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Conserved domains on  [gi|1655533408|ref|XP_029035844|]
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rho GTPase-activating protein 44-like isoform X5 [Osmia bicornis bicornis]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10166144)

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
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 245-447 5.83e-89

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: 277.03  E-value: 5.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 245 KPVYGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTALEYKDPHVIAGAL 324
Cdd:cd04386     2 KPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSDPHAVASAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 325 KSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIA 404
Cdd:cd04386    82 KSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1655533408 405 PNLIWSPQEDVNTMvMNMSTANNSSLIVDQLITYADWFFPGDV 447
Cdd:cd04386   162 PNLLWAKNEGSLAE-MAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 13-255 8.85e-85

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: 267.66  E-value: 8.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  13 DQTFSRAGKTEVLTDDLQAADKHVEQIRIALIGLNKRFGNIPnqtITQDSTVKEKRLKKCPEYILGQTMLESA---PEDG 89
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCL---QGQSGEDKDKRLKKLPEYGLAQSMLESSkelPDDS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  90 LMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASKHSASTGAT 169
Cdd:cd07595    78 LLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSGGQGAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 170 -KIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEELIPGLESYINDNEMKPVY 248
Cdd:cd07595   158 aKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPVF 237


                  ....*..
gi 1655533408 249 GYPLEEH 255
Cdd:cd07595   238 GQPLEEH 244
 
Name Accession Description Interval E-value
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 245-447 5.83e-89

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: 277.03  E-value: 5.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 245 KPVYGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTALEYKDPHVIAGAL 324
Cdd:cd04386     2 KPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSDPHAVASAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 325 KSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIA 404
Cdd:cd04386    82 KSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1655533408 405 PNLIWSPQEDVNTMvMNMSTANNSSLIVDQLITYADWFFPGDV 447
Cdd:cd04386   162 PNLLWAKNEGSLAE-MAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 13-255 8.85e-85

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: 267.66  E-value: 8.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  13 DQTFSRAGKTEVLTDDLQAADKHVEQIRIALIGLNKRFGNIPnqtITQDSTVKEKRLKKCPEYILGQTMLESA---PEDG 89
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCL---QGQSGEDKDKRLKKLPEYGLAQSMLESSkelPDDS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  90 LMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASKHSASTGAT 169
Cdd:cd07595    78 LLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSGGQGAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 170 -KIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEELIPGLESYINDNEMKPVY 248
Cdd:cd07595   158 aKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPVF 237


                  ....*..
gi 1655533408 249 GYPLEEH 255
Cdd:cd07595   238 GQPLEEH 244
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 265-412 1.24e-51

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 175.81  E-value: 1.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 265 LPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACClTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYPEW 344
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGP-DVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655533408 345 MAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQ 412
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 263-439 4.36e-49

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: 170.14  E-value: 4.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  263 IALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDaCCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYP 342
Cdd:smart00324   3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFD-SGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  343 EWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQEDVNTMVMNm 422
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI- 160

                          170
                   ....*....|....*..
gi 1655533408  423 staNNSSLIVDQLITYA 439
Cdd:smart00324 161 ---RHQNTVIEFLIENA 174
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-237 5.65e-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: 112.81  E-value: 5.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408   1 MKKQFFRVKQLADQTFSRAGKTEvLTDDLQAADKHVEQIRIALIGLNKRfgnIPNQTITQDSTVKEKRLKKCPEYILGQT 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKD---TKGYLQPNPGARAKQTVLEQPEELLAES 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  81 MLE-SAPEDGLMSF--TLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTaVPNILKHKKNLARLILDMDSMRTRYQ 157
Cdd:pfam03114  77 MIEaGKDLGEDSSFgkALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLLKE-FKEIQKHRKKLERKRLDYDAAKTRVK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 158 QAsKHSASTGATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETE-LANTIIQYVKLQRAYHESALHCLEELIPGLE 236
Cdd:pfam03114 156 KA-KKKKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEfVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLG 234


                  .
gi 1655533408 237 S 237
Cdd:pfam03114 235 K 235
BAR smart00721
BAR domain;
1-233 5.22e-23

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 98.61  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408    1 MKKQFFRVKQLADQTFSRAGKTEvLTDDLQAADKHVEQIRIALIGLNKRFGN--IPNQTITQDSTVKEKRLKKCPEYILG 78
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLylQPNPAVRAKLASQKKLSKSLGEVYEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408   79 QTMLESAPEDGLMSFTLQECGRAQTCLAnEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQ 158
Cdd:smart00721  81 GDDGEGLGADSSYGKALDKLGEALKKLL-QVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408  159 ASKHSASTGATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETE-LANTIIQYVKLQRAYHESALHCLEELIP 233
Cdd:smart00721 160 AKKSKEKKKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQQ 235
 
Name Accession Description Interval E-value
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 245-447 5.83e-89

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: 277.03  E-value: 5.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 245 KPVYGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTALEYKDPHVIAGAL 324
Cdd:cd04386     2 KPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSDPHAVASAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 325 KSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIA 404
Cdd:cd04386    82 KSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1655533408 405 PNLIWSPQEDVNTMvMNMSTANNSSLIVDQLITYADWFFPGDV 447
Cdd:cd04386   162 PNLLWAKNEGSLAE-MAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 13-255 8.85e-85

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: 267.66  E-value: 8.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  13 DQTFSRAGKTEVLTDDLQAADKHVEQIRIALIGLNKRFGNIPnqtITQDSTVKEKRLKKCPEYILGQTMLESA---PEDG 89
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCL---QGQSGEDKDKRLKKLPEYGLAQSMLESSkelPDDS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  90 LMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASKHSASTGAT 169
Cdd:cd07595    78 LLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSGGQGAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 170 -KIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEELIPGLESYINDNEMKPVY 248
Cdd:cd07595   158 aKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPVF 237


                  ....*..
gi 1655533408 249 GYPLEEH 255
Cdd:cd07595   238 GQPLEEH 244
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 13-255 1.61e-53

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: 184.85  E-value: 1.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  13 DQTFSRAGKTEVLTDDLQAADKHVEQIRIALIGLNKRF-----GNIpnqtitqdSTVKEKRLKKCPEYILGQTMLESAP- 86
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLiacfqGQV--------GTDAEKRHKKLPLTALAQNMQEGSAq 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  87 --EDGLMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASKHSA 164
Cdd:cd07618    73 lgEESLIGKMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 165 STG---ATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEELIPGLESYIND 241
Cdd:cd07618   153 TNFqamPSKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDK 232

                         250
                  ....*....|....
gi 1655533408 242 NEMKPVYGYPLEEH 255
Cdd:cd07618   233 WMEKPAFGTPLEEH 246
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 265-412 1.24e-51

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 175.81  E-value: 1.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 265 LPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACClTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYPEW 344
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGP-DVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655533408 345 MAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQ 412
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 263-439 4.36e-49

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: 170.14  E-value: 4.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  263 IALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDaCCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYP 342
Cdd:smart00324   3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFD-SGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  343 EWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQEDVNTMVMNm 422
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI- 160

                          170
                   ....*....|....*..
gi 1655533408  423 staNNSSLIVDQLITYA 439
Cdd:smart00324 161 ---RHQNTVIEFLIENA 174
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
 14-255 1.13e-47

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: 169.07  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  14 QTFSRAGKTEVLTDDLQAADKHVEqirialigLNKRFGNIPNQTIT-----QDSTVKEKRLKKCPEYILGQTMLESAP-- 86
Cdd:cd07619     2 QTVGRAEKTEVLSEDLLQVEKRLE--------LVKQVSHSTHKKLTaclqgQQGVDADKRSKKLPLTTLAQCMVEGAAvl 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  87 -EDGLMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASKHSAS 165
Cdd:cd07619    74 gDDSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 166 T-----GATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEELIPGLESYIN 240
Cdd:cd07619   154 SsnlqpTGAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQE 233

                         250
                  ....*....|....*
gi 1655533408 241 DNEMKPVYGYPLEEH 255
Cdd:cd07619   234 AWVEKPSYGKPLEEH 248
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 265-438 2.48e-47

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: 165.17  E-value: 2.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 265 LPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDacCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYPEW 344
Cdd:cd00159     2 LIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFD--RGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 345 MAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQEDVnTMVMNMST 424
Cdd:cd00159    80 IELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDD-ELLEDIKK 158

                         170
                  ....*....|....
gi 1655533408 425 ANNsslIVDQLITY 438
Cdd:cd00159   159 LNE---IVEFLIEN 169
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 247-443 4.14e-41

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: 148.70  E-value: 4.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 247 VYGYPLEEHLRV-TNRKIALPIQLCVSALLRLGMEEEGLFRI----AGASSKSRRIKLSLDACCLTLPtalEYKDPHVIA 321
Cdd:cd04395     1 TFGVPLDDCPPSsENPYVPLIVEVCCNIVEARGLETVGIYRVpgnnAAISALQEELNRGGFDIDLQDP---RWRDVNVVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 322 GALKSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAI 401
Cdd:cd04395    78 SLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1655533408 402 VIAPNLIWSPQEDVNTMVMNMStanNSSLIVDQLITYADWFF 443
Cdd:cd04395   158 VFGPTLVRTSDDNMETMVTHMP---DQCKIVETLIQHYDWFF 196
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 248-443 1.84e-35

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: 133.03  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 248 YGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACC-LTLPTALEYKDPHVIAGALKS 326
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGeKADISATVYPDINVITGALKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 327 YLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPN 406
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1655533408 407 LIWSPQEDVNTMVMNMStanNSSLIVDQLITYADWFF 443
Cdd:cd04372   161 LMRPPEDSALTTLNDMR---YQILIVQLLITNEDVLF 194
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 22-238 5.82e-30

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: 119.28  E-value: 5.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  22 TEVLTDDLQAADKHVEQIRIALIGLNKRFGNIPNqtiTQDSTVKEKRLKKCPEYILGQTMLESAPE---DGLMSFTLQEC 98
Cdd:cd07620    10 TELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQ---SQPGLEAEKRMKKLPLMALSISMAESFKDfdaESSIRRVLEMC 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  99 GRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASK--------------HSA 164
Cdd:cd07620    87 CFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGrsprsggrseevgeHQG 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655533408 165 STGATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEELIPGL-ESY 238
Cdd:cd07620   167 IRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELkENH 241
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 248-443 1.08e-29

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: 116.35  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 248 YGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLD---ACCLTLPTALEYKDPHVIAGAL 324
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDkdpLNVLLISPEDYESDIHSVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 325 KSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIA 404
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1655533408 405 PNLIWSPQEDVNTMvmnmstaNNSSLIVDQLITYADWFF 443
Cdd:cd04398   161 PTLMNAAPDNAADM-------SFQSRVIETLLDNAYQIF 192
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 248-443 2.39e-29

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: 115.51  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 248 YGYPLEeHLRVTNRK---IALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKlslDACCLTLPTALE-YKDPHVIAGA 323
Cdd:cd04404     6 FGVSLQ-FLKEKNPEqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQ---QKYNMGEPVDFDqYEDVHLPAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 324 LKSYLRELPEPLLTHKLYPEWMAAAKITNNEaRLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVI 403
Cdd:cd04404    82 LKTFLRELPEPLLTFDLYDDIVGFLNVDKEE-RVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1655533408 404 APNLIWSPQEDvntmvMNMSTANNSSLIVDQLITYADWFF 443
Cdd:cd04404   161 GPNLLWAKDAS-----MSLSAINPINTFTKFLLDHQDEIF 195
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 247-444 3.19e-29

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: 115.91  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 247 VYGYPLEEHL-----RVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTALEYKDPHVIA 321
Cdd:cd04391     1 LFGVPLSTLLerdqkKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDQVKQHDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 322 GALKSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAI 401
Cdd:cd04391    81 SLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1655533408 402 VIAPNLiWSPQ----EDVNTMVMNMSTANNSSLIVDQLITYAD--WFFP 444
Cdd:cd04391   161 IMAPNL-FPPRgkhsKDNESLQEEVNMAAGCANIMRLLIRYQDllWTVP 208
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 247-407 1.05e-28

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: 113.22  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 247 VYGYPLEEHLRVTNRKI---ALPIQL--CVSALLRLGME-EEGLFRIAGASSKSRRIKLSLDACC-LTLPTALEYKDPHV 319
Cdd:cd04400     1 IFGSPLEEAVELSSHKYngrDLPSVVyrCIEYLDKNRAIyEEGIFRLSGSASVIKQLKERFNTEYdVDLFSSSLYPDVHT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 320 IAGALKSYLRELPEPLLTHKLYPEWMAAAKI-TNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQN 398
Cdd:cd04400    81 VAGLLKLYLRELPTLILGGELHNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRN 160


                  ....*....
gi 1655533408 399 IAIVIAPNL 407
Cdd:cd04400   161 VCIVFSPTL 169
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 267-422 3.13e-28

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: 112.10  E-value: 3.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 267 IQLCVSALLRLGMEEEGLFRIAGASSKSRRI--------KLSLDACcltlptalEYKDPHVIAGALKSYLRELPEPLLTH 338
Cdd:cd04403    20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLrfavdhdeKLDLDDS--------KWEDIHVITGALKLFFRELPEPLFPY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 339 KLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIwSPQEDVNTM 418
Cdd:cd04403    92 SLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLL-RPEQETGNI 170


                  ....
gi 1655533408 419 VMNM 422
Cdd:cd04403   171 AVHM 174
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-237 5.65e-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: 112.81  E-value: 5.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408   1 MKKQFFRVKQLADQTFSRAGKTEvLTDDLQAADKHVEQIRIALIGLNKRfgnIPNQTITQDSTVKEKRLKKCPEYILGQT 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKD---TKGYLQPNPGARAKQTVLEQPEELLAES 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  81 MLE-SAPEDGLMSF--TLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTaVPNILKHKKNLARLILDMDSMRTRYQ 157
Cdd:pfam03114  77 MIEaGKDLGEDSSFgkALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLLKE-FKEIQKHRKKLERKRLDYDAAKTRVK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 158 QAsKHSASTGATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETE-LANTIIQYVKLQRAYHESALHCLEELIPGLE 236
Cdd:pfam03114 156 KA-KKKKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEfVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLG 234


                  .
gi 1655533408 237 S 237
Cdd:pfam03114 235 K 235
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 267-436 1.79e-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: 110.18  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 267 IQLCVSALLRLGMEEEGLFRIAGASSK-SRRIKLSLD---ACCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYP 342
Cdd:cd04374    32 VRKCIEAVETRGINEQGLYRVVGVNSKvQKLLSLGLDpktSTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 343 EWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIwSPQEDVNTMVMNM 422
Cdd:cd04374   112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLL-RPQEETVAAIMDI 190

                         170
                  ....*....|....
gi 1655533408 423 STANnssLIVDQLI 436
Cdd:cd04374   191 KFQN---IVVEILI 201
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 249-438 6.40e-27

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: 108.16  E-value: 6.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 249 GYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSL--DACCLTLpTALEYkDPHVIAGALKS 326
Cdd:cd04385     1 DGPALEDQQLTDNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQL-REGEY-TVHDVADVLKR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 327 YLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPN 406
Cdd:cd04385    79 FLRDLPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPT 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1655533408 407 LIwspQEDVNTMVMNMSTANnsslIVDQLITY 438
Cdd:cd04385   159 LF---QTDEHSVGQTSHEVK----VIEDLIDN 183
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 266-411 9.31e-27

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: 107.77  E-value: 9.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 266 PIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDAcclTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYPEWM 345
Cdd:cd04402    18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNS---GVEVDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYEEWM 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408 346 AAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSP 411
Cdd:cd04402    95 SALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPP 160
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 246-412 5.90e-26

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: 105.66  E-value: 5.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 246 PVYGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEeGLFRIAGASSKSRRIKLSLDACCLTLPTALEYK-DPHVIAGAL 324
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIqDIHSVSSLC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 325 KSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIA 404
Cdd:cd04384    80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159


                  ....*...
gi 1655533408 405 PNLIWSPQ 412
Cdd:cd04384   160 PNLLRSKQ 167
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 262-423 5.97e-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: 105.78  E-value: 5.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 262 KIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLY 341
Cdd:cd04387    15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLYFRELPEPLFTDELY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 342 PEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQEDVNTMVMN 421
Cdd:cd04387    95 PNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKESKIPTNT 174


                  ..
gi 1655533408 422 MS 423
Cdd:cd04387   175 MT 176
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 278-411 2.15e-25

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: 103.67  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 278 GMEEEGLFRIAGASSKSRRIKLSLDacclTLPTALEYKD--PHVIAGALKSYLRELPEPLLTHKLYPEWMAAAKITNNEA 355
Cdd:cd04377    30 GLYTEGIYRKSGSANKIKELRQGLD----TDPDSVNLEDypIHVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQE 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408 356 RLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSP 411
Cdd:cd04377   106 RVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRCP 161
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 258-436 7.07e-25

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: 102.38  E-value: 7.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 258 VTNRKIALPIQL--CVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACcltlPTALEYKD-P-HVIAGALKSYLRELPE 333
Cdd:cd04407     8 LTSNKTSVPIVLekLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQAD----PENVKLENyPiHAITGLLKQWLRELPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 334 PLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPqe 413
Cdd:cd04407    84 PLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRCP-- 161

                         170       180
                  ....*....|....*....|...
gi 1655533408 414 DVNTMVMNMSTANNSSLIVDQLI 436
Cdd:cd04407   162 DSSDPLTSMKDVAKTTTCVEMLI 184
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 247-418 3.91e-23

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: 97.51  E-value: 3.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 247 VYGYPLEEHL----RVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDacCLTLPTALEYKDPHVIAG 322
Cdd:cd04390     2 VFGQRLEDTVayerKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFD--AGERPSFDSDTDVHTVAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 323 ALKSYLRELPEPLLTHKLYPEWMAAAKITN--NEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIA 400
Cdd:cd04390    80 LLKLYLRELPEPVIPWAQYEDFLSCAQLLSkdEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLA 159

                         170
                  ....*....|....*...
gi 1655533408 401 IVIAPNLIWSPQEDVNTM 418
Cdd:cd04390   160 TVFGPNILRPKVEDPATI 177
BAR smart00721
BAR domain;
1-233 5.22e-23

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 98.61  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408    1 MKKQFFRVKQLADQTFSRAGKTEvLTDDLQAADKHVEQIRIALIGLNKRFGN--IPNQTITQDSTVKEKRLKKCPEYILG 78
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLylQPNPAVRAKLASQKKLSKSLGEVYEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408   79 QTMLESAPEDGLMSFTLQECGRAQTCLAnEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQ 158
Cdd:smart00721  81 GDDGEGLGADSSYGKALDKLGEALKKLL-QVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408  159 ASKHSASTGATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMSRETE-LANTIIQYVKLQRAYHESALHCLEELIP 233
Cdd:smart00721 160 AKKSKEKKKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQQ 235
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 248-436 4.04e-22

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: 94.44  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 248 YGYPLEEhLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDAcclTLPTALEYKD--PHVIAGALK 325
Cdd:cd04373     1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQ---DHNLDLVSKDftVNAVAGALK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 326 SYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAP 405
Cdd:cd04373    77 SFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWP 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1655533408 406 NLIwspQEDVNTMvMNMSTANNSSLIVDQLI 436
Cdd:cd04373   157 TLM---RPDFTSM-EALSATRIYQTIIETFI 183
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 267-438 2.51e-21

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: 92.49  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 267 IQLCVSALLRLGMEEEGLFRIAGasSKSRRIKLsldacCLTLPTALEYKD-----PHVIAGALKSYLRELPEPLLTHKLY 341
Cdd:cd04378    20 IKKCTSEIENRALGVQGIYRVSG--SKARVEKL-----CQAFENGKDLVElselsPHDISSVLKLFLRQLPEPLILFRLY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 342 PEWMAAAK---------------ITNNEArLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPN 406
Cdd:cd04378    93 NDFIALAKeiqrdteedkapntpIEVNRI-IRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPT 171

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1655533408 407 LIWSPQEDVNTMVMNMSTANNSSLIVDQLITY 438
Cdd:cd04378   172 LIRPRPGDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 245-407 2.48e-20

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: 90.17  E-value: 2.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 245 KPVYGYPLEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTlpTALEYKDPHVIAGAL 324
Cdd:cd04375     2 KNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDN--VNYDGQQAYDVADML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 325 KSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIA 404
Cdd:cd04375    80 KQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLA 159


                  ...
gi 1655533408 405 PNL 407
Cdd:cd04375   160 PSL 162
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 252-422 5.36e-20

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: 88.25  E-value: 5.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 252 LEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTALEYKDPHVIAGALKSYLREL 331
Cdd:cd04383     7 LEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNDHDINSVAGVLKLYFRGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 332 PEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSP 411
Cdd:cd04383    87 ENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPVP 166

                         170
                  ....*....|....*....
gi 1655533408 412 --------QEDVNTMVMNM 422
Cdd:cd04383   167 egqdqvscQAHVNELIKTI 185
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 270-420 7.06e-20

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: 88.12  E-value: 7.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 270 CVSALLRLGMEEEGLFRIAGASSKSRRIKLSLdaccL---TLPTaLEYKDPHVIAGALKSYLRELPEPLLTHKLYPEWMA 346
Cdd:cd04382    24 CVNEIEARGLTEEGLYRVSGSEREVKALKEKF----LrgkTVPN-LSKVDIHVICGCLKDFLRSLKEPLITFALWKEFME 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655533408 347 AAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDiNKMSPQNIAIVIAPNLIWSPQEDVNTMVM 420
Cdd:cd04382    99 AAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYSVPNPDPMTI 171
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 253-442 1.07e-19

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: 88.19  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 253 EEHLRVTNRKIALPIQL--CVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTaLEYKDPHVIAGALKSYLRE 330
Cdd:cd04397    15 DSTLGVGPGKLRIPALIddIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPD-LSKENPVQLAALLKKFLRE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 331 LPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDI-----NKMSPQNIAIVIAP 405
Cdd:cd04397    94 LPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKMDIHNLATVITP 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1655533408 406 NLIWSPQEDVNtmvmnmsTANNSSL---IVDQLITYADWF 442
Cdd:cd04397   174 NILYSKTDNPN-------TGDEYFLaieAVNYLIENNEEF 206
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 247-407 1.64e-19

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: 87.14  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 247 VYGYPLE--EHLRVTNrKIALP---IQLCVSALLRLGMEeeGLFRIAGASSKSRRIKLSLDA--CCLTlpTALeykdPHV 319
Cdd:cd04394     1 VFGVPLHslPHSTVPE-YGNVPkflVDACTFLLDHLSTE--GLFRKSGSVVRQKELKAKLEGgeACLS--SAL----PCD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 320 IAGALKSYLRELPEPLLTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNI 399
Cdd:cd04394    72 VAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNL 151


                  ....*...
gi 1655533408 400 AIVIAPNL 407
Cdd:cd04394   152 AVIFAPNL 159
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 248-414 3.87e-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: 86.37  E-value: 3.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 248 YGYPLEEHLR--VTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLD----ACCLTlptALEYKDPHVIA 321
Cdd:cd04379     1 FGVPLSRLVEreGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFErnsaAVELS---EELYPDINVIT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 322 GALKSYLRELPEPLLTHKLYPEWMAAA-------KITNNEARLRalwdVLHKLPPANLENLRFLIKFLAVLTKNQDINKM 394
Cdd:cd04379    78 GVLKDYLRELPEPLITPQLYEMVLEALavalpndVQTNTHLTLS----IIDCLPLSAKATLLLLLDHLSLVLSNSERNKM 153

                         170       180
                  ....*....|....*....|
gi 1655533408 395 SPQNIAIVIAPNLIWSPQED 414
Cdd:cd04379   154 TPQNLAVCFGPVLMFCSQEF 173
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 273-427 4.24e-19

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: 86.36  E-value: 4.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 273 ALLRLGMEEEGLFRIAGASSKSRRIKLSLDACcLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYPEWMAAAKIT- 351
Cdd:cd04392    18 EYLEKNLRVEGLFRKPGNSARQQELRDLLNSG-TDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLCq 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 352 -----------NNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQEDVNTMVM 420
Cdd:cd04392    97 fdekgnktsapDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHE 176


                  ....*..
gi 1655533408 421 NMSTANN 427
Cdd:cd04392   177 NAQKLNS 183
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 262-407 5.23e-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: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 262 KIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDAcclTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLY 341
Cdd:cd04381    19 DLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNR---RESPNLEEYEPPTVASLLKQYLRELPEPLLTKELM 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408 342 PEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNL 407
Cdd:cd04381    96 PRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPTV 161
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 270-408 9.30e-18

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: 82.49  E-value: 9.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 270 CVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDacCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLYPEWMAAAK 349
Cdd:cd04376    16 CCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFD--RGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFIGTAL 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 350 ItNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKN-QDI----------NKMSPQNIAIVIAPNLI 408
Cdd:cd04376    94 L-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaADSidedgqevsgNKMTSLNLATIFGPNLL 162
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 246-407 2.16e-17

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: 80.97  E-value: 2.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 246 PVYGYPLEE--HLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDacCLTLPTALEYKDPHVIAGA 323
Cdd:cd04393     1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLD--SGEEVDLSKEADVCSAASL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 324 LKSYLRELPEPLLTHKLYPEWM-AAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIV 402
Cdd:cd04393    79 LRLFLQELPEGLIPASLQIRLMqLYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAV 158


                  ....*
gi 1655533408 403 IAPNL 407
Cdd:cd04393   159 FGPDV 163
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 278-437 3.00e-17

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: 80.51  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 278 GMEEEGLFRIAGASSKSRRIKLSLDACCLTLPTAleyKDPHVIAGALKSYLRELPEPLLTHKLYPEwmaaaKITNNEARl 357
Cdd:cd04389    37 GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGL---EDPHVPASLLKLWLRELEEPLIPDALYQQ-----CISASEDP- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 358 RALWDVLHKLPPANLENLRFLIKFLAVLTK--NQDINKMSPQNIAIVIAPNLIWSPQEDVNTMVMNMStanNSSLIVDQL 435
Cdd:cd04389   108 DKAVEIVQKLPIINRLVLCYLINFLQVFAQpeNVAHTKMDVSNLAMVFAPNILRCTSDDPRVIFENTR---KEMSFLRTL 184


                  ..
gi 1655533408 436 IT 437
Cdd:cd04389   185 IE 186
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 263-438 3.04e-17

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: 81.01  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 263 IALPIQLCVSALLRLGMEEEGLFRIAGAssKSRRIKLsldacCLTLPTALEYKD-----PHVIAGALKSYLRELPEPLLT 337
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGA--KSRVEKL-----CQAFENGKDLVElselsPHDISNVLKLYLRQLPEPLIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 338 HKLYPEWMAAAKITNN-----EAR-----------------LRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMS 395
Cdd:cd04409    89 FRLYNEFIGLAKESQHvnetqEAKknsdkkwpnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMS 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1655533408 396 PQNIAIVIAPNLIWSPQEDVNTMVMNMSTANNSSLIVDQLITY 438
Cdd:cd04409   169 ASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 86-233 3.59e-17

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: 80.18  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  86 PEDGLMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMDSMRTRYQQASKHSAS 165
Cdd:cd07307    47 LSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKD 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655533408 166 tgATKIDSLREELEGAEAKVEQCRDHLAAEMFKLMS-RETELANTIIQYVKLQRAYHESALHCLEELIP 233
Cdd:cd07307   127 --SSKLAEAEEELQEAKEKYEELREELIEDLNKLEEkRKELFLSLLLSFIEAQSEFFKEVLKILEQLLP 193
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 256-411 3.01e-15

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: 74.65  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 256 LRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDACCLTLptALEYKDPHVIAGALKSYLRELPEPL 335
Cdd:cd04406     8 LTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSV--NLDDYNIHVIASVFKQWLRDLPNPL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408 336 LTHKLYPEWMAAAKITNNEARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSP 411
Cdd:cd04406    86 MTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRCP 161
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 270-408 1.45e-14

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: 72.93  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 270 CVSALLRLGMEEEGLFRIAGasSKSRRIKLsldacCLTLPTALEYKD-----PHVIAGALKSYLRELPEPLLTHKLYPEW 344
Cdd:cd04408    23 CTAEIENRALGVQGIYRISG--SKARVEKL-----CQAFENGRDLVDlsghsPHDITSVLKHFLKELPEPVLPFQLYDDF 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655533408 345 MAAAKITNN------------EARLRALWDVLHKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLI 408
Cdd:cd04408    96 IALAKELQRdsekaaespsivENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLL 171
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 247-442 6.99e-13

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: 68.59  E-value: 6.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 247 VYGYPLEEHLRVTNRKIAL-------------PIQL--CVSALLRLGMEEEGLFRIAGASSKSRRIKL----------SL 301
Cdd:cd04396     1 VFGVSLEESLKYASVAISIvdedgeqyvygyiPVVVakCGVYLKENATEVEGIFRVAGSSKRIRELQLifstppdygkSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 302 DACCLTLptaleykdpHVIAGALKSYLRELPEPLLTHKLY----------PEWMAAAKITNNE-------ARLRALWDVL 364
Cdd:cd04396    81 DWDGYTV---------HDAASVLRRYLNNLPEPLVPLDLYeefrnplrkrPRILQYMKGRINEplntdidQAIKEYRDLI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655533408 365 HKLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPQEDvntmvMNMSTANNSSLIVDQLITYADWF 442
Cdd:cd04396   152 TRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDHE-----MDPKEYKLSRLVVEFLIEHQDKF 224
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
 73-241 6.22e-10

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: 60.02  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  73 PEYILGQTMLESA---PEDGLMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDM 149
Cdd:cd07592    65 PEGLLGEVMLKYGrelGEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 150 DSMRTRyqqaskhsastGATKIDslrEELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLE 229
Cdd:cd07592   145 DYKKRK-----------QGKGPD---EELKQAEEKFEESKELAENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILE 210

                         170
                  ....*....|..
gi 1655533408 230 ELIPGLESYIND 241
Cdd:cd07592   211 ELQSKLQERISE 222
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 263-437 8.24e-06

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: 47.18  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 263 IALPIQL-CVSALLRLGMEEEGLFRIAGASSksrRIKLSLDACCLTLPTALEYKDPHVIAGALKSYLRELPEPLLTHKLY 341
Cdd:cd04388    14 VAPPLLIkLVEAIEKKGLESSTLYRTQSSSS---LTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 342 PEWMAAAK-ITNNEARLRALWDVLH--KLPPANLENLRFLIKFLAVLTKNQDINKMSPQNIAIVIAPNLIWSPqedvntm 418
Cdd:cd04388    91 SEMISRAQeVQSSDEYAQLLRKLIRspNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQ------- 163

                         170
                  ....*....|....*....
gi 1655533408 419 VMNMSTANNSSLIVDQLIT 437
Cdd:cd04388   164 PASSDSPEFHIRIIEVLIT 182
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 74-241 1.16e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; 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 three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 47.31  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  74 EYILGQTMLESAPEDGLMS---FTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMD 150
Cdd:cd07613    66 EALLAEAMLKFGRELGDECnfgPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFD 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 151 SMRTRyqqaskhsasTGATKIDSLREELEgaeaKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEE 230
Cdd:cd07613   146 YKKKR----------QGKIPDEELRQALE----KFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQ 211

                         170
                  ....*....|.
gi 1655533408 231 LIPGLESYIND 241
Cdd:cd07613   212 VTVKLEDRIRE 222
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 228-411 1.41e-05

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: 46.95  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 228 LEELI----PGLESYINDNEMKPvygyplEEHLRVTNRKIALPIQLCVSALLRLGMEEEGLFRIAGASSKSRRIKLSLDA 303
Cdd:cd04380    17 LETLIrlpdPGIRNLIDQLELGD------NPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPGLPSEPGELLAEIRD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 304 CcltLPTALEY---KDPHVIAGALKSYLRELPEPLLTHKLYPEwmAAAKITNNEarlRALWDVL-HKLPPANLENLRFLI 379
Cdd:cd04380    91 A---LDTGSPFnspGSAESVAEALLLFLESLPDPIIPYSLYER--LLEAVANNE---EDKRQVIrISLPPVHRNVFVYLC 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1655533408 380 KFLAVLTKNQDINKMSPQNIAIVIAPNLIWSP 411
Cdd:cd04380   163 SFLRELLSESADRGLDENTLATIFGRVLLRDP 194
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 130-233 1.84e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 46.58  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 130 TAVPNILKHKknlARLILDMDSMRTRYQQA------SKHSASTGATKIDSLREELEGAEA-------KVEQCRDHLAAEM 196
Cdd:cd07596   103 QAVKETLDDR---ADALLTLQSLKKDLASKkaqlekLKAAPGIKPAKVEELEEELEEAESaleearkRYEEISERLKEEL 179

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1655533408 197 --FKLmSRETELANTIIQYVKLQRAYHESALHCLEELIP 233
Cdd:cd07596   180 krFHE-ERARDLKAALKEFARLQVQYAEKIAEAWESLLP 217
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
 73-231 1.33e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; 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. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A2 (or endophilin-2) is also referred to as SH3P8 (SH3 domain containing protein 8) or SH3GL1 (SH3 domain containing Grb2-like protein 1). It localizes to presynaptic nerve terminals and forms heterodimers with endophilin-A1 through their BAR domains. Endophilin-A2 binds dynamin 1, synaptojanin 1, and the beta1-adrenergic receptor cytoplasmic tail through its SH3 domain.


Pssm-ID: 153298  Cd Length: 223  Bit Score: 43.93  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  73 PEYILGQTMLESAPEDGLMSF---TLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDM 149
Cdd:cd07614    65 SEGLLGETMIRYGKELGDESNfgdALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDF 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 150 DSMRTRYQQASKhsastgatkidslrEELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLE 229
Cdd:cd07614   145 DYKKKRQGKIPD--------------EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILD 210


                  ..
gi 1655533408 230 EL 231
Cdd:cd07614   211 EL 212
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
 74-240 3.67e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; 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 that interacts 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. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A3 (or endophilin-3) is also referred to as SH3P13 (SH3 domain containing protein 13) or SH3GL3 (SH3 domain containing Grb2-like protein 3). It regulates Arp2/3-dependent actin filament assembly during endocytosis. It binds N-WASP through its SH3 domain and enhances the ability of N-WASP to activate the Arp2/3 complex. Endophilin-A3 co-localizes with the vesicular glutamate transporter 1 (VGLUT1), and may play an important role in the synaptic release of glutamate.


Pssm-ID: 153299  Cd Length: 223  Bit Score: 42.70  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  74 EYILGQTMLESAPE---DGLMSFTLQECGRAQTCLANEIIEHEAKVEQYVAIPLQHILDTAVPNILKHKKNLARLILDMD 150
Cdd:cd07615    66 EGLLGDCMLRYGRElgeESTFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFD 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 151 SMRTRyqqaskhsastgATKIDSlrEELEGAEAKVEQCRDHLAAEMFKLMSRETELANTIIQYVKLQRAYHESALHCLEE 230
Cdd:cd07615   146 YKKKR------------QGKIPD--EEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILED 211

                         170
                  ....*....|
gi 1655533408 231 LIPGLESYIN 240
Cdd:cd07615   212 LQSKLQNRIS 221
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
 113-233 2.93e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; 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. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153284 [Multi-domain]  Cd Length: 242  Bit Score: 40.03  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 113 EAKVEQYVAI------PLQHILDTAVPNILKHKKNL--ARLILDMdsMRTRYQQASKhsastgATKIDSLREELEGAEAK 184
Cdd:cd07600   121 EARLEQDQLIqkefnaKLRETLNTSFQKAHKARKKVedKRLQLDT--ARAELKSAEP------AEKQEAARVEVETAEDE 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655533408 185 VEQCRDHLAAEMFKLMSrETELANTIIQYVKLQRAYHESALHCLEELIP 233
Cdd:cd07600   193 FVSATEEAVELMKEVLD-NPEPLQLLKELVKAQLAYHKTAAELLEELLS 240
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
 10-238 3.56e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; 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. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain, which can bind and bend membranes. It interacts with amphiphysin 1 and dynamin 1 through its SH3 domain.


Pssm-ID: 153300  Cd Length: 229  Bit Score: 39.67  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  10 QLADQTFSRAGKTEV---LTDDLQAAD-------KHVEQIRIALIglnkrfgniPNQTITQDSTVKEKRLKKCP-----E 74
Cdd:cd07616     1 QFTEEKFGQAEKTELdahLENLLSKAEctkhwteKIMKQTEVLLQ---------PNPNARIEEFVYEKLDRKAPsrmnnP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408  75 YILGQTMLESAPEDG---LMSFTLQECGRAQtclaNEIIEHEAKVEQYVAI----PLQHILDTAVPNILKHKKNLARLIL 147
Cdd:cd07616    72 ELLGQYMIDAGNEFGpgtAYGNALIKCGETQ----KQIGTADRELIQTSAInfltPLRNFIEGDYKTITKERKLLQNKRL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655533408 148 DMDSMRTRYQQASKHSASTGATKidslreelegaEAKVEQCRdhlaaemfklMSRETELANTIIQYVKLQRAYHesaLHC 227
Cdd:cd07616   148 DLDAAKTRLKKAKVAEARAAAEQ-----------ELRITQSE----------FDRQAEITRLLLEGISSTHAHH---LRC 203

                         250
                  ....*....|.
gi 1655533408 228 LEELIPGLESY 238
Cdd:cd07616   204 LNDFVEAQMTY 214
 
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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