ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  596 RREGWLYYKQILTKKGKKAGsgLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAgedeaaPVCIGSCLVDISYSE 675
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVS--DRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQ------RISIRGCIVDIAYSY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767995434  676 TKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENSRAE 716
Cdd:cd01253    73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE 113

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434   77 GNEPYSGEARSIPEPPPICYPRKTYAPPARAStRATMVPEPTSALPSDPRSPAAWSDPGlRVPPAARAHLDNSSLGMSQP 156
Cdd:PHA03247 2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP-AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  157 --RPSPGAFP----HLSSEPRTPRAFPEPGSRVPPSrlecQQALSHWLSNQVPRRAGERRCPAMAPRArSASQDRLEEVA 230
Cdd:PHA03247 2680 pqRPRRRAARptvgSLTSLADPPPPPPTPEPAPHAL----VSATPLPPGPAAARQASPALPAAPAPPA-VPAGPATPGGP 2754

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  231 APRPWPCSTSQDALSQLGqegwhRARSDDYLSRATRSAEA-LGPGALVSPRFERCGWASQRSSARTPACPTRDLP-GPQA 308
Cdd:PHA03247 2755 ARPARPPTTAGPPAPAPP-----AAPAAGPPRRLTRPAVAsLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLP 2829

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  309 PPPSGLQGLDDLGYIGYRSYSP---------SFQRRTGLLHALSF----RDSPFGGLPTFNLAQSPASFPPEASEPPRVV 375
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRPPSRSPAAKpaapARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  376 RPEPSTRALEPPAEDRGDEVVLRQKPPTGRKVQLTPARQMNLGFGDESPEPEASGRGERLGRKVAPLATTEDSLASIPFI 455
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP 2989

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 767995434  456 DEPTSPSidlqaKHVPASAVVSSAMNSAPVLGTSPSSPTFTFTL 499
Cdd:PHA03247 2990 ASSTPPL-----TGHSLSRVSSWASSLALHEETDPPPVSLKQTL 3028

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434    823 QRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDInlQDERWQDLNVISSLLKSFFRKLPEPLFTDD 902
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPD--LDLSEYDVHDVAGLLKLFLRELPEPLITYE 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434    903 KYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMv 982
Cdd:smart00324   79 LYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASL- 157

                           170
                    ....*....|....*..
gi 767995434    983 THMPDRYKIVETLIQHS 999
Cdd:smart00324  158 KDIRHQNTVIEFLIENA 174

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  596 RREGWLYYKQILTKKGKKAGsgLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAgedeaaPVCIGSCLVDISYSE 675
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVS--DRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQ------RISIRGCIVDIAYSY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767995434  676 TKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENSRAE 716
Cdd:cd01253    73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE 113

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 767995434      4 IFVKNVKEDGPAHRAGLRTGDRLVKVNGESVIGKTYSQVIALIQNSDDTLELSIMPKD 61
Cdd:smart00228   28 VVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434    595 IRREGWLYykqiltkkgKKAGSGLRQWKRVYAALRARSLSLSKERrepgpaaagaaAAGAGEDEAAPVCIGSCLVDI--S 672
Cdd:smart00233    1 VIKEGWLY---------KKSGGGKKSWKKRYFVLFNSTLLYYKSK-----------KDKKSYKPKGSIDLSGCTVREapD 60

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767995434    673 YSETKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRE 711
Cdd:smart00233   61 PDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRK 99

PDZ domain; PDZ domains are found in diverse signaling proteins.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767995434     3 TIFVKNVKEDGPAHRAGLRTGDRLVKVNGESVIGKTYSQVIALIQNSDDTLELSIM 58
Cdd:pfam00595   26 GIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81

sigma E protease regulator RseP;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434    6 VKNVKEDGPAHRAGLRTGDRLVKVNGESvIGKTYSQVIALIQNSDDTLELSImPKDEDILQLAYSQDAYlKGNEPYSGEA 85
Cdd:PRK10779  225 LAEVQPNSAASKAGLQAGDRIVKVDGQP-LTQWQTFVTLVRDNPGKPLALEI-ERQGSPLSLTLTPDSK-PGNGKAEGFA 301

                          90
                  ....*....|
gi 767995434   86 RSIPE--PPP 93
Cdd:PRK10779  302 GVVPKviPLP 311

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434    823 QRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDInlQDERWQDLNVISSLLKSFFRKLPEPLFTDD 902
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPD--LDLSEYDVHDVAGLLKLFLRELPEPLITYE 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434    903 KYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMv 982
Cdd:smart00324   79 LYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASL- 157

                           170
                    ....*....|....*..
gi 767995434    983 THMPDRYKIVETLIQHS 999
Cdd:smart00324  158 KDIRHQNTVIEFLIENA 174

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  826 PLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgdiNLQDERWQDLNVISSLLKSFFRKLPEPLFTDDKYN 905
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGE---DIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  906 DFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMvTHM 985
Cdd:cd00159    78 EFIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELL-EDI 156

                         170
                  ....*....|...
gi 767995434  986 PDRYKIVETLIQH 998
Cdd:cd00159   157 KKLNEIVEFLIEN 169

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  596 RREGWLYYKQILTKKGKKAGsgLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAgedeaaPVCIGSCLVDISYSE 675
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVS--DRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQ------RISIRGCIVDIAYSY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767995434  676 TKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENSRAE 716
Cdd:cd01253    73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE 113

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 767995434  821 ENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSLLKSFFRKLPEPLFT 900
Cdd:cd04372    12 HNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDINVITGALKLYFRDLPIPVIT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  901 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTD 980
Cdd:cd04372    92 YDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALT 171

                         170       180
                  ....*....|....*....|...
gi 767995434  981 MVTHMPDRYKIVETLIQHSDWFF 1003
Cdd:cd04372   172 TLNDMRYQILIVQLLITNEDVLF 194

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. 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 767995434  807 RAFGVRLEECQPATeNQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLqDERWQDLNVISSL 886
Cdd:cd04386     3 PVFGTPLEEHLKRT-GREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPL-DEFYSDPHAVASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  887 LKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVF 966
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767995434  967 GPTLV--RTSEDNMTDMVTHMPDRYKIVETLIQHSDWFFSDE 1006
Cdd:cd04386   161 APNLLwaKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGE 202

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 767995434  828 IVAACCRIVEARGLESTGIYRVPGnnaVVSSLQEQLNRG-------PGDINLQDERWqDLNVISSLLKSFFRKLPEPLFT 900
Cdd:cd04374    31 FVRKCIEAVETRGINEQGLYRVVG---VNSKVQKLLSLGldpktstPGDVDLDNSEW-EIKTITSALKTYLRNLPEPLMT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  901 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTD 980
Cdd:cd04374   107 YELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAA 186

                         170       180
                  ....*....|....*....|
gi 767995434  981 MvthMPDRYK--IVETLIQH 998
Cdd:cd04374   187 I---MDIKFQniVVEILIEN 203

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 767995434  809 FGVRLEECQP-ATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgDINLQDErwQDLNVISSLL 887
Cdd:cd04404     6 FGVSLQFLKEkNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGE-PVDFDQY--EDVHLPAVIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  888 KSFFRKLPEPLFTDDKYNDFIEANRIEDArERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 967
Cdd:cd04404    83 KTFLRELPEPLLTFDLYDDIVGFLNVDKE-ERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFG 161

                         170
                  ....*....|..
gi 767995434  968 PTLVRTSEDNMT 979
Cdd:cd04404   162 PNLLWAKDASMS 173

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 767995434  824 RVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDerwQDLNVISSLLKSFFRKLPEPLFTDDK 903
Cdd:cd04382    16 MIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSK---VDIHVICGCLKDFLRSLKEPLITFAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  904 YNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIAdHSEKNKMEPRNLALVFGPTLV--RTSEDNMTDM 981
Cdd:cd04382    93 WKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLARVFGPTIVgySVPNPDPMTI 171

                         170
                  ....*....|....
gi 767995434  982 VTHMPDRYKIVETL 995
Cdd:cd04382   172 LQDTVRQPRVVERL 185

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 767995434  821 ENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQdERWQDLNVISSLLKSFFRKLPEPLFT 900
Cdd:cd04387    12 ERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVM-LSEMDVNAIAGTLKLYFRELPEPLFT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  901 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTD 980
Cdd:cd04387    91 DELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKESKI 170

                         170
                  ....*....|....*..
gi 767995434  981 MVTHMPDRYKiVETLIQ 997
Cdd:cd04387   171 PTNTMTDSWS-LEVMSQ 186

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 767995434  825 VPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGpGDINLQDErwQDLNVISSLLKSFFRKLPEPLFTDDKY 904
Cdd:cd04376     9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRG-IDVVLDEN--HSVHDVAALLKEFFRDMPDPLLPRELY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  905 NDFIEANRIEDArERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEK-----------NKMEPRNLALVFGPTLVR- 972
Cdd:cd04376    86 TAFIGTALLEPD-EQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLHk 164

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767995434  973 --TSEDNMTDMVTHMPDR---YKIVETLIQHSDWFF 1003
Cdd:cd04376   165 qkSGEREFVQASLRIEEStaiINVVQTMIDNYEELF 200

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 767995434  825 VPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDlnvISSLLKSFFRKLPEPLFTDDKY 904
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHD---ISNVLKLYLRQLPEPLILFRLY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  905 NDFI----EANRIEDARERMRT------------------LRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNL 962
Cdd:cd04409    93 NEFIglakESQHVNETQEAKKNsdkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767995434  963 ALVFGPTLVR----TSEDNMTDMVTHmPDRYKIVETLIQH 998
Cdd:cd04409   173 GIIFGPTLIRprptDATVSLSSLVDY-PHQARLVELLITY 211

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 767995434  809 FGVRLEECqPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDlnvISSLLK 888
Cdd:cd04408     1 FGVDFSQL-PRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHD---ITSVLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995434  889 SFFRKLPEPLFTDDKYNDFIEANR--IEDARER----------MRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNK 956
Cdd:cd04408    77 HFLKELPEPVLPFQLYDDFIALAKelQRDSEKAaespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767995434  957 MEPRNLALVFGPTLVRTSEDNMTDMVTHMPDRYK--IVETLIQH 998
Cdd:cd04408   157 MSPNNLGIVFGPTLLRPLVGGDVSMICLLDTGYQaqLVEFLISN 200