASAQPGAD 1116
Cdd:cd00159    78 EFIEL--AKIEDEEERIEALK-ELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLL-RPPDSDDELL 153

                         170
                  ....*....|....*
gi 386766849 1117 IDHAQPIAVLKYLLQ 1131
Cdd:cd00159   154 EDIKKLNEIVEFLIE 168

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 386766849  935 FGADLETVVNRESknapgsAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEHVpDINVI 1014
Cdd:cd04387     1 FGVKISTVTKRER------SKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEM-DVNAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1015 TGVLKDYLRELPEPLFTRCLFQMTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQ 1094
Cdd:cd04387    74 AGTLKLYFRELPEPLFTDELYPNFAEGIAL---SDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLH 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 386766849 1095 ALATVMGPPLM--------LHSASAQPGADIDHAQPIAVLKYLLQ 1131
Cdd:cd04387   151 NLATVFGPTLLrpsekeskIPTNTMTDSWSLEVMSQVQVLLYFLQ 195

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 386766849  935 FGADLETVVNRESKNapgsapVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTP--EHVPDIN 1012
Cdd:cd04398     1 FGVPLEDLILREGDN------VPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISpeDYESDIH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1013 VITGVLKDYLRELPEPLFTRCLFQMTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMS 1092
Cdd:cd04398    75 SVASLLKLFFRELPEPLLTKALSREFIEAAKI---EDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMS 151

                         170       180
                  ....*....|....*....|....*...
gi 386766849 1093 AQALATVMGPPLMlhsasAQPGADIDHA 1120
Cdd:cd04398   152 VNNLAIIWGPTLM-----NAAPDNAADM 174

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 386766849  950 APGSAP-VPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFeRNSRAVELTPEHvpDINVITGVLKDYLRELPEP 1028
Cdd:cd04382    10 DPSTSPmIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKF-LRGKTVPNLSKV--DIHVICGCLKDFLRSLKEP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1029 LFTRCLFQMTVDalAVCLPDDPEGNAKLMLSILDcLPRANRATLVFLLDHLSlVVSNSERNKMSAQALATVMGPPLMLHS 1108
Cdd:cd04382    87 LITFALWKEFME--AAEILDEDNSRAALYQAISE-LPQPNRDTLAFLILHLQ-RVAQSPECKMDINNLARVFGPTIVGYS 162

                         170       180
                  ....*....|....*....|....*.
gi 386766849 1109 ASAQPGADI--DHAQPIAVLKYLLQI 1132
Cdd:cd04382   163 VPNPDPMTIlqDTVRQPRVVERLLEI 188

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 386766849  935 FGADLETVVNRESknapgsaPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELtpEHVPdINVI 1014
Cdd:cd04377     1 FGVSLSSLTSEDR-------SVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNL--EDYP-IHVI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1015 TGVLKDYLRELPEPLFTrclFQMTVDAL-AVCLPDDPEGNAKLMlSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1093
Cdd:cd04377    71 TSVLKQWLRELPEPLMT---FELYENFLrAMELEEKQERVRALY-SVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSA 146

                         170       180
                  ....*....|....*....|
gi 386766849 1094 QALATVMGPPLMLHSASAQP 1113
Cdd:cd04377   147 NALAIVFAPCILRCPDTADP 166

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 386766849  935 FGADLETVVNREsknapgsAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELtpEHVPdINVI 1014
Cdd:cd04407     1 FGVRVGSLTSNK-------TSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKL--ENYP-IHAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1015 TGVLKDYLRELPEPLFTrclFQMTVDAL-AVCLPDDPEGNAKLMlSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1093
Cdd:cd04407    71 TGLLKQWLRELPEPLMT---FAQYNDFLrAVELPEKQEQLQAIY-RVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSP 146

                         170       180
                  ....*....|....*....|
gi 386766849 1094 QALATVMGPPLMLHSASAQP 1113
Cdd:cd04407   147 NALAIVFAPCLLRCPDSSDP 166

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849  934 LFGADLETVVNRESKNAPGSApVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEHVpDINV 1013
Cdd:cd04391     1 LFGVPLSTLLERDQKKVPGSK-VPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDQV-KQHD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1014 ITGVLKDYLRELPEPLFTRCLFQMTVDALAvcLPDDPEGNAKLMLSILdCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1093
Cdd:cd04391    79 AASLLKLFIRELPQPLLTVEYLPAFYSVQG--LPSKKDQLQALNLLVL-LLPEANRDTLKALLEFLQKVVDHEEKNKMNL 155

                         170
                  ....*....|.
gi 386766849 1094 QALATVMGPPL 1104
Cdd:cd04391   156 WNVAMIMAPNL 166

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 386766849  935 FGADLETVVNreskNAPGSAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATkkrLLREAFERNSRAVELTPEHVPDINVI 1014
Cdd:cd04404     6 FGVSLQFLKE----KNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQ---VVKEVQQKYNMGEPVDFDQYEDVHLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1015 TGVLKDYLRELPEPLFTRCLFQMTVDALAVclpdDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQ 1094
Cdd:cd04404    79 AVILKTFLRELPEPLLTFDLYDDIVGFLNV----DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNS 154

                         170
                  ....*....|.
gi 386766849 1095 ALATVMGPPLM 1105
Cdd:cd04404   155 NLAVVFGPNLL 165

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 386766849  935 FGADLETVVNRESKNapgsapVPIVLRRCVEEVERRGLdIIGLYRLCGSATKKRLLREAFErNSRAVELT-PEHVPDINV 1013
Cdd:cd04384     3 FGCDLTEHLLNSGQD------VPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFD-SEQIPDLTkDVYIQDIHS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1014 ITGVLKDYLRELPEPLFTRCLFQMTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1093
Cdd:cd04384    75 VSSLCKLYFRELPNPLLTYQLYEKFSEAVSA---ASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHA 151

                         170
                  ....*....|..
gi 386766849 1094 QALATVMGPPLM 1105
Cdd:cd04384   152 KNLAIVWAPNLL 163

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 386766849  956 VPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTpEHVPdiNVITGVLKDYLRELPEPLFTRCLF 1035
Cdd:cd04408    16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLS-GHSP--HDITSVLKHFLKELPEPVLPFQLY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1036 QMTVdALAVCLPDDPEGNAKL----------MLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1105
Cdd:cd04408    93 DDFI-ALAKELQRDSEKAAESpsiveniirsLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLL 171

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 386766849  934 LFGADLETVVNRESKNAPGSaPVPIVLRRCVEEVE-RRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEHVPDIN 1012
Cdd:cd04400     1 IFGSPLEEAVELSSHKYNGR-DLPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFSSSLYPDVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1013 VITGVLKDYLRELPEPLFTRCL---FQMTVDalavcLPDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERN 1089
Cdd:cd04400    80 TVAGLLKLYLRELPTLILGGELhndFKRLVE-----ENHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVN 154

                         170
                  ....*....|....*
gi 386766849 1090 KMSAQALATVMGPPL 1104
Cdd:cd04400   155 KMNLRNVCIVFSPTL 169

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 386766849  935 FGADLETVVNReSKNAPGsAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFER--NSRAVELTPehvpdiN 1012
Cdd:cd04381     1 FGASLSLAVER-SRCHDG-IDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRreSPNLEEYEP------P 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1013 VITGVLKDYLRELPEPLFTRCLFQMTVDALAVclPDDPEGNAKLmLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMS 1092
Cdd:cd04381    73 TVASLLKQYLRELPEPLLTKELMPRFEEACGR--PTEAEREQEL-QRLLKELPECNRLLLAWLIVHMDHVIAQELETKMN 149

                         170
                  ....*....|..
gi 386766849 1093 AQALATVMGPPL 1104
Cdd:cd04381   150 IQNISIVLSPTV 161

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 386766849  934 LFGADLETVVNReskNAPGSApVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFErNSRAVELTPEhvPDINV 1013
Cdd:cd04393     2 VFGVPLQELQQA---GQPENG-VPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLD-SGEEVDLSKE--ADVCS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766849 1014 ITGVLKDYLRELPEPLFTRCLFQMTVDALAVCLPDDPEGNAklMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1093
Cdd:cd04393    75 AASLLRLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGRK--LRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTA 152