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Conserved domains on  [gi|1621999122|ref|XP_028572986|]
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rho GTPase-activating protein 44 isoform X3 [Podarcis muralis]

Protein Classification

BAR_Rich2 and RhoGAP_nadrin domain-containing protein( domain architecture ID 10166320)

BAR_Rich2 and RhoGAP_nadrin domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-260 1.58e-179

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: 519.60  E-value: 1.58e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  13 NQTVGRAEKTEVLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLG 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  93 KMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGLSSNLQPS 172
Cdd:cd07619    81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 173 GAKADALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIKAQQEAWIEKPS 252
Cdd:cd07619   161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                  ....*...
gi 1621999122 253 FGKPLEEH 260
Cdd:cd07619   241 YGKPLEEH 248
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-449 1.19e-101

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: 315.94  E-value: 1.19e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 249 EKPSFGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 326
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 327 LKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVL 406
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1621999122 407 GPNLLWPQTEGNITEMMATVSLQIVAIIEPLIQHADWFFPGDI 449
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
dnaA super family cl42516
chromosomal replication initiator protein DnaA;
546-639 2.94e-03

chromosomal replication initiator protein DnaA;


The actual alignment was detected with superfamily member PRK14086:

Pssm-ID: 455861 [Multi-domain]  Cd Length: 617  Bit Score: 41.35  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 546 LAATPQSPIPEqsldiSATPSPTPTSFGFPPGAERASTDGVSSSWSDSCYIYPSP-EDDKPPPYPCYSSFHHHHPKTGPC 624
Cdd:PRK14086  172 LGFPPRAPYAS-----PASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPrRDRTDRPEPPPGAGHVHRGGPGPP 246
                          90
                  ....*....|....*..
gi 1621999122 625 ARPEPPLPLYR--WPGY 639
Cdd:PRK14086  247 ERDDAPVVPIRpsAPGP 263
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-260 1.58e-179

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: 519.60  E-value: 1.58e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  13 NQTVGRAEKTEVLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLG 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  93 KMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGLSSNLQPS 172
Cdd:cd07619    81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 173 GAKADALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIKAQQEAWIEKPS 252
Cdd:cd07619   161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                  ....*...
gi 1621999122 253 FGKPLEEH 260
Cdd:cd07619   241 YGKPLEEH 248
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-449 1.19e-101

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: 315.94  E-value: 1.19e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 249 EKPSFGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 326
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 327 LKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVL 406
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1621999122 407 GPNLLWPQTEGNITEMMATVSLQIVAIIEPLIQHADWFFPGDI 449
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-242 4.02e-72

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: 238.00  E-value: 4.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122   1 MKKQFNRMRQLANQTVGRAEKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLME 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  81 GSAILGDDSLLGKMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAeVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSA 160
Cdd:pfam03114  80 AGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 161 KSSGLSSNLQPsgakadALREEMEEAANRVEICRDQLSADMYNFVAKEIDY-ANYFQTLIEVQAEYHRKSLALLQNVLPQ 239
Cdd:pfam03114 159 KKKSSKAKDES------QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQ 232

                  ...
gi 1621999122 240 IKA 242
Cdd:pfam03114 233 LGK 235
BAR smart00721
BAR domain;
1-242 3.50e-63

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 213.79  E-value: 3.50e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122    1 MKKQFNRMRQLANQTVGRAEKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLME 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122   81 GSAI--LGDDSLLGKMLKLCGEAEDKLSQELIHFeLEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQ 158
Cdd:smart00721  81 GDDGegLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  159 SAKSSGlssnlQPSGAKADALREEMEEAANRVEICRDQLSADMYNFVAKEID-YANYFQTLIEVQAEYHRKSLALLQNVL 237
Cdd:smart00721 160 AKKSKE-----KKKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQ 234

                   ....*
gi 1621999122  238 PQIKA 242
Cdd:smart00721 235 QQLDK 239
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
266-441 2.27e-59

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: 200.57  E-value: 2.27e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  266 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSeYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  345 EEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEGNITEMMA 424
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 1621999122  425 TvslQIVAIIEPLIQHA 441
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
270-415 2.58e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.44  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 270 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-VVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWI 348
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621999122 349 QASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQT 415
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
dnaA PRK14086
chromosomal replication initiator protein DnaA;
546-639 2.94e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.35  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 546 LAATPQSPIPEqsldiSATPSPTPTSFGFPPGAERASTDGVSSSWSDSCYIYPSP-EDDKPPPYPCYSSFHHHHPKTGPC 624
Cdd:PRK14086  172 LGFPPRAPYAS-----PASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPrRDRTDRPEPPPGAGHVHRGGPGPP 246
                          90
                  ....*....|....*..
gi 1621999122 625 ARPEPPLPLYR--WPGY 639
Cdd:PRK14086  247 ERDDAPVVPIRpsAPGP 263
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-260 1.58e-179

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: 519.60  E-value: 1.58e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  13 NQTVGRAEKTEVLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLG 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  93 KMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGLSSNLQPS 172
Cdd:cd07619    81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 173 GAKADALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIKAQQEAWIEKPS 252
Cdd:cd07619   161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                  ....*...
gi 1621999122 253 FGKPLEEH 260
Cdd:cd07619   241 YGKPLEEH 248
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
13-260 5.72e-127

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: 384.00  E-value: 5.72e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  13 NQTVGRAEKTEVLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLG 92
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLGEESLIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  93 KMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGlsSNLQPS 172
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSG--TNFQAM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 173 GAKADALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIKAQQEAWIEKPS 252
Cdd:cd07618   159 PSKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPA 238

                  ....*...
gi 1621999122 253 FGKPLEEH 260
Cdd:cd07618   239 FGTPLEEH 246
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
13-260 2.28e-118

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: 361.27  E-value: 2.28e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  13 NQTVGRAEKTEVLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLG 92
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLPEYGLAQSMLESSKELPDDSLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  93 KMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGLSSNlqps 172
Cdd:cd07595    81 KVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSGGQGA---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 173 GAKADALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIKAQQEAWIEKPS 252
Cdd:cd07595   157 AAKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPV 236

                  ....*...
gi 1621999122 253 FGKPLEEH 260
Cdd:cd07595   237 FGQPLEEH 244
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-449 1.19e-101

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: 315.94  E-value: 1.19e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 249 EKPSFGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 326
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 327 LKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVL 406
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1621999122 407 GPNLLWPQTEGNITEMMATVSLQIVAIIEPLIQHADWFFPGDI 449
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-242 4.02e-72

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: 238.00  E-value: 4.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122   1 MKKQFNRMRQLANQTVGRAEKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLME 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  81 GSAILGDDSLLGKMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAeVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSA 160
Cdd:pfam03114  80 AGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 161 KSSGLSSNLQPsgakadALREEMEEAANRVEICRDQLSADMYNFVAKEIDY-ANYFQTLIEVQAEYHRKSLALLQNVLPQ 239
Cdd:pfam03114 159 KKKSSKAKDES------QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQ 232

                  ...
gi 1621999122 240 IKA 242
Cdd:pfam03114 233 LGK 235
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
20-241 1.96e-63

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: 215.19  E-value: 1.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  20 EKTEVLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLGKMLKLCG 99
Cdd:cd07620     8 DATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDAESSIRRVLEMCC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 100 EAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGLSSNLQPSGA----- 174
Cdd:cd07620    88 FMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVGehqgi 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621999122 175 ----KADALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIK 241
Cdd:cd07620   168 rranKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELK 238
BAR smart00721
BAR domain;
1-242 3.50e-63

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 213.79  E-value: 3.50e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122    1 MKKQFNRMRQLANQTVGRAEKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSDKRSKKLPLTSLAQCLME 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122   81 GSAI--LGDDSLLGKMLKLCGEAEDKLSQELIHFeLEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQ 158
Cdd:smart00721  81 GDDGegLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  159 SAKSSGlssnlQPSGAKADALREEMEEAANRVEICRDQLSADMYNFVAKEID-YANYFQTLIEVQAEYHRKSLALLQNVL 237
Cdd:smart00721 160 AKKSKE-----KKKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQ 234

                   ....*
gi 1621999122  238 PQIKA 242
Cdd:smart00721 235 QQLDK 239
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
266-441 2.27e-59

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: 200.57  E-value: 2.27e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  266 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSeYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  345 EEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEGNITEMMA 424
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 1621999122  425 TvslQIVAIIEPLIQHA 441
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
270-415 2.58e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.44  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 270 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-VVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWI 348
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621999122 349 QASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQT 415
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
271-440 5.95e-54

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: 185.20  E-value: 5.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 271 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWIQA 350
Cdd:cd00159     3 IIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 351 SNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEgniTEMMATVSLQI 430
Cdd:cd00159    83 AKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDS---DDELLEDIKKL 159
                         170
                  ....*....|
gi 1621999122 431 VAIIEPLIQH 440
Cdd:cd00159   160 NEIVEFLIEN 169
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-445 1.32e-36

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: 136.70  E-value: 1.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEeHLAVSGRE---IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSaDPHAIAGALK 328
Cdd:cd04404     6 FGVSLQ-FLKEKNPEqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEpVDFDQYE-DVHLPAVILK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 329 SYLRELPEPLMTFELYEEWIQASNIqDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGP 408
Cdd:cd04404    84 TFLRELPEPLLTFDLYDDIVGFLNV-DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1621999122 409 NLLWPQTegnitemmATVSL----QIVAIIEPLIQHADWFF 445
Cdd:cd04404   163 NLLWAKD--------ASMSLsainPINTFTKFLLDHQDEIF 195
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
252-445 1.19e-34

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: 130.98  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 252 SFGKPLEEHLAVSGRE-IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL-----DCCVVDvqEYSADPHAIAG 325
Cdd:cd04395     1 TFGVPLDDCPPSSENPyVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELnrggfDIDLQD--PRWRDVNVVSS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 326 ALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIV 405
Cdd:cd04395    79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1621999122 406 LGPNLLWPqTEGNITEMMATVSLQiVAIIEPLIQHADWFF 445
Cdd:cd04395   159 FGPTLVRT-SDDNMETMVTHMPDQ-CKIVETLIQHYDWFF 196
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-445 4.33e-34

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: 129.45  E-value: 4.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDV-----QEYSADPHAIAGAL 327
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVllispEDYESDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 328 KSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLG 407
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1621999122 408 PNLLwPQTEGNITEMmatvSLQIVAiIEPLIQHADWFF 445
Cdd:cd04398   161 PTLM-NAAPDNAADM----SFQSRV-IETLLDNAYQIF 192
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
271-449 9.33e-34

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: 128.57  E-value: 9.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 271 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYEEWIQ 349
Cdd:cd04402    18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVeVDLKAEPV--LLLASVLKDFLRNIPGSLLSSDLYEEWMS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 350 ASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEGniTEMMATVSlQ 429
Cdd:cd04402    96 ALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPASS--ELQNEDLK-K 172
                         170       180
                  ....*....|....*....|
gi 1621999122 430 IVAIIEPLIQHADWFFPGDI 449
Cdd:cd04402   173 VTSLVQFLIENCQEIFGEDI 192
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
283-438 9.12e-33

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: 125.24  E-value: 9.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 283 GMQEEGLFRVAPSASKLKKLKAALDCCV--VDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRL 360
Cdd:cd04377    30 GLYTEGIYRKSGSANKIKELRQGLDTDPdsVNLEDYPI--HVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERV 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621999122 361 QALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEGNITEMMATVSlQIVAIIEPLI 438
Cdd:cd04377   108 RALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRCPDTADPLQSLQDVS-KTTTCVETLI 184
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
253-445 9.94e-33

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: 125.63  E-value: 9.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEHLAVS---GREIAfPI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGAL 327
Cdd:cd04390     3 FGQRLEDTVAYErkfGPRLV-PIlvEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 328 KSYLRELPEPLMTFELYEEWIQASNI--QDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIV 405
Cdd:cd04390    82 KLYLRELPEPVIPWAQYEDFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATV 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1621999122 406 LGPNLLWPQTEGNITEMMATVSLQIVAIIepLIQHADWFF 445
Cdd:cd04390   162 FGPNILRPKVEDPATIMEGTPQIQQLMTV--MISKHEPLF 199
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
272-440 9.23e-32

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: 122.89  E-value: 9.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL------DCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYE 345
Cdd:cd04374    32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 346 EWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEgNITEMMAT 425
Cdd:cd04374   112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEE-TVAAIMDI 190
                         170
                  ....*....|....*
gi 1621999122 426 VSLQIVaiIEPLIQH 440
Cdd:cd04374   191 KFQNIV--VEILIEN 203
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
267-445 1.63e-31

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: 122.24  E-value: 1.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 267 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDV-QEYSADPHAIAGALKSYLRELPEPLMTFEL 343
Cdd:cd04372    15 QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDrdGEKADIsATVYPDINVITGALKLYFRDLPIPVITYDT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 344 YEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPqTEGNITEMM 423
Cdd:cd04372    95 YPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRP-PEDSALTTL 173
                         170       180
                  ....*....|....*....|..
gi 1621999122 424 ATVSLQIVaIIEPLIQHADWFF 445
Cdd:cd04372   174 NDMRYQIL-IVQLLITNEDVLF 194
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-440 6.94e-30

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: 117.60  E-value: 6.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 251 PSFGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEeGLFRVAPSASKLKKLKAALD---CCVVDVQEYSADPHAIAGAL 327
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDseqIPDLTKDVYIQDIHSVSSLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 328 KSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLG 407
Cdd:cd04384    80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1621999122 408 PNLLW-PQTEGNITEMMAT---VSLQIVaIIEPLIQH 440
Cdd:cd04384   160 PNLLRsKQIESACFSGTAAfmeVRIQSV-VVEFILNH 195
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
272-434 1.40e-29

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: 116.34  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKaaldcCVVDVQEYSA-------DPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:cd04403    20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLR-----FAVDHDEKLDlddskweDIHVITGALKLFFRELPEPLFPYSLF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 345 EEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTE-GNITEMM 423
Cdd:cd04403    95 NDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQEtGNIAVHM 174
                         170
                  ....*....|.
gi 1621999122 424 ATVSlQIVAII 434
Cdd:cd04403   175 VYQN-QIVELI 184
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
253-410 8.77e-29

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


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 113.99  E-value: 8.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEHLAVS-----GREIAFPIEACVTMLLECG-MQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSA--DPHAI 323
Cdd:cd04400     2 FGSPLEEAVELSshkynGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYdVDLFSSSLypDVHTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 324 AGALKSYLRELPEPLMTFELYEEWIQASNIQ-DQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNI 402
Cdd:cd04400    82 AGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNV 161

                  ....*...
gi 1621999122 403 AIVLGPNL 410
Cdd:cd04400   162 CIVFSPTL 169
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-439 3.41e-28

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: 112.16  E-value: 3.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEhLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYSADPHAIAGALKSYL 331
Cdd:cd04373     1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQdHNLDLVSKDFTVNAVAGALKSFF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 332 RELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLL 411
Cdd:cd04373    80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLM 159
                         170       180
                  ....*....|....*....|....*...
gi 1621999122 412 WPQTEgNITEMMATVSLQivAIIEPLIQ 439
Cdd:cd04373   160 RPDFT-SMEALSATRIYQ--TIIETFIQ 184
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
283-439 8.64e-28

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: 111.24  E-value: 8.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 283 GMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQA 362
Cdd:cd04407    30 GLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQA 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621999122 363 LWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLL-WPQTEGNITEMMATvsLQIVAIIEPLIQ 439
Cdd:cd04407   110 IYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLrCPDSSDPLTSMKDV--AKTTTCVEMLIK 185
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
267-440 3.94e-27

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: 109.82  E-value: 3.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 267 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC--CVVDVQEYSadPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:cd04378    15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENgkDLVELSELS--PHDISSVLKLFLRQLPEPLILFRLY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 345 EEWIQ-ASNIQDQDKR-------------LQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNL 410
Cdd:cd04378    93 NDFIAlAKEIQRDTEEdkapntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTL 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1621999122 411 LWP-QTEGNITeMMATVSLQIVA-IIEPLIQH 440
Cdd:cd04378   173 IRPrPGDADVS-LSSLVDYGYQArLVEFLITN 203
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
272-440 1.22e-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: 107.78  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQ----EYSadPHAIAGALKSYLRELPEPLMTFELYEEW 347
Cdd:cd04385    19 VDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQlregEYT--VHDVADVLKRFLRDLPDPLLTSELHAEW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 348 IQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLwpQTEgnitEMMATVS 427
Cdd:cd04385    97 IEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLF--QTD----EHSVGQT 170
                         170
                  ....*....|...
gi 1621999122 428 LQIVAIIEPLIQH 440
Cdd:cd04385   171 SHEVKVIEDLIDN 183
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
272-438 5.22e-26

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


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 106.17  E-value: 5.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEY--SADPHAIAGALKSYLRELPEPLMTFELYEEWIQ 349
Cdd:cd04387    20 VRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMlsEMDVNAIAGTLKLYFRELPEPLFTDELYPNFAE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 350 ASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWP---QTEGNITEMMATV 426
Cdd:cd04387   100 GIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPsekESKIPTNTMTDSW 179
                         170
                  ....*....|..
gi 1621999122 427 SLQIVAIIEPLI 438
Cdd:cd04387   180 SLEVMSQVQVLL 191
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-411 5.99e-26

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


Pssm-ID: 239848  Cd Length: 188  Bit Score: 105.97  E-value: 5.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL---DCCVVDVQEYSaDPHAIAGALKS 329
Cdd:cd04383     3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFergEDPLADDQNDH-DINSVAGVLKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 330 YLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPN 409
Cdd:cd04383    82 YFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPT 161

                  ..
gi 1621999122 410 LL 411
Cdd:cd04383   162 LM 163
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-441 4.05e-25

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: 104.09  E-value: 4.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLE----EHLAVSGREIAFPIEACVTmlLECGMQEEGLFRVAPSASKLKKLKAALD---CCVvdvqeYSADPHAIAG 325
Cdd:cd04394     2 FGVPLHslphSTVPEYGNVPKFLVDACTF--LLDHLSTEGLFRKSGSVVRQKELKAKLEggeACL-----SSALPCDVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 326 ALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIV 405
Cdd:cd04394    75 LLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVI 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1621999122 406 LGPNLLwpQTEGNITEMMATVSLQI---VAIIEPLIQHA 441
Cdd:cd04394   155 FAPNLF--QSEEGGEKMSSSTEKRLrlqAAVVQTLIDNA 191
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
272-449 1.57e-24

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 102.52  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWIQAS 351
Cdd:cd04376    13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFIGTA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 352 NIQDQDkRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEY-----------QDANKMTPSNIAIVLGPNLLWPQ----TE 416
Cdd:cd04376    93 LLEPDE-QLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaadsidedgqeVSGNKMTSLNLATIFGPNLLHKQksgeRE 171
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1621999122 417 GNITEMMATVSLQIVAIIEPLIQHADWFF--PGDI 449
Cdd:cd04376   172 FVQASLRIEESTAIINVVQTMIDNYEELFmvSPEL 206
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-440 5.56e-24

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: 101.04  E-value: 5.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC--VVDVQEYSadPHAIAGALKSY 330
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGkdLVELSELS--PHDISNVLKLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 331 LRELPEPLMTFELYEEWI------QASNIQDQDKRLQA----------------LWNALEKLPKPSYNNLRYLIKFLAHL 388
Cdd:cd04409    79 LRQLPEPLILFRLYNEFIglakesQHVNETQEAKKNSDkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 389 TEYQDANKMTPSNIAIVLGPNLLWP-QTEgnitemmATVSLQIVA-------IIEPLIQH 440
Cdd:cd04409   159 SEQAEENKMSASNLGIIFGPTLIRPrPTD-------ATVSLSSLVdyphqarLVELLITY 211
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-444 6.93e-24

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: 100.52  E-value: 6.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLE---------EHLAVSGREIAFP--IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSAD-P 320
Cdd:cd04397     1 FGVPLEilvekfgadSTLGVGPGKLRIPalIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 321 HAIAGALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFL------AHLTEyQDA 394
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLkwvssfSHIDE-ETG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1621999122 395 NKMTPSNIAIVLGPNLLWPQTEGNiteMMATVSLQIVAIIEPLIQHADWF 444
Cdd:cd04397   160 SKMDIHNLATVITPNILYSKTDNP---NTGDEYFLAIEAVNYLIENNEEF 206
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
37-239 1.65e-23

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: 99.06  E-value: 1.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  37 ELVKQVSHSTHKKLTACLQGQQGSdsdkrskklplTSLAQCLMEGSAILGDDSL--LGKMLKLCGEAEDKLSQELIHFEL 114
Cdd:cd07307     7 KLLKKLIKDTKKLLDSLKELPAAA-----------EKLSEALQELGKELPDLSNtdLGEALEKFGKIQKELEEFRDQLEQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 115 EVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGLSSNLQPsgakadaLREEMEEAANRVEICR 194
Cdd:cd07307    76 KLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLAE-------AEEELQEAKEKYEELR 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1621999122 195 DQLSADMYNFVA-KEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQ 239
Cdd:cd07307   149 EELIEDLNKLEEkRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-410 2.48e-23

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: 98.28  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLeeHLAVS------GREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYsaDPHAIAG 325
Cdd:cd04381     1 FGASL--SLAVErsrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRrESPNLEEY--EPPTVAS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 326 ALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIV 405
Cdd:cd04381    77 LLKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIV 156

                  ....*
gi 1621999122 406 LGPNL 410
Cdd:cd04381   157 LSPTV 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
279-449 3.04e-23

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


Pssm-ID: 239856  Cd Length: 216  Bit Score: 98.96  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 279 LLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWIQASNIQDQ 356
Cdd:cd04391    33 LEERGLETEGILRIPGSAQRVKFLCQELEakFYEGTFLWDQVKQHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 357 DKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEGNIT------EM-MATVSLQ 429
Cdd:cd04391   113 KDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMIMAPNLFPPRGKHSKDneslqeEVnMAAGCAN 192
                         170       180
                  ....*....|....*....|..
gi 1621999122 430 ivaIIEPLIQHAD--WFFPGDI 449
Cdd:cd04391   193 ---IMRLLIRYQDllWTVPSFL 211
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-411 2.17e-22

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: 95.45  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEhLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLR 332
Cdd:cd04406     1 FGVELSR-LTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621999122 333 ELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLL 411
Cdd:cd04406    80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-410 5.89e-22

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: 94.45  E-value: 5.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 251 PSFGKPLEE--HLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALK 328
Cdd:cd04393     1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 329 SYLRELPEPLMTFELYEEWIQASniQD---QDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIV 405
Cdd:cd04393    81 LFLQELPEGLIPASLQIRLMQLY--QDyngEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAV 158

                  ....*
gi 1621999122 406 LGPNL 410
Cdd:cd04393   159 FGPDV 163
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
267-440 1.84e-20

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


Pssm-ID: 239873  Cd Length: 200  Bit Score: 90.26  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 267 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC--CVVDVQEYSadPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:cd04408    15 EVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENgrDLVDLSGHS--PHDITSVLKHFLKELPEPVLPFQLY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 345 EEWIQASNIQDQDKR------------LQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLW 412
Cdd:cd04408    93 DDFIALAKELQRDSEkaaespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLR 172
                         170       180
                  ....*....|....*....|....*...
gi 1621999122 413 PQTEGNITEMMATVSLQIVAIIEPLIQH 440
Cdd:cd04408   173 PLVGGDVSMICLLDTGYQAQLVEFLISN 200
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
275-410 7.81e-20

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


Pssm-ID: 239847  Cd Length: 193  Bit Score: 88.50  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 275 CVTMLLECGMQEEGLFRVAPSASKLKKL-------KAALDCCVVDVqeysadpHAIAGALKSYLRELPEPLMTFELYEEW 347
Cdd:cd04382    24 CVNEIEARGLTEEGLYRVSGSEREVKALkekflrgKTVPNLSKVDI-------HVICGCLKDFLRSLKEPLITFALWKEF 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621999122 348 IQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEyQDANKMTPSNIAIVLGPNL 410
Cdd:cd04382    97 MEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTI 158
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-431 1.65e-19

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


Pssm-ID: 239857  Cd Length: 208  Bit Score: 87.90  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPL-EEHLAVSGREIAFpieacvtmlLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYSADPHAIAGALKSY 330
Cdd:cd04392     1 FGAPLtEEGIAQIYQLIEY---------LEKNLRVEGLFRKPGNSARQQELRDLLNSgTDLDLESGGFHAHDCATVLKGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 331 LRELPEPLMTFELYEEWIQ------------ASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMT 398
Cdd:cd04392    72 LGELPEPLLTHAHYPAHLQiadlcqfdekgnKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMS 151
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1621999122 399 PSNIAIVLGPNLLWP------QTEGNITEMMATVSLQIV 431
Cdd:cd04392   152 ADNLALLFTPHLICPrnltpeDLHENAQKLNSIVTFMIK 190
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-410 1.23e-18

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: 85.55  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 249 EKPSFGKPLEEHLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDVQEYSAdpHAIAGA 326
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIEssTDNVNYDGQQA--YDVADM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 327 LKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVL 406
Cdd:cd04375    79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCL 158

                  ....
gi 1621999122 407 GPNL 410
Cdd:cd04375   159 APSL 162
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
283-411 8.38e-17

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


Pssm-ID: 239854  Cd Length: 187  Bit Score: 79.36  E-value: 8.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 283 GMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSaDPHAIAGALKSYLRELPEPLMTFELYEEWIQASNIQDQDKRLqa 362
Cdd:cd04389    37 GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGLE-DPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKAVEI-- 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1621999122 363 lwnaLEKLPKPSYNNLRYLIKFLAHLT--EYQDANKMTPSNIAIVLGPNLL 411
Cdd:cd04389   114 ----VQKLPIINRLVLCYLINFLQVFAqpENVAHTKMDVSNLAMVFAPNIL 160
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
253-416 1.08e-16

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: 79.82  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEE--HLAVSGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL--DCCVVDVQEYS-ADPHAIAGAL 327
Cdd:cd04379     1 FGVPLSRlvEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFerNSAAVELSEELyPDINVITGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 328 KSYLRELPEPLMTFELYEEWIQASNIQDQDKRLQALWNAL---EKLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAI 404
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLsiiDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                         170
                  ....*....|..
gi 1621999122 405 VLGPNLLWPQTE 416
Cdd:cd04379   161 CFGPVLMFCSQE 172
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
20-236 1.44e-14

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: 73.88  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  20 EKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQ---------GQQGSDSDKR----SKKLPLTS--LAQCLMEGSAI 84
Cdd:cd07592     1 EGTK-LDDEFLEMERKTDATSKLVEDLIPKTKEYLQpnpaaraklAMQNTYSKIRgqakSTKYPQPEglLGEVMLKYGRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  85 LGDDSLLGKMLKLCGEAEDKLSQelIHFELE--VERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqSAKS 162
Cdd:cd07592    80 LGEDSNFGQALVEVGEALKQLAE--VKDSLDdnVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYDYKKRK---QGKG 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621999122 163 SglssnlqpsgakADALREEMEEAANRVEICrdqlSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNV 236
Cdd:cd07592   155 P------------DEELKQAEEKFEESKELA----ENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEEL 212
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-444 6.24e-14

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: 72.06  E-value: 6.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 253 FGKPLEEHLAVSGREIAF-------------PI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-----VVD 312
Cdd:cd04396     2 FGVSLEESLKYASVAISIvdedgeqyvygyiPVvvAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdygkSFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 313 VQEYSAdpHAIAGALKSYLRELPEPLMTFELYEEW-----------------IQASNIQDQDKRLQALWNALEKLPKPSY 375
Cdd:cd04396    82 WDGYTV--HDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkgrINEPLNTDIDQAIKEYRDLITRLPNLNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 376 NNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLW-PQTEGNITEMMATVSlqivaIIEPLIQHADWF 444
Cdd:cd04396   160 QLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILShPDHEMDPKEYKLSRL-----VVEFLIEHQDKF 224
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
25-236 1.99e-11

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: 64.65  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  25 LNEDLLQVEKRLELVKQVSHSTHKKLTACLQ---------GQQGSDSDKRSK----KLPLTS--LAQCLMEGSAILGDDS 89
Cdd:cd07615     5 LDDDFQEMERKIDVTNKVVAELLSKTTEYLQpnpayraklGMLNTVSKIRGQvkttGYPQTEglLGDCMLRYGRELGEES 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  90 LLGKMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqsakssglssnl 169
Cdd:cd07615    85 TFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFDYKKKR-------------- 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621999122 170 qpSGAKADalrEEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNV 236
Cdd:cd07615   151 --QGKIPD---EEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILEDL 212
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
25-241 3.40e-11

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: 63.87  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  25 LNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSDSD----------KRSKKLP-----LTSLAQCLMEGSAILGDDS 89
Cdd:cd07613     5 LDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKlsmintmskiRGQEKGPgypqaEALLAEAMLKFGRELGDEC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  90 LLGKMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqsakssglssnl 169
Cdd:cd07613    85 NFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKR-------------- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621999122 170 qpSGAKADalrEEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNVLPQIK 241
Cdd:cd07613   151 --QGKIPD---EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLE 217
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
279-438 6.40e-11

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: 63.13  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 279 LLECGMQEEGLFR----VAPSASKLKKLKAALDCCVVDVQeySADPHAIAGALKSYLRELPEPLMTFELYEEWIQASNIQ 354
Cdd:cd04380    61 LYTRGLAQEGLFEepglPSEPGELLAEIRDALDTGSPFNS--PGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANN 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 355 DQDKRlQALWNAlekLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLLWPQTEGNITEMMATVSLQIvAII 434
Cdd:cd04380   139 EEDKR-QVIRIS---LPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERDRKR-AFI 213

                  ....
gi 1621999122 435 EPLI 438
Cdd:cd04380   214 EQFL 217
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
10-240 2.85e-10

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: 61.25  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  10 QLANQTVGRAEKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQ----------QGSDSDKRSKKLPLTSLAQCLM 79
Cdd:cd07594     1 QFTEEKLGTAEKTE-YDAHFENLLQRADKTKVWTEKILKQTEAVLQPNpnvrvedfiyEKLDRKKPDRLSNLEQLGQAMI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  80 EGSAILGDDSLLGKMLKLCGEAEDKLSQ---ELIHfelEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRw 156
Cdd:cd07594    80 EAGNDFGPGTAYGSALIKVGQAQKKLGQaerEFIQ---TSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACKTR- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 157 QQSAKSSGLSSnlqpsgaKADA-LREEMEEAANRVEICRdqlsadmynFVAKEI--DYANYFQTL---IEVQAEYHRKSL 230
Cdd:cd07594   156 VKKAKSAEAIE-------QAEQdLRVAQSEFDRQAEITK---------LLLEGIssTHANHLRCLrdfVEAQMTYYAQCY 219
                         250
                  ....*....|
gi 1621999122 231 ALLQNVLPQI 240
Cdd:cd07594   220 QYMDDLQRQL 229
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
74-241 1.40e-09

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: 59.34  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  74 LAQCLMEGSAILGDDSLLGKMLKLCGEAEDKLSQELIHFELEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSR 153
Cdd:cd07614    69 LGETMIRYGKELGDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKK 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 154 TRwqqsakssglssnlqpSGAKADalrEEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALL 233
Cdd:cd07614   149 KR----------------QGKIPD---EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQIL 209

                  ....*...
gi 1621999122 234 QNVLPQIK 241
Cdd:cd07614   210 DELAEKLK 217
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
283-411 4.30e-07

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 51.41  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 283 GMQEEGLFRvAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYEEWIQ-ASNIQDQDKRLQ 361
Cdd:cd04388    30 GLESSTLYR-TQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMISrAQEVQSSDEYAQ 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1621999122 362 ALWNALE--KLPKPSYNNLRYLIKFLAHLTEYQDANKMTPSNIAIVLGPNLL 411
Cdd:cd04388   109 LLRKLIRspNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
317-446 5.74e-07

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: 51.18  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 317 SADPHAIAGALKSYLRELPEPLMTFELYE------EWIQASNIQDQDKRLQALWNALEKLPKPSYNNLRYLIKFLA---H 387
Cdd:cd04399    75 KFEPSTVASVLKLYLLELPDSLIPHDIYDlirslySAYPPSQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYrliE 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621999122 388 LTEYQDANKMTPSNIAIVLGPNLLWPQTEGNITEMMATVSLqivaIIEPLIQHADWFFP 446
Cdd:cd04399   155 ITKMGESEEEYADKLATSLSREILRPIIESLLTIGDKHGYK----FFRDLLTHKDQIFS 209
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
10-224 2.62e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain, which can bind and bend membranes. It interacts with amphiphysin 1 and dynamin 1 through its SH3 domain.


Pssm-ID: 153300  Cd Length: 229  Bit Score: 46.61  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  10 QLANQTVGRAEKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGSD-----SDKRSKKLP--LTS---LAQCLM 79
Cdd:cd07616     1 QFTEEKFGQAEKTE-LDAHLENLLSKAECTKHWTEKIMKQTEVLLQPNPNARieefvYEKLDRKAPsrMNNpelLGQYMI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  80 EGSAILGDDSLLGKMLKLCGEAEDKLS---QELIHfelEVERDVIEPLFVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRW 156
Cdd:cd07616    80 DAGNEFGPGTAYGNALIKCGETQKQIGtadRELIQ---TSAINFLTPLRNFIEGDYKTITKERKLLQNKRLDLDAAKTRL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621999122 157 QQSAKSSGLSSNLQpsgakadALREEMEEAANRVEICR---DQLSAD-------MYNFVAKEIDY-ANYFQTLIEVQAE 224
Cdd:cd07616   157 KKAKVAEARAAAEQ-------ELRITQSEFDRQAEITRlllEGISSThahhlrcLNDFVEAQMTYyAQCYQYMLDLQKQ 228
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
20-236 1.01e-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: 44.65  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  20 EKTEvLNEDLLQVEKRLELVKQVSHSTHKKLTACLQ--GQQGSDSDKRSKKLPLTSLAQCLMEGSAILGDDSLLGKMLKL 97
Cdd:cd07593     1 QKTT-LSEEFLELEKEIELRKEGMERLHRSTEAYVEylSKKKPLLDDKDKCLPVEALGLVMINHGEEFPQDSEYGSCLSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  98 CGEAEDKLSQELIHFELEVER---DVIEPlfvlAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSAKSSGlssnlqpsga 174
Cdd:cd07593    80 LGRAHCKIGTLQEEFADRLSDtflANIER----SLAEMKEYHSARKKLESRRLAYDAALTKSQKAKKEDS---------- 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621999122 175 kadALREEMEEAANRVEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLALLQNV 236
Cdd:cd07593   146 ---RLEEELRRAKAKYEESSEDVEARMVAIKESEADQYRDLTDLLDAELDYHQQSLDVLREV 204
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
37-240 4.17e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153284 [Multi-domain]  Cd Length: 242  Bit Score: 43.11  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  37 ELVKQVSHSTHKKLTACLQGQQGSDSDK------RSKKLPLT---SLAQCLMEGSAILG-----DDSLLGKMLKLCGEAE 102
Cdd:cd07600    37 ESISDFSKTIGSKVSELSKATSPTEAQKvllgtpAPAKLPKTlnhALSRAALASSLELKslepeDEDPLSKALGKYSDAE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 103 DKLSQelihfeLEVERD------VIEPLFVLAEVEIPNIQKQRK--HLAKLVLDMdssrtrwqqsAKSSgLSSNLQPsgA 174
Cdd:cd07600   117 EKIAE------ARLEQDqliqkeFNAKLRETLNTSFQKAHKARKkvEDKRLQLDT----------ARAE-LKSAEPA--E 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621999122 175 KADALREEMEEAanrvEICRDQLSADMYNFVAKEIDYANY---FQTLIEVQAEYHRKSLALLQNVLPQI 240
Cdd:cd07600   178 KQEAARVEVETA----EDEFVSATEEAVELMKEVLDNPEPlqlLKELVKAQLAYHKTAAELLEELLSVL 242
dnaA PRK14086
chromosomal replication initiator protein DnaA;
546-639 2.94e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.35  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 546 LAATPQSPIPEqsldiSATPSPTPTSFGFPPGAERASTDGVSSSWSDSCYIYPSP-EDDKPPPYPCYSSFHHHHPKTGPC 624
Cdd:PRK14086  172 LGFPPRAPYAS-----PASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPrRDRTDRPEPPPGAGHVHRGGPGPP 246
                          90
                  ....*....|....*..
gi 1621999122 625 ARPEPPLPLYR--WPGY 639
Cdd:PRK14086  247 ERDDAPVVPIRpsAPGP 263
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
71-239 4.97e-03

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


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 39.65  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122  71 LTSLAQCLMEGSAILGD-DSLLGKML-KLCGEAEDKLSQELIHFEleverdviEPL--FVLAEVEIPNIQKQRkhlAKLV 146
Cdd:cd07596    48 LIKLAKCEEEVGGELGEaLSKLGKAAeELSSLSEAQANQELVKLL--------EPLkeYLRYCQAVKETLDDR---ADAL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621999122 147 LDMDSSRTRWQQS-AKSSGLSSNLQPSGAKADALREEMEEAANRVEICRDQLSADMYNFVA--------KEIDYANYFQT 217
Cdd:cd07596   117 LTLQSLKKDLASKkAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERLKEelkrfheeRARDLKAALKE 196
                         170       180
                  ....*....|....*....|..
gi 1621999122 218 LIEVQAEYHRKSLALLQNVLPQ 239
Cdd:cd07596   197 FARLQVQYAEKIAEAWESLLPE 218
 
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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