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Conserved domains on  [gi|940516998|ref|NP_001303613|]
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SH3 domain-binding protein 1 isoform 1 [Mus musculus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10166325)

Rho GTPase-activating protein for Rho/Rac/Cdc42-like small GTPases that act as molecular switches, active in their GTP-bound form but inactive when bound to GDP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 16-275 1.28e-133

The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. SH3-domain binding protein 1 (SH3BP1 or 3BP-1) is a Rac GTPase activating protein that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. SH3BP1 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153304  Cd Length: 257  Bit Score: 393.15  E-value: 1.28e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  16 GSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMG 95
Cdd:cd07620    1 GSLSVSQDATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDAESSIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  96 KALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQAAKNSGSNQGLGGA 175
Cdd:cd07620   81 RVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 176 SGSHTHTTTANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKEDSYANYFIHLLEIQADYHRKSLTSLDTALAELRDN 255
Cdd:cd07620  161 VGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELKEN 240

                        250       260
                 ....*....|....*....|
gi 940516998 256 HSQADHSPLTTAapfSRVYG 275
Cdd:cd07620  241 HSQKEPSVSVSS---QRVYG 257
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 272-473 2.22e-83

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.


The actual alignment was detected with superfamily member cd04386:

Pssm-ID: 470621  Cd Length: 203  Bit Score: 261.62  E-value: 2.22e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 272 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFCSDPHAVAGALK 349
Cdd:cd04386    3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASALK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 350 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 429
Cdd:cd04386   83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940516998 430 NLLWPPEkEGDQAQLDAAsvSSIQVVGVVEALIQNADTLFPGDI 473
Cdd:cd04386  163 NLLWAKN-EGSLAEMAAG--TSVHVVAIVELIISHADWFFPGEV 203
 
Name Accession Description Interval E-value
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 16-275 1.28e-133

The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. SH3-domain binding protein 1 (SH3BP1 or 3BP-1) is a Rac GTPase activating protein that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. SH3BP1 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153304  Cd Length: 257  Bit Score: 393.15  E-value: 1.28e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  16 GSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMG 95
Cdd:cd07620    1 GSLSVSQDATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDAESSIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  96 KALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQAAKNSGSNQGLGGA 175
Cdd:cd07620   81 RVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 176 SGSHTHTTTANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKEDSYANYFIHLLEIQADYHRKSLTSLDTALAELRDN 255
Cdd:cd07620  161 VGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELKEN 240

                        250       260
                 ....*....|....*....|
gi 940516998 256 HSQADHSPLTTAapfSRVYG 275
Cdd:cd07620  241 HSQKEPSVSVSS---QRVYG 257
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 272-473 2.22e-83

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.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 261.62  E-value: 2.22e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 272 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFCSDPHAVAGALK 349
Cdd:cd04386    3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASALK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 350 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 429
Cdd:cd04386   83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940516998 430 NLLWPPEkEGDQAQLDAAsvSSIQVVGVVEALIQNADTLFPGDI 473
Cdd:cd04386  163 NLLWAKN-EGSLAEMAAG--TSVHVVAIVELIISHADWFFPGEV 203
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 287-465 1.15e-55

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 187.47  E-value: 1.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   287 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPH-SLEEFCSDPHAVAGALKSYLRELPEPLMTSDLY 365
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   366 DDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEgdqaqlD 445
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE------V 154

                          170       180
                   ....*....|....*....|
gi 940516998   446 AASVSSIQVVGVVEALIQNA 465
Cdd:smart00324 155 ASLKDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 291-435 2.56e-50

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.96  E-value: 2.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  291 LPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS-LEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWM 369
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940516998  370 RAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPP 435
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 2-245 1.45e-28

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 114.35  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998    2 MKRQLHRMRQLA-HTgsSGRTPETAefLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTT 80
Cdd:pfam03114   1 LKKQFNRASQLLgEK--VGGAEKTK--LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAES 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   81 MAESFKELDPDSSMGKALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSeEELPAILKHKKSLQKLVSDWNTLKSRLS 160
Cdd:pfam03114  77 MIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  161 QAAKnsgsnqglggasgshTHTTTANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKE-DSYANYFIHLLEIQADYHR 239
Cdd:pfam03114 156 KAKK---------------KKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEvEFVVNQLVAFVEAQLDFHR 220


                  ....*.
gi 940516998  240 KSLTSL 245
Cdd:pfam03114 221 QCYQLL 226
BAR smart00721
BAR domain;
2-254 1.86e-17

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 82.05  E-value: 1.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998     2 MKRQLHRMRQLA--HTGSSGRTPetaefLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALST 79
Cdd:smart00721   2 FKKQFNRAKQKVgeKVGKAEKTK-----LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998    80 TMAESF--KELDPDSSMGKALEMTCAIQNQLARILAEFeMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKS 157
Cdd:smart00721  77 VYEGGDdgEGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   158 RLSQAAKNSGSNQGLGGASGSHTHTTTANkvemlkeeeeelkkKVEQCKDEYLADLYHFSTKE-DSYANYFIHLLEIQAD 236
Cdd:smart00721 156 KLKKAKKSKEKKKDEKLAKAEEELRKAKQ--------------EFEESNAQLVEELPQLVASRvDFFVNCLQALIEAQLN 221

                          250
                   ....*....|....*...
gi 940516998   237 YHRKSLTSLDTALAELRD 254
Cdd:smart00721 222 FHRESYKLLQQLQQQLDK 239
 
Name Accession Description Interval E-value
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 16-275 1.28e-133

The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. SH3-domain binding protein 1 (SH3BP1 or 3BP-1) is a Rac GTPase activating protein that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. SH3BP1 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153304  Cd Length: 257  Bit Score: 393.15  E-value: 1.28e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  16 GSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMG 95
Cdd:cd07620    1 GSLSVSQDATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDAESSIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  96 KALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQAAKNSGSNQGLGGA 175
Cdd:cd07620   81 RVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 176 SGSHTHTTTANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKEDSYANYFIHLLEIQADYHRKSLTSLDTALAELRDN 255
Cdd:cd07620  161 VGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELKEN 240

                        250       260
                 ....*....|....*....|
gi 940516998 256 HSQADHSPLTTAapfSRVYG 275
Cdd:cd07620  241 HSQKEPSVSVSS---QRVYG 257
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 272-473 2.22e-83

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.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 261.62  E-value: 2.22e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 272 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFCSDPHAVAGALK 349
Cdd:cd04386    3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASALK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 350 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 429
Cdd:cd04386   83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940516998 430 NLLWPPEkEGDQAQLDAAsvSSIQVVGVVEALIQNADTLFPGDI 473
Cdd:cd04386  163 NLLWAKN-EGSLAEMAAG--TSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 16-281 3.63e-82

The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.


Pssm-ID: 153279 [Multi-domain]  Cd Length: 244  Bit Score: 259.96  E-value: 3.63e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  16 GSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMG 95
Cdd:cd07595    1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLPEYGLAQSMLESSKELPDDSLLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  96 KALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQAAKNSGsnqglgga 175
Cdd:cd07595   81 KVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSG-------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 176 sgshtHTTTANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKEDSYANYFIHLLEIQADYHRKSLTSLDTALAELRDN 255
Cdd:cd07595  153 -----GQGAAAKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQ 227

                        250       260
                 ....*....|....*....|....*.
gi 940516998 256 HSQADHSPlttaapfsrVYGVSLRTH 281
Cdd:cd07595  228 IEQSPSKP---------VFGQPLEEH 244
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 19-281 7.76e-62

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


Pssm-ID: 153302  Cd Length: 246  Bit Score: 206.42  E-value: 7.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  19 GRTPETaEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMGKAL 98
Cdd:cd07618    5 GRAEKT-EVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLGEESLIGKML 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  99 EMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQAAKNSGSN-QGLggasg 177
Cdd:cd07618   84 DTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNfQAM----- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 178 shthtttANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKEDSYANYFIHLLEIQADYHRKSLTSLDTALAELRDNHS 257
Cdd:cd07618  159 -------PSKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQD 231

                        250       260
                 ....*....|....*....|....
gi 940516998 258 QADHSPlttaapfsrVYGVSLRTH 281
Cdd:cd07618  232 KWMEKP---------AFGTPLEEH 246
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
 23-253 1.31e-56

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 2 (Rich2) is a Rho GTPase activating protein that interacts with CD317, a lipid raft-associated integral membrane protein. It plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. Rich2 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153303  Cd Length: 248  Bit Score: 192.57  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  23 ETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMGKALEMTC 102
Cdd:cd07619    8 EKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLGKMLKLCG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 103 AIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQAAKNSG--SNQGLGGASGSHT 180
Cdd:cd07619   88 ETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGlsSNLQPTGAKADAL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940516998 181 H---TTTANKVEMlkeeeeelkkkveqCKDEYLADLYHFSTKEDSYANYFIHLLEIQADYHRKSLTSLDTALAELR 253
Cdd:cd07619  168 ReemEEAANRMEI--------------CRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIK 229
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 287-465 1.15e-55

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 187.47  E-value: 1.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   287 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPH-SLEEFCSDPHAVAGALKSYLRELPEPLMTSDLY 365
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   366 DDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEgdqaqlD 445
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE------V 154

                          170       180
                   ....*....|....*....|
gi 940516998   446 AASVSSIQVVGVVEALIQNA 465
Cdd:smart00324 155 ASLKDIRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 291-464 2.66e-51

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.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 175.18  E-value: 2.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 291 LPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMR 370
Cdd:cd00159    2 LIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 371 AASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEgdqaqlDAASVS 450
Cdd:cd00159   82 LAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSD------DELLED 155

                        170
                 ....*....|....
gi 940516998 451 SIQVVGVVEALIQN 464
Cdd:cd00159  156 IKKLNEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 291-435 2.56e-50

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.96  E-value: 2.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  291 LPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS-LEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWM 369
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940516998  370 RAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPP 435
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 274-469 1.89e-38

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.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 140.94  E-value: 1.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSLrTHLQDLGRD---IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMAS-DPHSLEEFcSDPHAVAGALK 349
Cdd:cd04404    6 FGVSL-QFLKEKNPEqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMgEPVDFDQY-EDVHLPAVILK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 350 SYLRELPEPLMTSDLYDDWMRAASLKEPgARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 429
Cdd:cd04404   84 TFLRELPEPLLTFDLYDDIVGFLNVDKE-ERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 940516998 430 NLLWPPEKegdqaqldAASVSSI-QVVGVVEALIQNADTLF 469
Cdd:cd04404  163 NLLWAKDA--------SMSLSAInPINTFTKFLLDHQDEIF 195
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 282-473 1.16e-32

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. 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.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 124.72  E-value: 1.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 282 LQDLGRDIALP--IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPH-SLEEFCSdpHAVAGALKSYLRELPEP 358
Cdd:cd04402    6 LSNICEDDNLPkpILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEvDLKAEPV--LLLASVLKDFLRNIPGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 359 LMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPeke 438
Cdd:cd04402   84 LLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPP--- 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 940516998 439 gDQAQLDAASVSsiQVVGVVEALIQNADTLFPGDI 473
Cdd:cd04402  161 -ASSELQNEDLK--KVTSLVQFLIENCQEIFGEDI 192
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 274-462 1.43e-32

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.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 124.09  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSLrTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFcsDPHAVAGALKSY 351
Cdd:cd04377    1 FGVSL-SSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSvnLEDY--PIHVITSVLKQW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 352 LRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNL 431
Cdd:cd04377   78 LRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCI 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 940516998 432 LWPPEKEGDQAQLDAASvssiQVVGVVEALI 462
Cdd:cd04377  158 LRCPDTADPLQSLQDVS----KTTTCVETLI 184
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 274-469 4.39e-32

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 122.90  E-value: 4.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSL-----EEFCSDPHAVAGAL 348
Cdd:cd04398    1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVllispEDYESDIHSVASLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 349 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLG 428
Cdd:cd04398   81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 940516998 429 PNLLwppekegDQAQLDAASVSSiqVVGVVEALIQNADTLF 469
Cdd:cd04398  161 PTLM-------NAAPDNAADMSF--QSRVIETLLDNAYQIF 192
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 304-436 1.91e-31

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.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 120.87  E-value: 1.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 304 GMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFcsdP-HAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGAR 380
Cdd:cd04407   30 GLYTEGIYRKSGSANRMKELHQLLQADPENvkLENY---PiHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQ 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 940516998 381 LEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPE 436
Cdd:cd04407  107 LQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRCPD 162
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 274-469 5.01e-30

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.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 117.23  E-value: 5.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSL---EEFCSDPHAVAGALKS 350
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKAdisATVYPDINVITGALKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 351 YLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPN 430
Cdd:cd04372   81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 940516998 431 LLWPPEKEGDQAQLDAAsvSSIQvvgVVEALIQNADTLF 469
Cdd:cd04372  161 LMRPPEDSALTTLNDMR--YQIL---IVQLLITNEDVLF 194
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 273-431 5.64e-30

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.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 117.07  E-value: 5.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 273 VYGVSLRTHLQ-----DLGRDIALPIEACVLLLLSEG-MQEEGLFRLAAGASVLKRLKQ--------TMASDPhslEEFc 338
Cdd:cd04400    1 IFGSPLEEAVElsshkYNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKErfnteydvDLFSSS---LYP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 339 sDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLK-EPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNK 417
Cdd:cd04400   77 -DVHTVAGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNK 155

                        170
                 ....*....|....
gi 940516998 418 MTPSNIAIVLGPNL 431
Cdd:cd04400  156 MNLRNVCIVFSPTL 169
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 2-245 1.45e-28

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 114.35  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998    2 MKRQLHRMRQLA-HTgsSGRTPETAefLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTT 80
Cdd:pfam03114   1 LKKQFNRASQLLgEK--VGGAEKTK--LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAES 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   81 MAESFKELDPDSSMGKALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSeEELPAILKHKKSLQKLVSDWNTLKSRLS 160
Cdd:pfam03114  77 MIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  161 QAAKnsgsnqglggasgshTHTTTANKVEMLKEEEEELKKKVEQCKDEYLADLYHFSTKE-DSYANYFIHLLEIQADYHR 239
Cdd:pfam03114 156 KAKK---------------KKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEvEFVVNQLVAFVEAQLDFHR 220


                  ....*.
gi 940516998  240 KSLTSL 245
Cdd:pfam03114 221 QCYQLL 226
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 272-464 2.20e-28

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.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 112.60  E-value: 2.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 272 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEeGLFRLAAGASVLKRLKQTMASD--PH-SLEEFCSDPHAVAGAL 348
Cdd:cd04384    1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEqiPDlTKDVYIQDIHSVSSLC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 349 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLG 428
Cdd:cd04384   80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 940516998 429 PNLLWPPEKEGDQAQLDAASVSS-IQVVgVVEALIQN 464
Cdd:cd04384  160 PNLLRSKQIESACFSGTAAFMEVrIQSV-VVEFILNH 195
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 289-469 6.57e-28

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 111.34  E-value: 6.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 289 IALPIEACVLLLLSEGMQEEGLFRL---AAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLY 365
Cdd:cd04395   18 VPLIVEVCCNIVEARGLETVGIYRVpgnNAAISALQEELNRGGFDIDLQDPRWRDVNVVSSLLKSFFRKLPEPLFTNELY 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 366 DDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLD 445
Cdd:cd04395   98 PDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRTSDDNMETMVTH 177

                        170       180
                 ....*....|....*....|....
gi 940516998 446 AASVSSIqvvgvVEALIQNADTLF 469
Cdd:cd04395  178 MPDQCKI-----VETLIQHYDWFF 196
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 287-469 4.05e-27

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.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 109.07  E-value: 4.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 287 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYD 366
Cdd:cd04390   20 RLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 367 DWMRAASL--KEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPpekegdQAQl 444
Cdd:cd04390  100 DFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILRP------KVE- 172

                        170       180
                 ....*....|....*....|....*..
gi 940516998 445 DAASV--SSIQVVGVVEALIQNADTLF 469
Cdd:cd04390  173 DPATImeGTPQIQQLMTVMISKHEPLF 199
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 281-464 4.65e-27

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.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 109.02  E-value: 4.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 281 HLQDLGRDIalpIEACVLLLLSEGMQEEGLFRLAAGASVLKRLkQTMASDPHSLE----EFCS---DPHAVAGALKSYLR 353
Cdd:cd04374   23 QLDDIGFKF---VRKCIEAVETRGINEQGLYRVVGVNSKVQKL-LSLGLDPKTSTpgdvDLDNsewEIKTITSALKTYLR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 354 ELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLW 433
Cdd:cd04374   99 NLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLR 178

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 940516998 434 PPEKegdqaqldaaSVSSIQVVG----VVEALIQN 464
Cdd:cd04374  179 PQEE----------TVAAIMDIKfqniVVEILIEN 203
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 272-443 2.41e-26

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.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 106.35  E-value: 2.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 272 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTM--ASDPHSLEEFCSDPHAVAGALK 349
Cdd:cd04383    1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFerGEDPLADDQNDHDINSVAGVLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 350 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 429
Cdd:cd04383   81 LYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGP 160

                        170
                 ....*....|....
gi 940516998 430 NLLWPPEkEGDQAQ 443
Cdd:cd04383  161 TLMPVPE-GQDQVS 173
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 293-462 3.11e-26

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.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 106.55  E-value: 3.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 293 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCS--DPHAVAGALKSYLRELPEPLMTSDLYDDWMR 370
Cdd:cd04387   20 VRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSemDVNAIAGTLKLYFRELPEPLFTDELYPNFAE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 371 AASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVS 450
Cdd:cd04387  100 GIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKESKIPTNTMTDSW 179

                        170
                 ....*....|..
gi 940516998 451 SIQVVGVVEALI 462
Cdd:cd04387  180 SLEVMSQVQVLL 191
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 293-442 3.60e-26

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


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 105.94  E-value: 3.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 293 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLK----QTMASDPHSLEEfcSDPHAVAGALKSYLRELPEPLMTSDLYDDW 368
Cdd:cd04403   20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRfavdHDEKLDLDDSKW--EDIHVITGALKLFFRELPEPLFPYSLFNDF 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940516998 369 MRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQA 442
Cdd:cd04403   98 VAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQETGNIA 171
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 280-464 1.93e-25

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. 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.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 103.54  E-value: 1.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 280 THLQD--LGR-DIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSD--PHAVAGALKSYLRE 354
Cdd:cd04385    3 PALEDqqLTDnDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLREGEytVHDVADVLKRFLRD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 355 LPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWP 434
Cdd:cd04385   83 LPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQT 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 940516998 435 PEKEGDQAQldaasvssiQVVGVVEALIQN 464
Cdd:cd04385  163 DEHSVGQTS---------HEVKVIEDLIDN 183
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 273-465 1.60e-24

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 101.78  E-value: 1.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 273 VYGVSLRT----HLQDLGRDIALPIEACVLLLlsEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEfcSDPHAVAGAL 348
Cdd:cd04394    1 VFGVPLHSlphsTVPEYGNVPKFLVDACTFLL--DHLSTEGLFRKSGSVVRQKELKAKLEGGEACLSS--ALPCDVAGLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 349 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLG 428
Cdd:cd04394   77 KQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFA 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 940516998 429 PNLLwppEKEGDQAQLDAASVSSIQV-VGVVEALIQNA 465
Cdd:cd04394  157 PNLF---QSEEGGEKMSSSTEKRLRLqAAVVQTLIDNA 191
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 304-464 3.69e-24

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.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 100.57  E-value: 3.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 304 GMQeeGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAA----------- 372
Cdd:cd04378   33 GVQ--GIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYNDFIALAkeiqrdteedk 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 373 SLKEPGARLEALH---DVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDqaqldaASV 449
Cdd:cd04378  111 APNTPIEVNRIIRklkDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIRPRPGDAD------VSL 184

                        170
                 ....*....|....*....
gi 940516998 450 SSIQVVG----VVEALIQN 464
Cdd:cd04378  185 SSLVDYGyqarLVEFLITN 203
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 293-473 8.24e-24

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.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 99.82  E-value: 8.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 293 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTM-ASDPHSLEEFCSdPHAVAGALKSYLRELPEPLMTSDLYDDWMRA 371
Cdd:cd04376   13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFdRGIDVVLDENHS-VHDVAALLKEFFRDMPDPLLPRELYTAFIGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 372 ASLkEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLA-----------EEQDVNKMTPSNIAIVLGPNLLW---PPEK 437
Cdd:cd04376   92 ALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAehaadsidedgQEVSGNKMTSLNLATIFGPNLLHkqkSGER 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 940516998 438 EGDQAQLDAAsvSSIQVVGVVEALIQNADTLF--PGDI 473
Cdd:cd04376  171 EFVQASLRIE--ESTAIINVVQTMIDNYEELFmvSPEL 206
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 287-464 2.97e-23

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 97.53  E-value: 2.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 287 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDpHSLE--EFCSDPHAVAGALKSYLRELPEPLMTSDL 364
Cdd:cd04373   13 KPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQD-HNLDlvSKDFTVNAVAGALKSFFSELPDPLIPYSM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 365 YDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPpekegDQAQL 444
Cdd:cd04373   92 HLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMRP-----DFTSM 166

                        170       180
                 ....*....|....*....|
gi 940516998 445 DAASVSSIqVVGVVEALIQN 464
Cdd:cd04373  167 EALSATRI-YQTIIETFIQQ 185
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 273-469 4.72e-23

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


Pssm-ID: 239856  Cd Length: 216  Bit Score: 97.80  E-value: 4.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 273 VYGVSLRTHL-QDLGRD----IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDphsleEFCSD------- 340
Cdd:cd04391    1 LFGVPLSTLLeRDQKKVpgskVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAK-----FYEGTflwdqvk 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 341 PHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTP 420
Cdd:cd04391   76 QHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940516998 421 SNIAIVLGPNL-----LWPPEKEGDQAQLDAASVSSIqvvgVVEALIQNADTLF 469
Cdd:cd04391  156 WNVAMIMAPNLfpprgKHSKDNESLQEEVNMAAGCAN----IMRLLIRYQDLLW 205
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 293-468 7.19e-21

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. 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.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 91.27  E-value: 7.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 293 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSD-PHAVAGALKSYLRELPEPLMTSDLYDDWMRA 371
Cdd:cd04397   31 IDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnPVQLAALLKKFLRELPDPLLTFKLYRLWISS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 372 ASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLA-----EEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDA 446
Cdd:cd04397  111 QKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfshiDEETGSKMDIHNLATVITPNILYSKTDNPNTGDEYF 190

                        170       180
                 ....*....|....*....|..
gi 940516998 447 ASVSsiqvvgVVEALIQNADTL 468
Cdd:cd04397  191 LAIE------AVNYLIENNEEF 206
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 272-431 1.38e-20

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.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 89.83  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 272 RVYGVSLRtHLQDLGR---DIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGAL 348
Cdd:cd04393    1 KVFGVPLQ-ELQQAGQpenGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 349 KSYLRELPEPLMTSDLYDDWMRA-ASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVL 427
Cdd:cd04393   80 RLFLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVF 159


                 ....
gi 940516998 428 GPNL 431
Cdd:cd04393  160 GPDV 163
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 308-464 3.34e-20

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.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 89.11  E-value: 3.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 308 EGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAA---------SLKEPG 378
Cdd:cd04408   35 QGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLYDDFIALAkelqrdsekAAESPS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 379 ARLEALH---DVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPekEGDQAQLDAASVSSIQVV 455
Cdd:cd04408  115 IVENIIRslkELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRPL--VGGDVSMICLLDTGYQAQ 192


                 ....*....
gi 940516998 456 gVVEALIQN 464
Cdd:cd04408  193 -LVEFLISN 200
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 273-431 1.33e-19

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. 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.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 87.86  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 273 VYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYL 352
Cdd:cd04375    4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYF 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940516998 353 RELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNL 431
Cdd:cd04375   84 RDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSL 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 274-452 2.99e-19

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 86.75  E-value: 2.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSLRTHLQDLG--RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLE---EFCSDPHAVAGAL 348
Cdd:cd04379    1 FGVPLSRLVEREGesRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVElseELYPDINVITGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 349 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHD---VCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAI 425
Cdd:cd04379   81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLtlsIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160

                        170       180
                 ....*....|....*....|....*..
gi 940516998 426 VLGPnLLWPPEKEGDQAQLDAASVSSI 452
Cdd:cd04379  161 CFGP-VLMFCSQEFSRYGISPTSKMAA 186
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 274-431 4.50e-19

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 85.18  E-value: 4.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSL-----RTHLQDlGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS-LEEFcsDPHAVAGA 347
Cdd:cd04381    1 FGASLslaveRSRCHD-GIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPnLEEY--EPPTVASL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 348 LKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVL 427
Cdd:cd04381   78 LKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVL 157


                 ....
gi 940516998 428 GPNL 431
Cdd:cd04381  158 SPTV 161
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 296-472 1.26e-18

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.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 84.27  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 296 CVLLLLSEGMQEEGLFRLAAGASVLKRLKQTM---ASDPHsLEEFcsDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAA 372
Cdd:cd04382   24 CVNEIEARGLTEEGLYRVSGSEREVKALKEKFlrgKTVPN-LSKV--DIHVICGCLKDFLRSLKEPLITFALWKEFMEAA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 373 SLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDvNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSI 452
Cdd:cd04382  101 EILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYSVPNPDPMTILQDTVRQP 179

                        170       180
                 ....*....|....*....|
gi 940516998 453 QvvgVVEALIqnadtLFPGD 472
Cdd:cd04382  180 R---VVERLL-----EIPSD 191
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 274-436 1.46e-18

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


Pssm-ID: 239871  Cd Length: 186  Bit Score: 83.90  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 274 YGVSLrTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLR 353
Cdd:cd04406    1 FGVEL-SRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 354 ELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLW 433
Cdd:cd04406   80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILR 159


                 ...
gi 940516998 434 PPE 436
Cdd:cd04406  160 CPD 162
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 289-434 5.15e-18

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.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 83.32  E-value: 5.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 289 IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDW 368
Cdd:cd04409   16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 369 M----------------RAASLKEPGARLE------ALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIV 426
Cdd:cd04409   96 IglakesqhvnetqeakKNSDKKWPNMCTElnrillKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGII 175


                 ....*...
gi 940516998 427 LGPNLLWP 434
Cdd:cd04409  176 FGPTLIRP 183
BAR smart00721
BAR domain;
2-254 1.86e-17

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 82.05  E-value: 1.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998     2 MKRQLHRMRQLA--HTGSSGRTPetaefLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALST 79
Cdd:smart00721   2 FKKQFNRAKQKVgeKVGKAEKTK-----LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998    80 TMAESF--KELDPDSSMGKALEMTCAIQNQLARILAEFeMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKS 157
Cdd:smart00721  77 VYEGGDdgEGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998   158 RLSQAAKNSGSNQGLGGASGSHTHTTTANkvemlkeeeeelkkKVEQCKDEYLADLYHFSTKE-DSYANYFIHLLEIQAD 236
Cdd:smart00721 156 KLKKAKKSKEKKKDEKLAKAEEELRKAKQ--------------EFEESNAQLVEELPQLVASRvDFFVNCLQALIEAQLN 221

                          250
                   ....*....|....*...
gi 940516998   237 YHRKSLTSLDTALAELRD 254
Cdd:smart00721 222 FHRESYKLLQQLQQQLDK 239
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 298-452 1.80e-16

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 78.66  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 298 LLLLSEGMQEEGLFRLAAGASVLKRLKQTMASD-PHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASL-- 374
Cdd:cd04392   17 IEYLEKNLRVEGLFRKPGNSARQQELRDLLNSGtDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLcq 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 375 -KEPGAR---------LEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQL 444
Cdd:cd04392   97 fDEKGNKtsapdkerlLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHE 176


                 ....*...
gi 940516998 445 DAASVSSI 452
Cdd:cd04392  177 NAQKLNSI 184
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 273-468 1.08e-15

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.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 76.68  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 273 VYGVSLRTHLQD-------LGRD--------IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEF 337
Cdd:cd04396    1 VFGVSLEESLKYasvaisiVDEDgeqyvygyIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 338 CSDP---HAVAGALKSYLRELPEPLMTSDLYDDWmRAASLKEPG------------------ARLEALHDVCSRLPQENF 396
Cdd:cd04396   81 DWDGytvHDAASVLRRYLNNLPEPLVPLDLYEEF-RNPLRKRPRilqymkgrineplntdidQAIKEYRDLITRLPNLNR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940516998 397 NNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVssiqvvgVVEALIQNADTL 468
Cdd:cd04396  160 QLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDHEMDPKEYKLSRL-------VVEFLIEHQDKF 224
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 298-432 2.12e-15

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) 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.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 74.73  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 298 LLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFcSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAAslKEP 377
Cdd:cd04389   31 KVLALGGFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGL-EDPHVPASLLKLWLRELEEPLIPDALYQQCISAS--EDP 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 940516998 378 GARLEalhdVCSRLPQENFNNLRYLMKFLALLAEEQDV--NKMTPSNIAIVLGPNLL 432
Cdd:cd04389  108 DKAVE----IVQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNIL 160
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 300-439 2.46e-08

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. 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.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 55.04  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 300 LLSEGMQEEGLFRLAAGASVLKRLKQTM--ASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEp 377
Cdd:cd04380   61 LYTRGLAQEGLFEEPGLPSEPGELLAEIrdALDTGSPFNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNE- 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940516998 378 garLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEG 439
Cdd:cd04380  140 ---EDKRQVIRISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAG 198
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 67-249 4.91e-08

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 53.60  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  67 KRVKKLP-----LMALSTTMAESFKEL------DPDSSMGKALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEEL 135
Cdd:cd07307   14 KDTKKLLdslkeLPAAAEKLSEALQELgkelpdLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 136 PAILKHKKSLQKLVSDWNTLKSRLSQAAKnsgSNQGLGGASGSHTHTTTANkvemlkeeeeelkKKVEQCKDEYLADLYH 215
Cdd:cd07307   94 KEIKKRRKKLDKARLDYDAAREKLKKLRK---KKKDSSKLAEAEEELQEAK-------------EKYEELREELIEDLNK 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 940516998 216 F-STKEDSYANYFIHLLEIQADYHRKSLTSLDTAL 249
Cdd:cd07307  158 LeEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLL 192
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 288-432 1.89e-07

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. 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.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 52.18  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 288 DIALPIeacvLLLLSEGMQEEGL-----FRLAAGASVLKrLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTS 362
Cdd:cd04388   13 DVAPPL----LIKLVEAIEKKGLesstlYRTQSSSSLTE-LRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPA 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940516998 363 DLYDDWMRAA----SLKEPGARLEALHDvCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLL 432
Cdd:cd04388   88 PVYSEMISRAqevqSSDEYAQLLRKLIR-SPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
 16-162 2.24e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle.


Pssm-ID: 153278  Cd Length: 229  Bit Score: 49.31  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998  16 GSSGRTPETAEFlgEDLLQveqRLEPAKRAAHNVHKRLQACLQGQ----------SGADMDKRVKKLPLMALSTTMAESF 85
Cdd:cd07594    8 GTAEKTEYDAHF--ENLLQ---RADKTKVWTEKILKQTEAVLQPNpnvrvedfiyEKLDRKKPDRLSNLEQLGQAMIEAG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940516998  86 KELDPDSSMGKALEMTCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQA 162
Cdd:cd07594   83 NDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACKTRVKKA 159
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 340-470 1.33e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. 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.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 46.56  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940516998 340 DPHAVAGALKSYLRELPEPLMTSDLYDDwMRAASLKEPG-------ARLEALHDVCSRLPQENFNNLRYLMKFLALL--- 409
Cdd:cd04399   77 EPSTVASVLKLYLLELPDSLIPHDIYDL-IRSLYSAYPPsqedsdtARIQGLQSTLSQLPKSHIATLDAIITHFYRLiei 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940516998 410 -----AEEQDVNKMTPSnIAIVLGPNLLWPPEKEGDQAQldaasvssiqvVGVVEALIQNADTLFP 470
Cdd:cd04399  156 tkmgeSEEEYADKLATS-LSREILRPIIESLLTIGDKHG-----------YKFFRDLLTHKDQIFS 209
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
 77-146 1.24e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. The BAR domains of endophilin-A1 and A3 form crescent-shaped dimers that can detect membrane curvature and drive membrane bending.


Pssm-ID: 153276  Cd Length: 223  Bit Score: 40.76  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940516998  77 LSTTMAESFKELDPDSSMGKAL-EMTCAIQnQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQ 146
Cdd:cd07592   69 LGEVMLKYGRELGEDSNFGQALvEVGEALK-QLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLE 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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