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Conserved domains on  [gi|1958788712|ref|XP_038934763|]
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SH3 domain-binding protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 1-211 1.42e-104

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.


The actual alignment was detected with superfamily member cd07620:

Pssm-ID: 472257  Cd Length: 257  Bit Score: 316.88  E-value: 1.42e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   1 MDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKS 80
Cdd:cd07620    50 AEKRMKKLPLMALSISMAESFKDFDAESSIRRVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  81 LQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYA 160
Cdd:cd07620   130 FAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYA 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958788712 161 NYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAapfSRVYG 211
Cdd:cd07620   210 NYFIRLLELQAEYHKNSLEFLDKNITELKENHSQKEPSVSVSS---QRVYG 257
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 208-409 1.12e-82

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: 258.54  E-value: 1.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 208 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFCSDPHAVAGALK 285
Cdd:cd04386     3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASALK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 286 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 365
Cdd:cd04386    83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958788712 366 NLLWPPEkEGDQAQLDAAsvSSIQVVGVVEVLIQNADTLFPGDI 409
Cdd:cd04386   163 NLLWAKN-EGSLAEMAAG--TSVHVVAIVELIISHADWFFPGEV 203
 
Name Accession Description Interval E-value
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 1-211 1.42e-104

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: 316.88  E-value: 1.42e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   1 MDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKS 80
Cdd:cd07620    50 AEKRMKKLPLMALSISMAESFKDFDAESSIRRVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  81 LQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYA 160
Cdd:cd07620   130 FAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYA 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958788712 161 NYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAapfSRVYG 211
Cdd:cd07620   210 NYFIRLLELQAEYHKNSLEFLDKNITELKENHSQKEPSVSVSS---QRVYG 257
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 208-409 1.12e-82

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: 258.54  E-value: 1.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 208 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFCSDPHAVAGALK 285
Cdd:cd04386     3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASALK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 286 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 365
Cdd:cd04386    83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958788712 366 NLLWPPEkEGDQAQLDAAsvSSIQVVGVVEVLIQNADTLFPGDI 409
Cdd:cd04386   163 NLLWAKN-EGSLAEMAAG--TSVHVVAIVELIISHADWFFPGEV 203
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 223-401 1.24e-55

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.32  E-value: 1.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  223 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPH-SLEEFCSDPHAVAGALKSYLRELPEPLMTSDLY 301
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  302 DDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEgdqaqlD 381
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE------V 154

                          170       180
                   ....*....|....*....|
gi 1958788712  382 AASVSSIQVVGVVEVLIQNA 401
Cdd:smart00324 155 ASLKDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 227-371 5.46e-50

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 170.03  E-value: 5.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 227 LPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS-LEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWM 305
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788712 306 RAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPP 371
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-181 3.82e-21

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: 92.78  E-value: 3.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   1 MDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSeEELPAILKRKKS 80
Cdd:pfam03114  61 AKQTVLEQPEELLAESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  81 LQKLVSDWNTLKSRLSQAAKNSGssqslgggssshthmATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKE-DSY 159
Cdd:pfam03114 140 LERKRLDYDAAKTRVKKAKKKKS---------------SKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEvEFV 204

                         170       180
                  ....*....|....*....|..
gi 1958788712 160 ANYFTHLLEIQADYHRKSLTSL 181
Cdd:pfam03114 205 VNQLVAFVEAQLDFHRQCYQLL 226
BAR smart00721
BAR domain;
4-190 4.33e-14

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 72.03  E-value: 4.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712    4 RVKKLPLMALSTAMAESF------KELDPDSSMGKALEMSCAIQNQLARILAEFeMTLERDVLQPLNRLSEEELPAILKR 77
Cdd:smart00721  61 RAKLASQKKLSKSLGEVYeggddgEGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   78 KKSLQKLVSDWNTLKSRLSQAAKNSGSsqslgggssshthmATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKE- 156
Cdd:smart00721 140 RKKLERKLLDYDSARHKLKKAKKSKEK--------------KKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRv 205

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958788712  157 DSYANYFTHLLEIQADYHRKSLTSLDTALAELRD 190
Cdd:smart00721 206 DFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
 
Name Accession Description Interval E-value
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 1-211 1.42e-104

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: 316.88  E-value: 1.42e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   1 MDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKS 80
Cdd:cd07620    50 AEKRMKKLPLMALSISMAESFKDFDAESSIRRVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  81 LQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYA 160
Cdd:cd07620   130 FAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYA 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958788712 161 NYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAapfSRVYG 211
Cdd:cd07620   210 NYFIRLLELQAEYHKNSLEFLDKNITELKENHSQKEPSVSVSS---QRVYG 257
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 208-409 1.12e-82

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: 258.54  E-value: 1.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 208 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFCSDPHAVAGALK 285
Cdd:cd04386     3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASALK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 286 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 365
Cdd:cd04386    83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958788712 366 NLLWPPEkEGDQAQLDAAsvSSIQVVGVVEVLIQNADTLFPGDI 409
Cdd:cd04386   163 NLLWAKN-EGSLAEMAAG--TSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 1-217 3.96e-70

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: 227.22  E-value: 3.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   1 MDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKS 80
Cdd:cd07595    50 KDKRLKKLPEYGLAQSMLESSKELPDDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  81 LQKLVSDWNTLKSRLSQAAKNSGssqslgggssshtHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYA 160
Cdd:cd07595   130 LSKLVLDMDSARSRYNAAHKSSG-------------GQGAAAKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIA 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788712 161 NYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPlttaapfsrVYGVSLRTH 217
Cdd:cd07595   197 SYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKP---------VFGQPLEEH 244
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 223-401 1.24e-55

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.32  E-value: 1.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  223 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPH-SLEEFCSDPHAVAGALKSYLRELPEPLMTSDLY 301
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  302 DDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEgdqaqlD 381
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE------V 154

                          170       180
                   ....*....|....*....|
gi 1958788712  382 AASVSSIQVVGVVEVLIQNA 401
Cdd:smart00324 155 ASLKDIRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 227-400 1.51e-51

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


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 175.18  E-value: 1.51e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 227 LPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMR 306
Cdd:cd00159     2 LIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 307 AASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEgdqaqlDAASVS 386
Cdd:cd00159    82 LAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSD------DELLED 155

                         170
                  ....*....|....
gi 1958788712 387 SIQVVGVVEVLIQN 400
Cdd:cd00159   156 IKKLNEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 227-371 5.46e-50

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 170.03  E-value: 5.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 227 LPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS-LEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWM 305
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788712 306 RAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPP 371
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 2-217 1.34e-48

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: 170.22  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   2 DKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSL 81
Cdd:cd07618    51 EKRHKKLPLTALAQNMQEGSAQLGEESLIGKMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  82 QKLVSDWNTLKSRLSQAAKNSGSsqslgggssshTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYAN 161
Cdd:cd07618   131 AKLVLDWDSARGRYNQAHKSSGT-----------NFQAMPSKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAK 199

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788712 162 YFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPlttaapfsrVYGVSLRTH 217
Cdd:cd07618   200 FFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKP---------AFGTPLEEH 246
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
 2-189 1.10e-39

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: 145.96  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   2 DKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSL 81
Cdd:cd07619    51 DKRSKKLPLTTLAQCMVEGAAVLGDDSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  82 QKLVSDWNTLKSRLSQAAKNSGSSQSLGGgssshthmaTANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYAN 161
Cdd:cd07619   131 AKLVLDMDSSRTRWQQSSKSSGLSSNLQP---------TGAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYAN 201

                         170       180
                  ....*....|....*....|....*...
gi 1958788712 162 YFTHLLEIQADYHRKSLTSLDTALAELR 189
Cdd:cd07619   202 YFQTLIEVQAEYHRKSLELLQSVLPQIK 229
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 210-405 1.32e-38

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 140.94  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSLrTHLQDLGRD---IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMAS-DPHSLEEFcSDPHAVAGALK 285
Cdd:cd04404     6 FGVSL-QFLKEKNPEqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMgEPVDFDQY-EDVHLPAVILK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 286 SYLRELPEPLMTSDLYDDWMRAASLKEPgARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 365
Cdd:cd04404    84 TFLRELPEPLLTFDLYDDIVGFLNVDKE-ERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958788712 366 NLLWPPEKegdqaqldAASVSSI-QVVGVVEVLIQNADTLF 405
Cdd:cd04404   163 NLLWAKDA--------SMSLSAInPINTFTKFLLDHQDEIF 195
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 210-405 1.08e-32

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


Pssm-ID: 239863  Cd Length: 192  Bit Score: 124.44  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSL-----EEFCSDPHAVAGAL 284
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVllispEDYESDIHSVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 285 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLG 364
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958788712 365 PNLLwppekegDQAQLDAASVSSiqVVGVVEVLIQNADTLF 405
Cdd:cd04398   161 PTLM-------NAAPDNAADMSF--QSRVIETLLDNAYQIF 192
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 218-409 2.62e-32

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 123.18  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 218 LQDLGRDIALP--IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPH-SLEEFCSdpHAVAGALKSYLRELPEP 294
Cdd:cd04402     6 LSNICEDDNLPkpILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEvDLKAEPV--LLLASVLKDFLRNIPGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 295 LMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPeke 374
Cdd:cd04402    84 LLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPP--- 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958788712 375 gDQAQLDAASVSsiQVVGVVEVLIQNADTLFPGDI 409
Cdd:cd04402   161 -ASSELQNEDLK--KVTSLVQFLIENCQEIFGEDI 192
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 210-398 2.62e-32

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


Pssm-ID: 239842  Cd Length: 186  Bit Score: 123.32  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSLrTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFcsDPHAVAGALKSY 287
Cdd:cd04377     1 FGVSL-SSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSvnLEDY--PIHVITSVLKQW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 288 LRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNL 367
Cdd:cd04377    78 LRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCI 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958788712 368 LWPPEKEGDQAQLDAASvssiQVVGVVEVLI 398
Cdd:cd04377   158 LRCPDTADPLQSLQDVS----KTTTCVETLI 184
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 240-372 4.59e-31

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


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 119.71  E-value: 4.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 240 GMQEEGLFRLAAGASVLKRLKQTMASDPHS--LEEFcsdP-HAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGAR 316
Cdd:cd04407    30 GLYTEGIYRKSGSANRMKELHQLLQADPENvkLENY---PiHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQ 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788712 317 LEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPE 372
Cdd:cd04407   107 LQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRCPD 162
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 210-405 4.34e-30

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


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 117.23  E-value: 4.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSL---EEFCSDPHAVAGALKS 286
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKAdisATVYPDINVITGALKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 287 YLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPN 366
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958788712 367 LLWPPEKEGDQAQLDAAsvSSIQvvgVVEVLIQNADTLF 405
Cdd:cd04372   161 LMRPPEDSALTTLNDMR--YQIL---IVQLLITNEDVLF 194
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 209-367 5.60e-30

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 116.69  E-value: 5.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 209 VYGVSLRTHLQ-----DLGRDIALPIEACVLLLLSEG-MQEEGLFRLAAGASVLKRLKQ--------TMASDPhslEEFc 274
Cdd:cd04400     1 IFGSPLEEAVElsshkYNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKErfnteydvDLFSSS---LYP- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 275 sDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLK-EPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNK 353
Cdd:cd04400    77 -DVHTVAGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNK 155

                         170
                  ....*....|....
gi 1958788712 354 MTPSNIAIVLGPNL 367
Cdd:cd04400   156 MNLRNVCIVFSPTL 169
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 208-400 1.74e-28

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


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 112.60  E-value: 1.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 208 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEeGLFRLAAGASVLKRLKQTMAS----DPHSlEEFCSDPHAVAGA 283
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSeqipDLTK-DVYIQDIHSVSSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 284 LKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVL 363
Cdd:cd04384    79 CKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958788712 364 GPNLLWPPEKEGDQAQLDAASVSS-IQVVgVVEVLIQN 400
Cdd:cd04384   159 APNLLRSKQIESACFSGTAAFMEVrIQSV-VVEFILNH 195
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 225-405 2.89e-28

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


Pssm-ID: 239860  Cd Length: 196  Bit Score: 112.11  E-value: 2.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 225 IALPIEACVLLLLSEGMQEEGLFRL---AAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLY 301
Cdd:cd04395    18 VPLIVEVCCNIVEARGLETVGIYRVpgnNAAISALQEELNRGGFDIDLQDPRWRDVNVVSSLLKSFFRKLPEPLFTNELY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 302 DDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLD 381
Cdd:cd04395    98 PDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRTSDDNMETMVTH 177

                         170       180
                  ....*....|....*....|....
gi 1958788712 382 AASVSSIqvvgvVEVLIQNADTLF 405
Cdd:cd04395   178 MPDQCKI-----VETLIQHYDWFF 196
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 223-405 8.43e-28

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: 111.00  E-value: 8.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 223 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYD 302
Cdd:cd04390    20 RLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 303 DWMRAASL--KEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPpekegdQAQl 380
Cdd:cd04390   100 DFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILRP------KVE- 172

                         170       180
                  ....*....|....*....|....*..
gi 1958788712 381 DAASV--SSIQVVGVVEVLIQNADTLF 405
Cdd:cd04390   173 DPATImeGTPQIQQLMTVMISKHEPLF 199
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 217-400 1.41e-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: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 217 HLQDLGRDIalpIEACVLLLLSEGMQEEGLFRLAAGASVLKRLkQTMASDPHSLE----EFCS---DPHAVAGALKSYLR 289
Cdd:cd04374    23 QLDDIGFKF---VRKCIEAVETRGINEQGLYRVVGVNSKVQKL-LSLGLDPKTSTpgdvDLDNsewEIKTITSALKTYLR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 290 ELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLW 369
Cdd:cd04374    99 NLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLR 178

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958788712 370 PPEKegdqaqldaaSVSSIQVVG----VVEVLIQN 400
Cdd:cd04374   179 PQEE----------TVAAIMDIKfqniVVEILIEN 203
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 229-398 1.73e-26

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 106.94  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 229 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCS--DPHAVAGALKSYLRELPEPLMTSDLYDDWMR 306
Cdd:cd04387    20 VRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSemDVNAIAGTLKLYFRELPEPLFTDELYPNFAE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 307 AASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVS 386
Cdd:cd04387   100 GIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKESKIPTNTMTDSW 179

                         170
                  ....*....|..
gi 1958788712 387 SIQVVGVVEVLI 398
Cdd:cd04387   180 SLEVMSQVQVLL 191
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 208-379 2.84e-26

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


Pssm-ID: 239848  Cd Length: 188  Bit Score: 105.97  E-value: 2.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 208 RVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTM--ASDPHSLEEFCSDPHAVAGALK 285
Cdd:cd04383     1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFerGEDPLADDQNDHDINSVAGVLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 286 SYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGP 365
Cdd:cd04383    81 LYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGP 160

                         170
                  ....*....|....
gi 1958788712 366 NLLWPPEkEGDQAQ 379
Cdd:cd04383   161 TLMPVPE-GQDQVS 173
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 229-378 3.40e-26

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


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 105.94  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 229 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLK----QTMASDPHSLEEfcSDPHAVAGALKSYLRELPEPLMTSDLYDDW 304
Cdd:cd04403    20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRfavdHDEKLDLDDSKW--EDIHVITGALKLFFRELPEPLFPYSLFNDF 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788712 305 MRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQA 378
Cdd:cd04403    98 VAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQETGNIA 171
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 216-400 2.78e-25

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 103.16  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 216 THLQD--LGR-DIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSD--PHAVAGALKSYLRE 290
Cdd:cd04385     3 PALEDqqLTDnDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLREGEytVHDVADVLKRFLRD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 291 LPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWP 370
Cdd:cd04385    83 LPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQT 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958788712 371 PEKEGDQAQldaasvssiQVVGVVEVLIQN 400
Cdd:cd04385   163 DEHSVGQTS---------HEVKVIEDLIDN 183
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 209-401 1.27e-24

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


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 101.78  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 209 VYGVSLRT----HLQDLGRDIALPIEACVLLLlsEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEfcSDPHAVAGAL 284
Cdd:cd04394     1 VFGVPLHSlphsTVPEYGNVPKFLVDACTFLL--DHLSTEGLFRKSGSVVRQKELKAKLEGGEACLSS--ALPCDVAGLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 285 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLG 364
Cdd:cd04394    77 KQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFA 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958788712 365 PNLLwppEKEGDQAQLDAASVSSIQV-VGVVEVLIQNA 401
Cdd:cd04394   157 PNLF---QSEEGGEKMSSSTEKRLRLqAAVVQTLIDNA 191
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 240-400 3.27e-24

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


Pssm-ID: 239843  Cd Length: 203  Bit Score: 100.57  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 240 GMQeeGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAA----------- 308
Cdd:cd04378    33 GVQ--GIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYNDFIALAkeiqrdteedk 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 309 SLKEPGARLEALH---DVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDqaqldaASV 385
Cdd:cd04378   111 APNTPIEVNRIIRklkDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIRPRPGDAD------VSL 184

                         170
                  ....*....|....*....
gi 1958788712 386 SSIQVVG----VVEVLIQN 400
Cdd:cd04378   185 SSLVDYGyqarLVEFLITN 203
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 229-409 1.97e-23

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: 98.67  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 229 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTM-ASDPHSLEEFCSdPHAVAGALKSYLRELPEPLMTSDLYDDWMRA 307
Cdd:cd04376    13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFdRGIDVVLDENHS-VHDVAALLKEFFRDMPDPLLPRELYTAFIGT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 308 ASLkEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLA-----------EEQDVNKMTPSNIAIVLGPNLLW---PPEK 373
Cdd:cd04376    92 ALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAehaadsidedgQEVSGNKMTSLNLATIFGPNLLHkqkSGER 170

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958788712 374 EGDQAQLDAAsvSSIQVVGVVEVLIQNADTLF--PGDI 409
Cdd:cd04376   171 EFVQASLRIE--ESTAIINVVQTMIDNYEELFmvSPEL 206
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 223-400 4.60e-23

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


Pssm-ID: 239838  Cd Length: 185  Bit Score: 96.76  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 223 RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDpHSLE--EFCSDPHAVAGALKSYLRELPEPLMTSDL 300
Cdd:cd04373    13 KPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQD-HNLDlvSKDFTVNAVAGALKSFFSELPDPLIPYSM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 301 YDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPpekegDQAQL 380
Cdd:cd04373    92 HLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMRP-----DFTSM 166

                         170       180
                  ....*....|....*....|
gi 1958788712 381 DAASVSSIqVVGVVEVLIQN 400
Cdd:cd04373   167 EALSATRI-YQTIIETFIQQ 185
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 209-405 1.02e-22

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: 96.65  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 209 VYGVSLRTHL-QDLGRD----IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDphsleEFCSD------- 276
Cdd:cd04391     1 LFGVPLSTLLeRDQKKVpgskVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAK-----FYEGTflwdqvk 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 277 PHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTP 356
Cdd:cd04391    76 QHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958788712 357 SNIAIVLGPNL-----LWPPEKEGDQAQLDAASVSSIqvvgVVEVLIQNADTLF 405
Cdd:cd04391   156 WNVAMIMAPNLfpprgKHSKDNESLQEEVNMAAGCAN----IMRLLIRYQDLLW 205
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-181 3.82e-21

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: 92.78  E-value: 3.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   1 MDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSeEELPAILKRKKS 80
Cdd:pfam03114  61 AKQTVLEQPEELLAESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  81 LQKLVSDWNTLKSRLSQAAKNSGssqslgggssshthmATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKE-DSY 159
Cdd:pfam03114 140 LERKRLDYDAAKTRVKKAKKKKS---------------SKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEvEFV 204

                         170       180
                  ....*....|....*....|..
gi 1958788712 160 ANYFTHLLEIQADYHRKSLTSL 181
Cdd:pfam03114 205 VNQLVAFVEAQLDFHRQCYQLL 226
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 208-367 1.24e-20

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 89.83  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 208 RVYGVSLRtHLQDLGR---DIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGAL 284
Cdd:cd04393     1 KVFGVPLQ-ELQQAGQpenGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 285 KSYLRELPEPLMTSDLYDDWMRA-ASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVL 363
Cdd:cd04393    80 RLFLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVF 159


                  ....
gi 1958788712 364 GPNL 367
Cdd:cd04393   160 GPDV 163
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 229-404 1.57e-20

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: 90.50  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 229 IEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSD-PHAVAGALKSYLRELPEPLMTSDLYDDWMRA 307
Cdd:cd04397    31 IDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnPVQLAALLKKFLRELPDPLLTFKLYRLWISS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 308 ASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLA-----EEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDA 382
Cdd:cd04397   111 QKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfshiDEETGSKMDIHNLATVITPNILYSKTDNPNTGDEYF 190

                         170       180
                  ....*....|....*....|..
gi 1958788712 383 ASVSsiqvvgVVEVLIQNADTL 404
Cdd:cd04397   191 LAIE------AVNYLIENNEEF 206
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 244-400 2.52e-20

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


Pssm-ID: 239873  Cd Length: 200  Bit Score: 89.49  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 244 EGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAA---------SLKEPG 314
Cdd:cd04408    35 QGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLYDDFIALAkelqrdsekAAESPS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 315 ARLEALH---DVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPekEGDQAQLDAASVSSIQVV 391
Cdd:cd04408   115 IVENIIRslkELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRPL--VGGDVSMICLLDTGYQAQ 192


                  ....*....
gi 1958788712 392 gVVEVLIQN 400
Cdd:cd04408   193 -LVEFLISN 200
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 209-367 1.39e-19

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 87.86  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 209 VYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYL 288
Cdd:cd04375     4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYF 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958788712 289 RELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNL 367
Cdd:cd04375    84 RDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSL 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 210-388 6.99e-19

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


Pssm-ID: 239844  Cd Length: 207  Bit Score: 85.60  E-value: 6.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSLRTHLQDLG--RDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLE---EFCSDPHAVAGAL 284
Cdd:cd04379     1 FGVPLSRLVEREGesRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVElseELYPDINVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 285 KSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHD---VCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAI 361
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLtlsIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160

                         170       180
                  ....*....|....*....|....*..
gi 1958788712 362 VLGPnLLWPPEKEGDQAQLDAASVSSI 388
Cdd:cd04379   161 CFGP-VLMFCSQEFSRYGISPTSKMAA 186
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 210-367 7.44e-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: 84.79  E-value: 7.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSL-----RTHLQDlGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHS-LEEFcsDPHAVAGA 283
Cdd:cd04381     1 FGASLslaveRSRCHD-GIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPnLEEY--EPPTVASL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 284 LKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVL 363
Cdd:cd04381    78 LKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVL 157


                  ....
gi 1958788712 364 GPNL 367
Cdd:cd04381   158 SPTV 161
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 232-391 2.54e-18

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 83.50  E-value: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 232 CVLLLLSEGMQEEGLFRLAAGASVLKRLKQTM---ASDPHsLEEFcsDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAA 308
Cdd:cd04382    24 CVNEIEARGLTEEGLYRVSGSEREVKALKEKFlrgKTVPN-LSKV--DIHVICGCLKDFLRSLKEPLITFALWKEFMEAA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 309 SLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDvNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSI 388
Cdd:cd04382   101 EILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYSVPNPDPMTILQDTVRQP 179


                  ...
gi 1958788712 389 QVV 391
Cdd:cd04382   180 RVV 182
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 210-372 2.55e-18

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


Pssm-ID: 239871  Cd Length: 186  Bit Score: 83.13  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 210 YGVSLrTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLR 289
Cdd:cd04406     1 FGVEL-SRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 290 ELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLW 369
Cdd:cd04406    80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILR 159


                  ...
gi 1958788712 370 PPE 372
Cdd:cd04406   160 CPD 162
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 225-370 8.36e-18

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 82.55  E-value: 8.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 225 IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDW 304
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 305 M----------------RAASLKEPGARLE------ALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIV 362
Cdd:cd04409    96 IglakesqhvnetqeakKNSDKKWPNMCTElnrillKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGII 175


                  ....*...
gi 1958788712 363 LGPNLLWP 370
Cdd:cd04409   176 FGPTLIRP 183
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 234-405 1.20e-16

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


Pssm-ID: 239857  Cd Length: 208  Bit Score: 79.04  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 234 LLLLSEGMQEEGLFRLAAGASVLKRLKQTMASD-PHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASL-- 310
Cdd:cd04392    17 IEYLEKNLRVEGLFRKPGNSARQQELRDLLNSGtDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLcq 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 311 -KEPGAR---------LEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQL 380
Cdd:cd04392    97 fDEKGNKtsapdkerlLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHE 176

                         170       180
                  ....*....|....*....|....*
gi 1958788712 381 DAASVSSIqvvgvVEVLIQNADTLF 405
Cdd:cd04392   177 NAQKLNSI-----VTFMIKHSQKLF 196
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 209-404 9.67e-16

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 76.68  E-value: 9.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 209 VYGVSLRTHLQD-------LGRD--------IALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEF 273
Cdd:cd04396     1 VFGVSLEESLKYasvaisiVDEDgeqyvygyIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 274 CSDP---HAVAGALKSYLRELPEPLMTSDLYDDWmRAASLKEPG------------------ARLEALHDVCSRLPQENF 332
Cdd:cd04396    81 DWDGytvHDAASVLRRYLNNLPEPLVPLDLYEEF-RNPLRKRPRilqymkgrineplntdidQAIKEYRDLITRLPNLNR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788712 333 NNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVssiqvvgVVEVLIQNADTL 404
Cdd:cd04396   160 QLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDHEMDPKEYKLSRL-------VVEFLIEHQDKF 224
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 234-368 4.58e-15

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 73.96  E-value: 4.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 234 LLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFcSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAAslKEP 313
Cdd:cd04389    31 KVLALGGFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGL-EDPHVPASLLKLWLRELEEPLIPDALYQQCISAS--EDP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788712 314 GARLEalhdVCSRLPQENFNNLRYLMKFLALLAEEQDV--NKMTPSNIAIVLGPNLL 368
Cdd:cd04389   108 DKAVE----IVQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNIL 160
BAR smart00721
BAR domain;
4-190 4.33e-14

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 72.03  E-value: 4.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712    4 RVKKLPLMALSTAMAESF------KELDPDSSMGKALEMSCAIQNQLARILAEFeMTLERDVLQPLNRLSEEELPAILKR 77
Cdd:smart00721  61 RAKLASQKKLSKSLGEVYeggddgEGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   78 KKSLQKLVSDWNTLKSRLSQAAKNSGSsqslgggssshthmATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKE- 156
Cdd:smart00721 140 RKKLERKLLDYDSARHKLKKAKKSKEK--------------KKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRv 205

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958788712  157 DSYANYFTHLLEIQADYHRKSLTSLDTALAELRD 190
Cdd:smart00721 206 DFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 3-185 1.21e-13

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: 69.78  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712   3 KRVKKLP-----LMALSTAMAESFKEL------DPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEEL 71
Cdd:cd07307    14 KDTKKLLdslkeLPAAAEKLSEALQELgkelpdLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  72 PAILKRKKSLQKLVSDWNTLKSRLSQAAKnsgssqslgggssshthmaTANKVETLKEDEEEL---KRKVEQCKDEYLAD 148
Cdd:cd07307    94 KEIKKRRKKLDKARLDYDAAREKLKKLRK-------------------KKKDSSKLAEAEEELqeaKEKYEELREELIED 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958788712 149 LYHF-STKEDSYANYFTHLLEIQADYHRKSLTSLDTAL 185
Cdd:cd07307   155 LNKLeEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLL 192
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 236-375 4.13e-08

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 54.27  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 236 LLSEGMQEEGLFRLAAGASVLKRLKQTM--ASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEp 313
Cdd:cd04380    61 LYTRGLAQEGLFEEPGLPSEPGELLAEIrdALDTGSPFNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNE- 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788712 314 garLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEG 375
Cdd:cd04380   140 ---EDKRQVIRISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAG 198
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 224-399 2.39e-07

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 51.41  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 224 DIALPIeacvLLLLSEGMQEEGL-----FRLAAGASVLKrLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTS 298
Cdd:cd04388    13 DVAPPL----LIKLVEAIEKKGLesstlYRTQSSSSLTE-LRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712 299 DLYDDWMRAA----SLKEPGARLEALHDvCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEke 374
Cdd:cd04388    88 PVYSEMISRAqevqSSDEYAQLLRKLIR-SPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQP-- 164

                         170       180
                  ....*....|....*....|....*
gi 1958788712 375 gdqaqldAASVSSIQVVGVVEVLIQ 399
Cdd:cd04388   165 -------ASSDSPEFHIRIIEVLIT 182
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
 13-188 6.36e-07

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


Pssm-ID: 153278  Cd Length: 229  Bit Score: 50.85  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  13 LSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSLQKLVSDWNTLK 92
Cdd:cd07594    74 LGQAMIEAGNDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  93 SRLSQaAKNsgssqslgggssshthMATANKVET-LKEDEEELKRKVEQCKdeylADLYHFSTKEDSYANYFTHLLEIQA 171
Cdd:cd07594   154 TRVKK-AKS----------------AEAIEQAEQdLRVAQSEFDRQAEITK----LLLEGISSTHANHLRCLRDFVEAQM 212

                         170
                  ....*....|....*..
gi 1958788712 172 DYHRKSLTSLDTALAEL 188
Cdd:cd07594   213 TYYAQCYQYMDDLQRQL 229
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 276-345 3.11e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 45.40  E-value: 3.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788712 276 DPHAVAGALKSYLRELPEPLMTSDLYDDwMRAASLKEPG-------ARLEALHDVCSRLPQENFNNLRYLMKFLALL 345
Cdd:cd04399    77 EPSTVASVLKLYLLELPDSLIPHDIYDL-IRSLYSAYPPsqedsdtARIQGLQSTLSQLPKSHIATLDAIITHFYRL 152
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 10-187 7.38e-03

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: 38.49  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  10 LMALSTAMAESFKEL-DPDSSMGKALE-MSCAIQNQLARILAEFEMTLERDVlqplnRLSEEELPAILKRKKSLQKLVSD 87
Cdd:cd07596    48 LIKLAKCEEEVGGELgEALSKLGKAAEeLSSLSEAQANQELVKLLEPLKEYL-----RYCQAVKETLDDRADALLTLQSL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  88 WNTLKSRLSQAAKnsgssqslgggsSSHTHMATANKVETLKEDEEELKRKVEQCKDEY-------LADLYHFST-KEDSY 159
Cdd:cd07596   123 KKDLASKKAQLEK------------LKAAPGIKPAKVEELEEELEEAESALEEARKRYeeiserlKEELKRFHEeRARDL 190

                         170       180
                  ....*....|....*....|....*...
gi 1958788712 160 ANYFTHLLEIQADYHRKSLTSLDTALAE 187
Cdd:cd07596   191 KAALKEFARLQVQYAEKIAEAWESLLPE 218
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
 13-98 7.88e-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: 38.52  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788712  13 LSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSLQKLVSDWNTLK 92
Cdd:cd07616    74 LGQYMIDAGNEFGPGTAYGNALIKCGETQKQIGTADRELIQTSAINFLTPLRNFIEGDYKTITKERKLLQNKRLDLDAAK 153


                  ....*.
gi 1958788712  93 SRLSQA 98
Cdd:cd07616   154 TRLKKA 159
 
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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