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Conserved domains on  [gi|1958649178|ref|XP_006230256|]
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rho GTPase-activating protein 17 isoform X3 [Rattus norvegicus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10166313)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 13-257 0e+00

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: 528.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQL-EESLLG 91
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLgEESLIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  92 KMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPS 171
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 172 KIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPAFG 251
Cdd:cd07618   161 KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAFG 240


                  ....*.
gi 1958649178 252 TPLEEH 257
Cdd:cd07618   241 TPLEEH 246
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 246-446 1.01e-123

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: 369.86  E-value: 1.01e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 246 EKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSH--LDEFYSDPHAVAGA 323
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 324 LKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958649178 404 GPNLLWAKQEGTLAEIAAATSVHVVAVIEPIIQHADWFFPGEV 446
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
 
Name Accession Description Interval E-value
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 13-257 0e+00

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: 528.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQL-EESLLG 91
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLgEESLIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  92 KMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPS 171
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 172 KIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPAFG 251
Cdd:cd07618   161 KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAFG 240


                  ....*.
gi 1958649178 252 TPLEEH 257
Cdd:cd07618   241 TPLEEH 246
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 246-446 1.01e-123

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: 369.86  E-value: 1.01e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 246 EKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSH--LDEFYSDPHAVAGA 323
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 324 LKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958649178 404 GPNLLWAKQEGTLAEIAAATSVHVVAVIEPIIQHADWFFPGEV 446
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-239 8.17e-71

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: 232.61  E-value: 8.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178   1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQE 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  81 ASAQL-EESLLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAeVEIPNIQKQRKQLARLVLDWDSVRARWNQAH 159
Cdd:pfam03114  80 AGKDLgEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 160 --KSSGTNFQGlpskidTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYG-KFFVTLLEAQADYHRKALAVLEKALPE 236
Cdd:pfam03114 159 kkKSSKAKDES------QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVvNQLVAFVEAQLDFHRQCYQLLEQLQQQ 232


                  ...
gi 1958649178 237 MRA 239
Cdd:pfam03114 233 LGK 235
BAR smart00721
BAR domain;
1-237 4.91e-61

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 206.08  E-value: 4.91e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178    1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQ- 79
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178   80 -EASAQLEE-SLLGKMLETCGDAENQLAFELSQHeVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQ 157
Cdd:smart00721  81 gDDGEGLGAdSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  158 AHKSSGTNFQglpSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKE-GEYGKFFVTLLEAQADYHRKALAVLEKALPE 236
Cdd:smart00721 160 AKKSKEKKKD---EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRvDFFVNCLQALIEAQLNFHRESYKLLQQLQQQ 236


                   .
gi 1958649178  237 M 237
Cdd:smart00721 237 L 237
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 267-412 1.75e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 184.67  E-value: 1.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 267 LPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALD-CSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWT 345
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDrGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649178 346 QVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQ 412
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 263-438 1.94e-54

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: 185.55  E-value: 1.94e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  263 REIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS-HLDEFYSDPHAVAGALKSYLRELPEPLMTFSLY 341
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  342 EEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQEGTLAEIAa 421
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD- 159

                          170
                   ....*....|....*..
gi 1958649178  422 atSVHVVAVIEPIIQHA 438
Cdd:smart00324 160 --IRHQNTVIEFLIENA 174
 
Name Accession Description Interval E-value
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 13-257 0e+00

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: 528.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQL-EESLLG 91
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLgEESLIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  92 KMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPS 171
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 172 KIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPAFG 251
Cdd:cd07618   161 KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAFG 240


                  ....*.
gi 1958649178 252 TPLEEH 257
Cdd:cd07618   241 TPLEEH 246
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 246-446 1.01e-123

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: 369.86  E-value: 1.01e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 246 EKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSH--LDEFYSDPHAVAGA 323
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 324 LKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958649178 404 GPNLLWAKQEGTLAEIAAATSVHVVAVIEPIIQHADWFFPGEV 446
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 13-257 2.96e-123

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: 370.13  E-value: 2.96e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQLEE-SLLG 91
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLPEYGLAQSMLESSKELPDdSLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  92 KMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGtnFQGLPS 171
Cdd:cd07595    81 KVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSG--GQGAAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 172 KIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPAFG 251
Cdd:cd07595   159 KVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPVFG 238


                  ....*.
gi 1958649178 252 TPLEEH 257
Cdd:cd07595   239 QPLEEH 244
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
 13-257 9.92e-113

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: 343.18  E-value: 9.92e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQL-EESLLG 91
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLgDDSLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  92 KMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSG--TNFQGL 169
Cdd:cd07619    81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGlsSNLQPT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 170 PSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPA 249
Cdd:cd07619   161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240


                  ....*...
gi 1958649178 250 FGTPLEEH 257
Cdd:cd07619   241 YGKPLEEH 248
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-239 8.17e-71

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: 232.61  E-value: 8.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178   1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQE 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  81 ASAQL-EESLLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAeVEIPNIQKQRKQLARLVLDWDSVRARWNQAH 159
Cdd:pfam03114  80 AGKDLgEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 160 --KSSGTNFQGlpskidTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYG-KFFVTLLEAQADYHRKALAVLEKALPE 236
Cdd:pfam03114 159 kkKSSKAKDES------QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVvNQLVAFVEAQLDFHRQCYQLLEQLQQQ 232


                  ...
gi 1958649178 237 MRA 239
Cdd:pfam03114 233 LGK 235
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
 20-238 2.64e-61

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: 207.87  E-value: 2.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  20 EKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQLE-ESLLGKMLETCG 98
Cdd:cd07620     8 DATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDaESSIRRVLEMCC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  99 DAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGtNFQGL--------- 169
Cdd:cd07620    88 FMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSP-RSGGRseevgehqg 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649178 170 ---PSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMR 238
Cdd:cd07620   167 irrANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELK 238
BAR smart00721
BAR domain;
1-237 4.91e-61

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 206.08  E-value: 4.91e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178    1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQ- 79
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178   80 -EASAQLEE-SLLGKMLETCGDAENQLAFELSQHeVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQ 157
Cdd:smart00721  81 gDDGEGLGAdSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  158 AHKSSGTNFQglpSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKE-GEYGKFFVTLLEAQADYHRKALAVLEKALPE 236
Cdd:smart00721 160 AKKSKEKKKD---EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRvDFFVNCLQALIEAQLNFHRESYKLLQQLQQQ 236


                   .
gi 1958649178  237 M 237
Cdd:smart00721 237 L 237
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 267-412 1.75e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 184.67  E-value: 1.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 267 LPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALD-CSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWT 345
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDrGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649178 346 QVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQ 412
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 263-438 1.94e-54

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: 185.55  E-value: 1.94e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  263 REIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS-HLDEFYSDPHAVAGALKSYLRELPEPLMTFSLY 341
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  342 EEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQEGTLAEIAa 421
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD- 159

                          170
                   ....*....|....*..
gi 1958649178  422 atSVHVVAVIEPIIQHA 438
Cdd:smart00324 160 --IRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 267-437 3.51e-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: 176.34  E-value: 3.51e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 267 LPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQ 346
Cdd:cd00159     2 LIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 347 VASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQEGtlaEIAAATSVH 426
Cdd:cd00159    82 LAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSD---DELLEDIKK 158

                         170
                  ....*....|.
gi 1958649178 427 VVAVIEPIIQH 437
Cdd:cd00159   159 LNEIVEFLIEN 169
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-420 1.74e-37

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: 139.01  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEeHLKRSGRE---IALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKS 326
Cdd:cd04404     6 FGVSLQ-FLKEKNPEqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLPAVILKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 327 YLRELPEPLMTFSLYEEWTQVASVQDQDKK---LQYLwttcQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04404    85 FLRELPEPLLTFDLYDDIVGFLNVDKEERVervKQLL----QTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVF 160

                         170
                  ....*....|....*...
gi 1958649178 404 GPNLLWAK-QEGTLAEIA 420
Cdd:cd04404   161 GPNLLWAKdASMSLSAIN 178
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-442 1.92e-31

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: 121.36  E-value: 1.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALD-----CSTSHLDEFYSDPHAVAGAL 324
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDkdplnVLLISPEDYESDIHSVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 325 KSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLG 404
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958649178 405 PNLLwakqeGTLAEIAAATSVHvVAVIEPIIQHADWFF 442
Cdd:cd04398   161 PTLM-----NAAPDNAADMSFQ-SRVIETLLDNAYQIF 192
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 248-437 2.41e-31

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: 121.46  E-value: 2.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 248 PAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEeGLFRIGAGASKLKKLKAALD---CSTSHLDEFYSDPHAVAGAL 324
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDseqIPDLTKDVYIQDIHSVSSLC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 325 KSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLG 404
Cdd:cd04384    80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958649178 405 PNLLWAKQ--EGTLAEIAAATSVHV-VAVIEPIIQH 437
Cdd:cd04384   160 PNLLRSKQieSACFSGTAAFMEVRIqSVVVEFILNH 195
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 250-441 2.57e-31

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: 121.40  E-value: 2.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEE---HLKRSGREIA-LPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALK 325
Cdd:cd04390     3 FGQRLEDtvaYERKFGPRLVpILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 326 SYLRELPEPLMTFSLYEEWTQVASV--QDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04390    83 LYLRELPEPVIPWAQYEDFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVF 162

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958649178 404 GPNLLWAKQEGTLAEIAAATSV-HVVAVIepIIQHADWF 441
Cdd:cd04390   163 GPNILRPKVEDPATIMEGTPQIqQLMTVM--ISKHEPLF 199
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-408 2.12e-29

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: 115.63  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEhLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS-HLDEFYSDPHAVAGALKSYL 328
Cdd:cd04373     1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNlDLVSKDFTVNAVAGALKSFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 329 RELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04373    80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLM 159
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-442 4.29e-29

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: 114.92  E-value: 4.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLD---EFYSDPHAVAGALKS 326
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADisaTVYPDINVITGALKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 327 YLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPN 406
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958649178 407 LLWAKQEGTLAEIAAATsvHVVAVIEPIIQHADWFF 442
Cdd:cd04372   161 LMRPPEDSALTTLNDMR--YQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 268-409 5.37e-28

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: 111.62  E-value: 5.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 268 PIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDcSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQV 347
Cdd:cd04402    18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLN-SGVEVDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYEEWMSA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649178 348 ASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLW 409
Cdd:cd04402    97 LDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLW 158
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 249-442 1.07e-27

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: 110.95  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 249 AFGTPLEEHLKRSGRE-IALPIEACVMLLLETGMKEEGLFRI---GAGASKLKK-LKAALDCSTSHlDEFYSDPHAVAGA 323
Cdd:cd04395     1 TFGVPLDDCPPSSENPyVPLIVEVCCNIVEARGLETVGIYRVpgnNAAISALQEeLNRGGFDIDLQ-DPRWRDVNVVSSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 324 LKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04395    80 LKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVF 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958649178 404 GPNLLWAKQEGTlaEIAAATSVHVVAVIEPIIQHADWFF 442
Cdd:cd04395   160 GPTLVRTSDDNM--ETMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 280-408 6.73e-27

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: 108.29  E-value: 6.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 280 GMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQY 359
Cdd:cd04377    30 GLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERVRA 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958649178 360 LWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04377   110 LYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCIL 158
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 255-419 1.54e-26

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: 107.86  E-value: 1.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 255 EEHLKRSGREIalpIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAAL----DCSTSHLDEFYS--DPHAVAGALKSYL 328
Cdd:cd04374    21 EAQLDDIGFKF---VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDNSewEIKTITSALKTYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 329 RELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04374    98 RNLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLL 177

                         170
                  ....*....|.
gi 1958649178 409 WAKQEgTLAEI 419
Cdd:cd04374   178 RPQEE-TVAAI 187
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 250-407 2.80e-26

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: 106.67  E-value: 2.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREI---ALPIEA--CVMLLLETG-MKEEGLFRIGAGASKLKKLKAALD-------CStshlDEFYSD 316
Cdd:cd04400     2 FGSPLEEAVELSSHKYngrDLPSVVyrCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNteydvdlFS----SSLYPD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 317 PHAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQY-LWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMT 395
Cdd:cd04400    78 VHTVAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRSQRALeLKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMN 157

                         170
                  ....*....|..
gi 1958649178 396 PSNIAIVLGPNL 407
Cdd:cd04400   158 LRNVCIVFSPTL 169
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 250-413 3.97e-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: 3.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDcstsH------LDEFYSDPHAVAGA 323
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVD----HdekldlDDSKWEDIHVITGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 324 LKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04403    77 LKLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVF 156

                         170
                  ....*....|
gi 1958649178 404 GPNLLWAKQE 413
Cdd:cd04403   157 GPTLLRPEQE 166
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 251-437 7.13e-26

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: 105.08  E-value: 7.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 251 GTPLEEH-LKRSGreIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAAL--DCSTSHLDEFYSDPHAVAGALKSY 327
Cdd:cd04385     2 GPALEDQqLTDND--IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQLREGEYTVHDVADVLKRF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 328 LRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNL 407
Cdd:cd04385    80 LRDLPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTL 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958649178 408 LWAKqegtlaEIAAATSVHVVAVIEPIIQH 437
Cdd:cd04385   160 FQTD------EHSVGQTSHEVKVIEDLIDN 183
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 72-236 1.64e-25

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: 104.45  E-value: 1.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  72 TALAQNMQEASAQLEESL---LGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDW 148
Cdd:cd07307    31 EKLSEALQELGKELPDLSntdLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDY 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 149 DSVRARWNQAHKSSGTnfqglPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGE-YGKFFVTLLEAQADYHRKAL 227
Cdd:cd07307   111 DAAREKLKKLRKKKKD-----SSKLAEAEEELQEAKEKYEELREELIEDLNKLEEKRKElFLSLLLSFIEAQSEFFKEVL 185


                  ....*....
gi 1958649178 228 AVLEKALPE 236
Cdd:cd07307   186 KILEQLLPY 194
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 280-408 1.43e-24

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: 101.61  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 280 GMKEEGLFRIGAGASKLKKLKAAL--DCSTSHLDEFysdP-HAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKK 356
Cdd:cd04407    30 GLYTEGIYRKSGSANRMKELHQLLqaDPENVKLENY---PiHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQ 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958649178 357 LQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04407   107 LQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLL 158
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 250-407 2.51e-24

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: 100.59  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRS----GREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS-HLDEFysDPHAVAGAL 324
Cdd:cd04381     1 FGASLSLAVERSrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESpNLEEY--EPPTVASLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 325 KSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLG 404
Cdd:cd04381    79 KQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLS 158


                  ...
gi 1958649178 405 PNL 407
Cdd:cd04381   159 PTV 161
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 250-437 2.62e-24

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: 100.96  E-value: 2.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHL--DEFYSDPHAVAGALKSY 327
Cdd:cd04383     3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLadDQNDHDINSVAGVLKLY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 328 LRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNL 407
Cdd:cd04383    83 FRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTL 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958649178 408 LWAKQEGTLAEIAAatsvHVVAVIEPIIQH 437
Cdd:cd04383   163 MPVPEGQDQVSCQA----HVNELIKTIIIH 188
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 250-408 2.67e-24

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: 101.16  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYS--DPHAVAGALKSY 327
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSemDVNAIAGTLKLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 328 LRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNL 407
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160


                  .
gi 1958649178 408 L 408
Cdd:cd04387   161 L 161
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 269-446 1.09e-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: 99.82  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 269 IEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS-HLDEFYSdPHAVAGALKSYLRELPEPLMTFSLYEEW--T 345
Cdd:cd04376    13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDvVLDENHS-VHDVAALLKEFFRDMPDPLLPRELYTAFigT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 346 QVASVQDQDKKLQYLwttCQKLPPQNFVNFRYLIKFLAKLAQTSDV-----------NKMTPSNIAIVLGPNLLwAKQEG 414
Cdd:cd04376    92 ALLEPDEQLEALQLL---IYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLL-HKQKS 167

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958649178 415 TLAEIA-----AATSVHVVAVIEPIIQHADWFF--PGEV 446
Cdd:cd04376   168 GEREFVqaslrIEESTAIINVVQTMIDNYEELFmvSPEL 206
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-408 2.36e-22

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: 95.62  E-value: 2.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLE----EHLKRSGREIALPIEACVMLLLETGMkeEGLFRIGAGASKLKKLKAALD----CSTSHLdefysdPHAVA 321
Cdd:cd04394     2 FGVPLHslphSTVPEYGNVPKFLVDACTFLLDHLST--EGLFRKSGSVVRQKELKAKLEggeaCLSSAL------PCDVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 322 GALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAI 401
Cdd:cd04394    74 GLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAV 153


                  ....*..
gi 1958649178 402 VLGPNLL 408
Cdd:cd04394   154 IFAPNLF 160
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 250-437 2.89e-22

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: 95.57  E-value: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLR 329
Cdd:cd04378     1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 330 ELPEPLMTFSLYEEWTQVA----SVQDQDKK----------LQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMT 395
Cdd:cd04378    81 QLPEPLILFRLYNDFIALAkeiqRDTEEDKApntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958649178 396 PSNIAIVLGPNLLWAKQ-EGTLAEIAAATSVHVVAVIEPIIQH 437
Cdd:cd04378   161 PNNLGIVFGPTLIRPRPgDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 248-407 1.02e-21

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: 93.30  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 248 PAFGTPLEEhLKRSGR---EIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGAL 324
Cdd:cd04393     1 KVFGVPLQE-LQQAGQpenGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 325 KSYLRELPEPLMTFSLYEEWTQV-ASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04393    80 RLFLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVF 159


                  ....
gi 1958649178 404 GPNL 407
Cdd:cd04393   160 GPDV 163
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 246-407 1.06e-21

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: 94.41  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 246 EKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDefYSDPHA--VAGA 323
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVN--YDGQQAydVADM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 324 LKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVL 403
Cdd:cd04375    79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCL 158


                  ....
gi 1958649178 404 GPNL 407
Cdd:cd04375   159 APSL 162
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-443 1.55e-21

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: 93.95  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRS-----GREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDcSTSHLDEFYSD---PHAVA 321
Cdd:cd04391     2 FGVPLSTLLERDqkkvpGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELE-AKFYEGTFLWDqvkQHDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 322 GALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAI 401
Cdd:cd04391    81 SLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958649178 402 VLGPNL-----LWAKQEGTLAE--IAAATSVHvvaVIEPIIQHAD--WFFP 443
Cdd:cd04391   161 IMAPNLfpprgKHSKDNESLQEevNMAAGCAN---IMRLLIRYQDllWTVP 208
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-411 1.67e-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: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGRE-----------IALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSD-P 317
Cdd:cd04397     1 FGVPLEILVEKFGADstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 318 HAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDV-----N 392
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgS 160

                         170
                  ....*....|....*....
gi 1958649178 393 KMTPSNIAIVLGPNLLWAK 411
Cdd:cd04397   161 KMDIHNLATVITPNILYSK 179
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 250-432 3.95e-20

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: 89.45  E-value: 3.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSG--REIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLD---EFYSDPHAVAGAL 324
Cdd:cd04379     1 FGVPLSRLVEREGesRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVElseELYPDINVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 325 KSYLRELPEPLMTFSLYEEWTQVASVQ-----DQDKKLQYLWTTCqkLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNI 399
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVAlpndvQTNTHLTLSIIDC--LPLSAKATLLLLLDHLSLVLSNSERNKMTPQNL 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958649178 400 AIVLGPNLLWAKQEGTLAEIAAATSVHVVAVIE 432
Cdd:cd04379   159 AVCFGPVLMFCSQEFSRYGISPTSKMAAVSTVD 191
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 250-437 1.02e-19

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: 88.33  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS--HLDEFYsdPHAVAGALKSY 327
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDlvELSELS--PHDISNVLKLY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 328 LRELPEPLMTFSLYEEWTQVA-----------SVQDQDKKLQYLWTTC-----------QKLPPQNFVNFRYLIKFLAKL 385
Cdd:cd04409    79 LRQLPEPLILFRLYNEFIGLAkesqhvnetqeAKKNSDKKWPNMCTELnrillkskdllRQLPAPNYNTLQFLIVHLHRV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958649178 386 AQTSDVNKMTPSNIAIVLGPNLLWAKQegTLAEIAAATSV---HVVAVIEPIIQH 437
Cdd:cd04409   159 SEQAEENKMSASNLGIIFGPTLIRPRP--TDATVSLSSLVdypHQARLVELLITY 211
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 250-408 8.92e-19

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: 85.05  E-value: 8.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEhLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLR 329
Cdd:cd04406     1 FGVELSR-LTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649178 330 ELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04406    80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 250-437 2.74e-17

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: 81.02  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLR 329
Cdd:cd04408     1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 330 ELPEPLMTFSLYEEWTQVASVQDQDKK------------LQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPS 397
Cdd:cd04408    81 ELPEPVLPFQLYDDFIALAKELQRDSEkaaespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958649178 398 NIAIVLGPNLLWAKQEGTLAEIAAATSVHVVAVIEPIIQH 437
Cdd:cd04408   161 NLGIVFGPTLLRPLVGGDVSMICLLDTGYQAQLVEFLISN 200
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 274-412 1.74e-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: 1.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 274 MLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTS-HLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVA---- 348
Cdd:cd04392    17 IEYLEKNLRVEGLFRKPGNSARQQELRDLLNSGTDlDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIAdlcq 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649178 349 --------SVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQ 412
Cdd:cd04392    97 fdekgnktSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRN 168
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 250-441 1.90e-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: 79.38  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEEHLKRSGREIAL-------------PI--EACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFY 314
Cdd:cd04396     2 FGVSLEESLKYASVAISIvdedgeqyvygyiPVvvAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSFD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 315 SDP---HAVAGALKSYLRELPEPLMTFSLYEEW-----------------TQVASVQDQDKKLQYLWTTCQKLPPQNFVN 374
Cdd:cd04396    82 WDGytvHDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkgrINEPLNTDIDQAIKEYRDLITRLPNLNRQL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649178 375 FRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQEgtlaEIAAATSVHVVAVIEPIIQHADWF 441
Cdd:cd04396   162 LLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDH----EMDPKEYKLSRLVVEFLIEHQDKF 224
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 275-408 4.24e-16

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: 77.05  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 275 LLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFySDPHAVAGALKSYLRELPEPLMTFSLYEEwtQVASVQDQD 354
Cdd:cd04389    32 VLALGGFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGL-EDPHVPASLLKLWLRELEEPLIPDALYQQ--CISASEDPD 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649178 355 KKLQYLwttcQKLPPQNFVNFRYLIKFLAKLAQTSDV--NKMTPSNIAIVLGPNLL 408
Cdd:cd04389   109 KAVEIV----QKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNIL 160
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 272-407 7.39e-16

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: 76.56  E-value: 7.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 272 CVMLLLETGMKEEGLFRIGAGASKLKKLKAAL--DCSTSHLDEFysDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVAS 349
Cdd:cd04382    24 CVNEIEARGLTEEGLYRVSGSEREVKALKEKFlrGKTVPNLSKV--DIHVICGCLKDFLRSLKEPLITFALWKEFMEAAE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649178 350 VQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQtSDVNKMTPSNIAIVLGPNL 407
Cdd:cd04382   102 ILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTI 158
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 250-408 1.60e-13

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: 70.45  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 250 FGTPLEE--HLKRSGREI------------------ALPIE--ACVMLLLETGMKEEGLFRIGAGASKLKKLKA----AL 303
Cdd:cd04380    13 FGSSLETliRLPDPGIRNlidqlelgdnpdysevplSIPKEiwRLVDYLYTRGLAQEGLFEEPGLPSEPGELLAeirdAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 304 DCSTSHLDEFysDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKlQYLWttcQKLPPQNFVNFRYLIKFLA 383
Cdd:cd04380    93 DTGSPFNSPG--SAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNEEDKR-QVIR---ISLPPVHRNVFVYLCSFLR 166

                         170       180
                  ....*....|....*....|....*
gi 1958649178 384 KLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04380   167 ELLSESADRGLDENTLATIFGRVLL 191
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 279-408 3.37e-12

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: 66.05  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 279 TGMKEEGLFRiGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVA-SVQDQDKKL 357
Cdd:cd04388    29 KGLESSTLYR-TQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMISRAqEVQSSDEYA 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958649178 358 QYL--WTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLL 408
Cdd:cd04388   108 QLLrkLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
 74-233 5.31e-10

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


Pssm-ID: 153276  Cd Length: 223  Bit Score: 60.40  E-value: 5.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  74 LAQNMQEASAQL-EESLLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVR 152
Cdd:cd07592    69 LGEVMLKYGRELgEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYDYKK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 153 ARwnqahKSSGTNfqglpskidtlkEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEK 232
Cdd:cd07592   149 RK-----QGKGPD------------EELKQAEEKFEESKELAENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEE 211


                  .
gi 1958649178 233 A 233
Cdd:cd07592   212 L 212
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 25-232 1.66e-08

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 55.78  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  25 LSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAE----------RRHKKLP-----LTALAQNMQEASAQL-EES 88
Cdd:cd07613     5 LDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKlsmintmskiRGQEKGPgypqaEALLAEAMLKFGRELgDEC 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  89 LLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARwnqahkssgtnfQG 168
Cdd:cd07613    85 NFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKR------------QG 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649178 169 lpsKIDtlKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEK 232
Cdd:cd07613   153 ---KIP--DEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQ 211
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
 70-232 1.08e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A2 (or endophilin-2) is also referred to as SH3P8 (SH3 domain containing protein 8) or SH3GL1 (SH3 domain containing Grb2-like protein 1). It localizes to presynaptic nerve terminals and forms heterodimers with endophilin-A1 through their BAR domains. Endophilin-A2 binds dynamin 1, synaptojanin 1, and the beta1-adrenergic receptor cytoplasmic tail through its SH3 domain.


Pssm-ID: 153298  Cd Length: 223  Bit Score: 53.56  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  70 PLTALAQNMQEASAQL-EESLLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDW 148
Cdd:cd07614    65 SEGLLGETMIRYGKELgDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDF 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 149 DSVRARwnqahkssgtnfQG-LPSkidtlkEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKAL 227
Cdd:cd07614   145 DYKKKR------------QGkIPD------EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAV 206


                  ....*
gi 1958649178 228 AVLEK 232
Cdd:cd07614   207 QILDE 211
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
 86-231 1.22e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins localized at synapses that interacts with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A3 (or endophilin-3) is also referred to as SH3P13 (SH3 domain containing protein 13) or SH3GL3 (SH3 domain containing Grb2-like protein 3). It regulates Arp2/3-dependent actin filament assembly during endocytosis. It binds N-WASP through its SH3 domain and enhances the ability of N-WASP to activate the Arp2/3 complex. Endophilin-A3 co-localizes with the vesicular glutamate transporter 1 (VGLUT1), and may play an important role in the synaptic release of glutamate.


Pssm-ID: 153299  Cd Length: 223  Bit Score: 53.10  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  86 EESLLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARwnqahkssgtn 165
Cdd:cd07615    82 EESTFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFDYKKKR----------- 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649178 166 fQGlpsKIDtlKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLE 231
Cdd:cd07615   151 -QG---KIP--DEEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILE 210
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 139-236 3.81e-05

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


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 45.81  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 139 KQLARLVLDWDSVRARWN----QAHKSSGTNFQGlPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMA--------KEG 206
Cdd:cd07596   110 DDRADALLTLQSLKKDLAskkaQLEKLKAAPGIK-PAKVEELEEELEEAESALEEARKRYEEISERLKEelkrfheeRAR 188

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958649178 207 EYGKFFVTLLEAQADYHRKALAVLEKALPE 236
Cdd:cd07596   189 DLKAALKEFARLQVQYAEKIAEAWESLLPE 218
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
 20-249 2.31e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This subfamily is composed predominantly of uncharacterized fungal proteins with similarity to Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein (MUG137), which may play a role in meiosis and sporulation in fission yeast. MUG137 contains an N-terminal BAR domain and a C-terminal SH3 domain, similar to endophilins. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153277  Cd Length: 215  Bit Score: 43.11  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  20 EKTEvLSEDLLQIER----RLDTVRSMcHHS----HKRLiacfqGQHGTDAERRHKKLPLTALAQNMQEASAQL-EESLL 90
Cdd:cd07593     1 QKTT-LSEEFLELEKeielRKEGMERL-HRSteayVEYL-----SKKKPLLDDKDKCLPVEALGLVMINHGEEFpQDSEY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  91 GKMLETCGDAENQLAfelSQHEVFVEKEIMDPLYGIAE--VEIPNIQKQRKQLarlvldwDSVRARWNQA-HKSSgtnfq 167
Cdd:cd07593    74 GSCLSKLGRAHCKIG---TLQEEFADRLSDTFLANIERslAEMKEYHSARKKL-------ESRRLAYDAAlTKSQ----- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 168 glPSKIDT--LKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEkalpemRAHQDkWA 245
Cdd:cd07593   139 --KAKKEDsrLEEELRRAKAKYEESSEDVEARMVAIKESEADQYRDLTDLLDAELDYHQQSLDVLR------EVRQS-WP 209


                  ....
gi 1958649178 246 EKPA 249
Cdd:cd07593   210 SKSS 213
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
 10-158 4.03e-04

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: 42.76  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  10 QLANQTVGRAEKTEvLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAE-------RRHKKLPLTA---LAQNMQ 79
Cdd:cd07594     1 QFTEEKLGTAEKTE-YDAHFENLLQRADKTKVWTEKILKQTEAVLQPNPNVRVEdfiyeklDRKKPDRLSNleqLGQAMI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178  80 EASAQLEESL-LGKMLETCGDAENQLAfeLSQHEvFVEK---EIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARW 155
Cdd:cd07594    80 EAGNDFGPGTaYGSALIKVGQAQKKLG--QAERE-FIQTsssNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACKTRV 156


                  ...
gi 1958649178 156 NQA 158
Cdd:cd07594   157 KKA 159
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 293-385 8.99e-03

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: 38.47  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649178 293 ASKLK---KLKAALDCSTSHLDEFYS----DPHAVAGALKSYLRELPEPLMTFSLYEEWTQV-----ASVQDQD-KKLQY 359
Cdd:cd04399    47 PVSLKethQLRNLLNKPKKPDKEVIIlkkfEPSTVASVLKLYLLELPDSLIPHDIYDLIRSLysaypPSQEDSDtARIQG 126

                          90       100
                  ....*....|....*....|....*.
gi 1958649178 360 LWTTCQKLPPQNFVNFRYLIKFLAKL 385
Cdd:cd04399   127 LQSTLSQLPKSHIATLDAIITHFYRL 152
 
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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