RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary 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 83582811 156 AVFGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASL 235
Cdd:cd04390   1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 236 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 315
Cdd:cd04390  81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83582811 316 VIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMIRDHEVLF 354
Cdd:cd04390 161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811    545 NSGEDDLDSLQRTVQSLQKEIETQKQV---YEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDV 621
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100
                   ....*....|....*....|..
gi 83582811    622 EKRNRVLEEEVKEFVKSMEKPK 643
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKR 916

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary 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 83582811 156 AVFGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASL 235
Cdd:cd04390   1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 236 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 315
Cdd:cd04390  81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83582811 316 VIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMIRDHEVLF 354
Cdd:cd04390 161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199

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 83582811    177 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEG 255
Cdd:smart00324   3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDlSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811    256 FLLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMrG 335
Cdd:smart00324  83 FIEAAKLEDETERL--RALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLK-D 159

                          170
                   ....*....|....*
gi 83582811    336 TPQIQRVMTMMIRDH 350
Cdd:smart00324 160 IRHQNTVIEFLIENA 174

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 83582811     47 PIKVGWLKKQ-RSIVKNWQQRYFVLRAQQLYYYKDEE---DSKPQGCMYLPGSTVKEIATNPEEAGKFVFEVIPASsdqn 122
Cdd:smart00233   1 VIKEGWLYKKsGGGKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTSD---- 76

                           90       100
                   ....*....|....*....|....*...
gi 83582811    123 rigQDSYVLMASSQVEMEEWVKFLRRVA 150
Cdd:smart00233  77 ---RKTLLLQAESEEEREKWVEALRKAI 101

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811    545 NSGEDDLDSLQRTVQSLQKEIETQKQV---YEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDV 621
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100
                   ....*....|....*....|..
gi 83582811    622 EKRNRVLEEEVKEFVKSMEKPK 643
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKR 916

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811   537 SEMEAGSKNSGEDDLDSLQRTVQSLQKEIETQKQVY----------EEQIKNLEKENYDVWAKVVRLNEELERERKKFAA 606
Cdd:pfam06160 324 NENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeeleeiLEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 83582811   607 LEISLRNVERSredVEKRN------------RVLEEEVKEFVKSMEKPK 643
Cdd:pfam06160 404 FKLELREIKRL---VEKSNlpglpesyldyfFDVSDEIEDLADELNEVP 449

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary 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 83582811 156 AVFGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASL 235
Cdd:cd04390   1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 236 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 315
Cdd:cd04390  81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83582811 316 VIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMIRDHEVLF 354
Cdd:cd04390 161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199

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 83582811    177 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEG 255
Cdd:smart00324   3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDlSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811    256 FLLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMrG 335
Cdd:smart00324  83 FIEAAKLEDETERL--RALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLK-D 159

                          170
                   ....*....|....*
gi 83582811    336 TPQIQRVMTMMIRDH 350
Cdd:smart00324 160 IRHQNTVIEFLIENA 174

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811   178 PILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 256
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDlEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811   257 LLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKV 326
Cdd:pfam00620  81 IEAAKLPDEEERL--EALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148

Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. 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 83582811  48 IKVGWLKKQRSIVKNWQQRYFVLRAQQLYYYKDEEDSKPQGCMYLPGSTVKEIATNPEEAGKFVFEVIPAsSDQNRI--G 125
Cdd:cd13379   4 IKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLPGNRVTEHPCNEEEPGKFLFEVVPG-GDRERMtaN 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 83582811 126 QDSYVLMASSQVEMEEWVKFLRRVAGTPSGA 156
Cdd:cd13379  83 HETYLLMASTQNDMEDWVKSIRRVIWAPFGG 113

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 83582811 157 VFGQRLDEtvayeqkfgpHL------VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAG--ERPSFDRDTD 228
Cdd:cd04386   4 VFGTPLEE----------HLkrtgreIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfSLPLDEFYSD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 229 VHTVASLLKLYLRDLPEPVVPWSQYEGFLlcgQLMN-ADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNK 307
Cdd:cd04386  74 PHAVASALKSYLRELPDPLLTYNLYEDWV---QAANkPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 83582811 308 MSVDNLATVIGVNLIRSKVEDPAVIMRGTPQIQRVMT--MMIRDHEVLFP 355
Cdd:cd04386 151 MSPSNIAIVLAPNLLWAKNEGSLAEMAAGTSVHVVAIveLIISHADWFFP 200

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 83582811 173 GPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQ 252
Cdd:cd04404  19 EQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLPAVILKTFLRELPEPLLTFDL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 253 YEGFLLCGQLMNADEAKAQQELVKqlsTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKveDPAVI 332
Cdd:cd04404  99 YDDIVGFLNVDKEERVERVKQLLQ---TLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPNLLWAK--DASMS 173

                       170       180
                ....*....|....*....|..
gi 83582811 333 MRGTPQIQRVMTMMIRDHEVLF 354
Cdd:cd04404 174 LSAINPINTFTKFLLDHQDEIF 195

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 83582811 157 VFGQRLDETVAYE-QKFGPHLVPILVEKCAEFILEHG-VSEEGIFRLPGQDNLVKQLRDAFDAGerpsFDRDT------- 227
Cdd:cd04400   1 IFGSPLEEAVELSsHKYNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTE----YDVDLfssslyp 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 228 DVHTVASLLKLYLRDLPEPVVPWSQYEGFLLCGQLmNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNK 307
Cdd:cd04400  77 DVHTVAGLLKLYLRELPTLILGGELHNDFKRLVEE-NHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNK 155

                ....*....
gi 83582811 308 MSVDNLATV 316
Cdd:cd04400 156 MNLRNVCIV 164

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 174 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDA-GERPSFDRDT--DVHTVASLLKLYLRDLPEPVVPW 250
Cdd:cd04372  13 NTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdGEKADISATVypDINVITGALKLYFRDLPIPVITY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 251 SQYEGFLLCGQLMNADEakaQQELVKQ-LSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDP 329
Cdd:cd04372  93 DTYPKFIDAAKISNPDE---RLEAVHEaLMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSA 169

                       170       180
                ....*....|....*....|....*.
gi 83582811 330 AVIMRG-TPQIQrVMTMMIRDHEVLF 354
Cdd:cd04372 170 LTTLNDmRYQIL-IVQLLITNEDVLF 194

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 83582811 174 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 253
Cdd:cd04382  14 SPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALW 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 254 EGFLLCGQlmNADEAKAQQELVKQLSTLPRDNYNLLSYIcrFLHeIQ--LNCAVNKMSVDNLATVIGVNLIRSKVEDP-- 329
Cdd:cd04382  94 KEFMEAAE--ILDEDNSRAALYQAISELPQPNRDTLAFL--ILH-LQrvAQSPECKMDINNLARVFGPTIVGYSVPNPdp 168

                       170
                ....*....|....*..
gi 83582811 330 AVIMRGTPQIQRVMTMM 346
Cdd:cd04382 169 MTILQDTVRQPRVVERL 185

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 83582811 158 FGQRLDETVAYEqkfgpHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLK 237
Cdd:cd04377   1 FGVSLSSLTSED-----RSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 238 LYLRDLPEPVVPWSQYEGFLlcgqlmNADEAKAQQELVKQLST----LPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNL 313
Cdd:cd04377  76 QWLRELPEPLMTFELYENFL------RAMELEEKQERVRALYSvleqLPRANLNTLERLIFHLVRVALQEEVNRMSANAL 149

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 83582811 314 ATVIGVNLIRS-KVEDPAVIMRGTPQIQRVMTMMIRD 349
Cdd:cd04377 150 AIVFAPCILRCpDTADPLQSLQDVSKTTTCVETLIKE 186

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 158 FGQRLDETVayeqKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD--RDTDVHTVASL 235
Cdd:cd04383   3 FNGSLEEYI----QDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADdqNDHDINSVAGV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 236 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVkqLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 315
Cdd:cd04383  79 LKLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREI--LSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAI 156

                ....*...
gi 83582811 316 VIGVNLIR 323
Cdd:cd04383 157 CFGPTLMP 164

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 83582811 176 LVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERP--SFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 253
Cdd:cd04387  15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDvsVMLSEMDVNAIAGTLKLYFRELPEPLFTDELY 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83582811 254 EGFLlcGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVED 328
Cdd:cd04387  95 PNFA--EGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKE 167

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 177 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 256
Cdd:cd04407  15 VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDF 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 257 LLCGQLMNADEakAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIR-SKVEDPAVIMRG 335
Cdd:cd04407  95 LRAVELPEKQE--QLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRcPDSSDPLTSMKD 172

                       170
                ....*....|....
gi 83582811 336 TPQIQRVMTMMIRD 349
Cdd:cd04407 173 VAKTTTCVEMLIKE 186

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 157 VFGQRLDETVAYEQ-------------KFGphLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGER--P 221
Cdd:cd04396   1 VFGVSLEESLKYASvaisivdedgeqyVYG--YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDygK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 222 SFDRDT-DVHTVASLLKLYLRDLPEPVVPWSQYEGF---------------LLCGQLMNADEAKAQQELVKQLSTLPRDN 285
Cdd:cd04396  79 SFDWDGyTVHDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkGRINEPLNTDIDQAIKEYRDLITRLPNLN 158

                       170       180       190
                ....*....|....*....|....*....|.
gi 83582811 286 YNLLSYICRFLHEIQLNCAVNKMSVDNLATV 316
Cdd:cd04396 159 RQLLLYLLDLLAVFARNSDKNLMTASNLAAI 189

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 174 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 253
Cdd:cd04378  13 PDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83582811 254 EGFL-LCGQLMNADEAKAQQEL----------VKQL-STLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNL 321
Cdd:cd04378  93 NDFIaLAKEIQRDTEEDKAPNTpievnriirkLKDLlRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTL 172

                       170
                ....*....|..
gi 83582811 322 IRSKVEDPAVIM 333
Cdd:cd04378 173 IRPRPGDADVSL 184