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 1937273554  171 QLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIAIESAVSNSGCLKVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVL 250
Cdd:cd06718      1 RRVELIKPPGKPLGFYIRDGNGVERVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLII 80

                   ....
gi 1937273554  251 AIRQ 254
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 1937273554  935 PIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSPEHvpDINVITGVLKDYLRELPEPLFTRCLFQ 1014
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEE--DVHVVASLLKLFLRELPEPLLTFELYE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937273554 1015 MTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1083
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 1937273554  171 QLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIAIESAVSNSGCLKVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVL 250
Cdd:cd06718      1 RRVELIKPPGKPLGFYIRDGNGVERVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLII 80

                   ....
gi 1937273554  251 AIRQ 254
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 1937273554  766 LWIHLLAGRGLRSAPELGAQhvgggphgpapsrDLYCVIECDRVHKARTVVRSGDLQFDWDESFELDLV--GNKQLDVLV 843
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKS-------------DPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEV 67

                           90       100
                   ....*....|....*....|....*....
gi 1937273554  844 YSWDPQHRHKLCYRGAISLSTILRQSPLH 872
Cdd:cd00030     68 WDKDRFSKDDFLGEVEIPLSELLDSGKEG 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 1937273554   768 IHLLAGRGLRSAPELGaqhvgggphgpapSRDLYCVIECD--RVHKARTVVRSGDLQFDWDESFELDLV--GNKQLDVLV 843
Cdd:smart00239    4 VKIISARNLPPKDKGG-------------KSDPYVKVSLDgdPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEV 70

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1937273554   844 YSWDPQHRHKLCYRGAISLSTILRQSPLHQL 874
Cdd:smart00239   71 YDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937273554  183 LGLYIREGNGadrtdGVFISRIAIESAVSNSGcLKVGDEILAVNLVDVTHMSLDDVV 239
Cdd:COG0793     62 LGAELGEEDG-----KVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAV 112

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  935 PIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSPEHvpDINVITGVLKDYLRELPEPLFTRCLFQ 1014
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEE--DVHVVASLLKLFLRELPEPLLTFELYE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937273554 1015 MTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1083
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 1937273554  935 PIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSPEhvpDINVITGVLKDYLRELPEPLFTRCLFQ 1014
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDY---DVHDVASLLKLYLRELPEPLIPFELYD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554 1015 MTVDAlaVCLPDDPEGNAKLMlSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLMlHSASAQPGSD 1094
Cdd:cd00159     78 EFIEL--AKIEDEEERIEALK-ELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLL-RPPDSDDELL 153

                          170
                   ....*....|....*
gi 1937273554 1095 IDHAQPIAVLKYLLQ 1109
Cdd:cd00159    154 EDIKKLNEIVEFLIE 168

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 1937273554  171 QLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIAIESAVSNSGCLKVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVL 250
Cdd:cd06718      1 RRVELIKPPGKPLGFYIRDGNGVERVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLII 80

                   ....
gi 1937273554  251 AIRQ 254
Cdd:cd06718     81 TVKP 84

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 1937273554  913 FGADLETVVNRESkgapgsAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSPEHVPDINVI 992
Cdd:cd04372      1 YGCDLTTLVKAHN------TQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDINVI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  993 TGVLKDYLRELPEPLFTRCLFQMTVDALAVCLPDDpegNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQ 1072
Cdd:cd04372     75 TGALKLYFRDLPIPVITYDTYPKFIDAAKISNPDE---RLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAE 151

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1937273554 1073 ALATVMGPPLMLHSASAQPGSDIDHAQPIAVLKYLLQ 1109
Cdd:cd04372    152 NLGIVFGPTLMRPPEDSALTTLNDMRYQILIVQLLIT 188

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 1937273554  928 APGSAP-VPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSPEhvpDINVITGVLKDYLRELPEP 1006
Cdd:cd04382     10 DPSTSPmIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKV---DIHVICGCLKDFLRSLKEP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554 1007 LFTRCLFQMTVDalAVCLPDDPEGNAKLMLSILDcLPRANRATLVFLLDHLSlVVSNSERNKMSAQALATVMGPPLMLHS 1086
Cdd:cd04382     87 LITFALWKEFME--AAEILDEDNSRAALYQAISE-LPQPNRDTLAFLILHLQ-RVAQSPECKMDINNLARVFGPTIVGYS 162

                          170       180
                   ....*....|....*....|....*.
gi 1937273554 1087 ASAQPGSDI--DHAQPIAVLKYLLQI 1110
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 1937273554  913 FGADLETVVNRESkgapgsaPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELspEHVPdINVI 992
Cdd:cd04377      1 FGVSLSSLTSEDR-------SVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNL--EDYP-IHVI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  993 TGVLKDYLRELPEPLFTrclFQMTVDAL-AVCLPDDPEGNAKLMlSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1071
Cdd:cd04377     71 TSVLKQWLRELPEPLMT---FELYENFLrAMELEEKQERVRALY-SVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSA 146

                          170       180
                   ....*....|....*....|
gi 1937273554 1072 QALATVMGPPLMLHSASAQP 1091
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 1937273554  913 FGADLETVVNREskgapgsAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELspEHVPdINVI 992
Cdd:cd04407      1 FGVRVGSLTSNK-------TSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKL--ENYP-IHAI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  993 TGVLKDYLRELPEPLFTrclFQMTVDAL-AVCLPDDPEGNAKLMlSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1071
Cdd:cd04407     71 TGLLKQWLRELPEPLMT---FAQYNDFLrAVELPEKQEQLQAIY-RVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSP 146

                          170       180
                   ....*....|....*....|
gi 1937273554 1072 QALATVMGPPLMLHSASAQP 1091
Cdd:cd04407    147 NALAIVFAPCLLRCPDSSDP 166

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 1937273554  913 FGADLETVVNRESKGapgsapVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSPEHVPDinvI 992
Cdd:cd04409      1 FGADFAQVAKKSPDG------IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHD---I 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  993 TGVLKDYLRELPEPLFTRCLFQMTVDALAVCLPDDPEGNAKLMLS-------------------ILDCLPRANRATLVFL 1053
Cdd:cd04409     72 SNVLKLYLRQLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNSDkkwpnmctelnrillkskdLLRQLPAPNYNTLQFL 151

                          170       180       190
                   ....*....|....*....|....*....|
gi 1937273554 1054 LDHLSLVVSNSERNKMSAQALATVMGPPLM 1083
Cdd:cd04409    152 IVHLHRVSEQAEENKMSASNLGIIFGPTLI 181

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 1937273554  913 FGADLETVVNReskgAPGSAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATkkrLLREAFERNSRAVELSPEHVPDINVI 992
Cdd:cd04404      6 FGVSLQFLKEK----NPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQ---VVKEVQQKYNMGEPVDFDQYEDVHLP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  993 TGVLKDYLRELPEPLFTRCLFQMTVDALAVclpdDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQ 1072
Cdd:cd04404     79 AVILKTFLRELPEPLLTFDLYDDIVGFLNV----DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNS 154

                          170       180
                   ....*....|....*....|...
gi 1937273554 1073 ALATVMGPPLMLHSASAQPGSDI 1095
Cdd:cd04404    155 NLAVVFGPNLLWAKDASMSLSAI 177

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 1937273554  934 VPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELSpEHVPdiNVITGVLKDYLRELPEPLFTRCLF 1013
Cdd:cd04408     16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLS-GHSP--HDITSVLKHFLKELPEPVLPFQLY 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554 1014 QMTVdALAVCLPDDPEGNAKL----------MLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1083
Cdd:cd04408     93 DDFI-ALAKELQRDSEKAAESpsiveniirsLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLL 171

                          170
                   ....*....|..
gi 1937273554 1084 lhsaSAQPGSDI 1095
Cdd:cd04408    172 ----RPLVGGDV 179

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  913 FGADLETVVNRESKGapgsapVPIVLRRCVEEVERRGLdIIGLYRLCGSATKKRLLREAFERNSRAVELSPEHVPDINVI 992
Cdd:cd04384      3 FGCDLTEHLLNSGQD------VPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQDIHSV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  993 TGVLKDYLRELPEPLFTRCLFQMTVDALAVclpDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQ 1072
Cdd:cd04384     76 SSLCKLYFRELPNPLLTYQLYEKFSEAVSA---ASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAK 152

                          170
                   ....*....|.
gi 1937273554 1073 ALATVMGPPLM 1083
Cdd:cd04384    153 NLAIVWAPNLL 163

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. 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 1937273554  938 LRRCVEEVERRGLDIIGLYRLCGSATK-KRLLREAFERNSRA---VELSPEHVpDINVITGVLKDYLRELPEPLFTrclF 1013
Cdd:cd04374     32 VRKCIEAVETRGINEQGLYRVVGVNSKvQKLLSLGLDPKTSTpgdVDLDNSEW-EIKTITSALKTYLRNLPEPLMT---Y 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554 1014 QMTVDALAVCLPDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLM 1083
Cdd:cd04374    108 ELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLL 177

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 1937273554  912 LFGADLETVVNReskGAPGSApVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFErNSRAVELSPEhvPDINV 991
Cdd:cd04393      2 VFGVPLQELQQA---GQPENG-VPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLD-SGEEVDLSKE--ADVCS 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554  992 ITGVLKDYLRELPEPLFTRCLFQMTVDALAVCLPDDPEGNAklMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSA 1071
Cdd:cd04393     75 AASLLRLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGRK--LRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTA 152

                   ....*....
gi 1937273554 1072 QALATVMGP 1080
Cdd:cd04393    153 ENLAAVFGP 161

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 1937273554  934 VPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERnSRAVELSPEHVPdiNVITGVLKDYLRELPEPLFTRCLF 1013
Cdd:cd04376      9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDR-GIDVVLDENHSV--HDVAALLKEFFRDMPDPLLPRELY 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937273554 1014 QMTVDAlAVCLPDDPEGNAKLMLSIldcLPRANRATLVFLLDHLSLVVSNSER-----------NKMSAQALATVMGPPL 1082
Cdd:cd04376     86 TAFIGT-ALLEPDEQLEALQLLIYL---LPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNL 161