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Conserved domains on  [gi|1207187308|ref|XP_021327135|]
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rho GTPase-activating protein 44 isoform X1 [Danio rerio]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166321)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature

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 ...
13-265 2.57e-178

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: 517.68  E-value: 2.57e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  13 NQTVGRAEKTEVLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLAQCMVEGAAVLGD 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRS-----KKLPLTTLAQCMVEGAAVLGD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  93 DSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSGHPS 172
Cdd:cd07619    76 DSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 173 NVQQGGAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIKAHQEAW 252
Cdd:cd07619   156 NLQPTGAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAW 235
                         250
                  ....*....|...
gi 1207187308 253 IEKPSYGKALEEH 265
Cdd:cd07619   236 VEKPSYGKPLEEH 248
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
254-454 3.10e-96

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


The actual alignment was detected with superfamily member cd04386:

Pssm-ID: 470621  Cd Length: 203  Bit Score: 302.07  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 254 EKPSYGKALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGV--MDVQEYSADPHAIAGA 331
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfsLPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 332 LKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVL 411
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207187308 412 GPNLLWTHSEGNMTEMMTTMSLQIVGIIEPIIQHADWFFPGEI 454
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-265 2.57e-178

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: 517.68  E-value: 2.57e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  13 NQTVGRAEKTEVLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLAQCMVEGAAVLGD 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRS-----KKLPLTTLAQCMVEGAAVLGD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  93 DSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSGHPS 172
Cdd:cd07619    76 DSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 173 NVQQGGAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIKAHQEAW 252
Cdd:cd07619   156 NLQPTGAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAW 235
                         250
                  ....*....|...
gi 1207187308 253 IEKPSYGKALEEH 265
Cdd:cd07619   236 VEKPSYGKPLEEH 248
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
254-454 3.10e-96

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: 302.07  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 254 EKPSYGKALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGV--MDVQEYSADPHAIAGA 331
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfsLPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 332 LKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVL 411
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207187308 412 GPNLLWTHSEGNMTEMMTTMSLQIVGIIEPIIQHADWFFPGEI 454
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-247 6.73e-66

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: 221.44  E-value: 6.73e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308   1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLA 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTV-----LEQPEELLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  81 QCMVEGAAVLGDDSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAeVEIPNIQKQRKHLAKLVLDMDSARTR 160
Cdd:pfam03114  75 ESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 161 WQQSSKSSGHPSNvqqggaKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDY-ANYFQTLIEVQAEYHRKSLEILQ 239
Cdd:pfam03114 154 VKKAKKKKSSKAK------DESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLE 227

                  ....*...
gi 1207187308 240 SVLPQIKA 247
Cdd:pfam03114 228 QLQQQLGK 235
BAR smart00721
BAR domain;
1-247 4.54e-60

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 205.31  E-value: 4.54e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308    1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSVKSPSKKLPlttla 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLG----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308   81 QCMVEGAAV--LGDDSLLGKMLKLCGDTEEKLAQELLVFeLQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSAR 158
Cdd:smart00721  76 EVYEGGDDGegLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSAR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  159 TRWQQSSKSSGHPSNvqqggAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEID-YANYFQTLIEVQAEYHRKSLEI 237
Cdd:smart00721 155 HKLKKAKKSKEKKKD-----EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKL 229
                          250
                   ....*....|
gi 1207187308  238 LQSVLPQIKA 247
Cdd:smart00721 230 LQQLQQQLDK 239
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
271-446 5.92e-57

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: 194.02  E-value: 5.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  271 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCG-VMDVQEYSADPHAIAGALKSYLRELPEPLMTFELY 349
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGpDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  350 DEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSEGNMTEMMT 429
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 1207187308  430 TmslQIVGIIEPIIQHA 446
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
275-420 1.22e-50

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 175.04  E-value: 1.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 275 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCG-VMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWI 353
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207187308 354 QASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHS 420
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-265 2.57e-178

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: 517.68  E-value: 2.57e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  13 NQTVGRAEKTEVLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLAQCMVEGAAVLGD 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRS-----KKLPLTTLAQCMVEGAAVLGD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  93 DSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSGHPS 172
Cdd:cd07619    76 DSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 173 NVQQGGAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIKAHQEAW 252
Cdd:cd07619   156 NLQPTGAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAW 235
                         250
                  ....*....|...
gi 1207187308 253 IEKPSYGKALEEH 265
Cdd:cd07619   236 VEKPSYGKPLEEH 248
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
13-265 1.38e-125

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: 381.30  E-value: 1.38e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  13 NQTVGRAEKTEVLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLAQCMVEGAAVLGD 92
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRH-----KKLPLTALAQNMQEGSAQLGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  93 DSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSghPS 172
Cdd:cd07618    76 ESLIGKMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSS--GT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 173 NVQQGGAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIKAHQEAW 252
Cdd:cd07618   154 NFQAMPSKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKW 233
                         250
                  ....*....|...
gi 1207187308 253 IEKPSYGKALEEH 265
Cdd:cd07618   234 MEKPAFGTPLEEH 246
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
13-265 2.35e-110

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: 341.24  E-value: 2.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  13 NQTVGRAEKTEVLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLAQCMVEGAAVLGD 92
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRL-----KKLPEYGLAQSMLESSKELPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  93 DSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSGHps 172
Cdd:cd07595    76 DSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSGG-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 173 nvQQGGAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIKAHQEAW 252
Cdd:cd07595   154 --QGAAAKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQS 231
                         250
                  ....*....|...
gi 1207187308 253 IEKPSYGKALEEH 265
Cdd:cd07595   232 PSKPVFGQPLEEH 244
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
254-454 3.10e-96

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: 302.07  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 254 EKPSYGKALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGV--MDVQEYSADPHAIAGA 331
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfsLPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 332 LKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVL 411
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207187308 412 GPNLLWTHSEGNMTEMMTTMSLQIVGIIEPIIQHADWFFPGEI 454
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-247 6.73e-66

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: 221.44  E-value: 6.73e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308   1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLA 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTV-----LEQPEELLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  81 QCMVEGAAVLGDDSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAeVEIPNIQKQRKHLAKLVLDMDSARTR 160
Cdd:pfam03114  75 ESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 161 WQQSSKSSGHPSNvqqggaKSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDY-ANYFQTLIEVQAEYHRKSLEILQ 239
Cdd:pfam03114 154 VKKAKKKKSSKAK------DESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLE 227

                  ....*...
gi 1207187308 240 SVLPQIKA 247
Cdd:pfam03114 228 QLQQQLGK 235
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
20-246 3.39e-61

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


Pssm-ID: 153304  Cd Length: 257  Bit Score: 209.03  E-value: 3.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  20 EKTEVLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSvkspsKKLPLTTLAQCMVEGAAVLGDDSLLGKM 99
Cdd:cd07620     8 DATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRM-----KKLPLMALSISMAESFKDFDAESSIRRV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 100 LKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSGHPSNVQQGGA 179
Cdd:cd07620    83 LEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207187308 180 ---------KSDSLREEMEETANRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIK 246
Cdd:cd07620   163 ehqgirranKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELK 238
BAR smart00721
BAR domain;
1-247 4.54e-60

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 205.31  E-value: 4.54e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308    1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSVKSPSKKLPlttla 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLG----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308   81 QCMVEGAAV--LGDDSLLGKMLKLCGDTEEKLAQELLVFeLQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSAR 158
Cdd:smart00721  76 EVYEGGDDGegLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSAR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  159 TRWQQSSKSSGHPSNvqqggAKSDSLREEMEETANRMEICRDQLSADMYNFVAKEID-YANYFQTLIEVQAEYHRKSLEI 237
Cdd:smart00721 155 HKLKKAKKSKEKKKD-----EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKL 229
                          250
                   ....*....|
gi 1207187308  238 LQSVLPQIKA 247
Cdd:smart00721 230 LQQLQQQLDK 239
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
271-446 5.92e-57

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: 194.02  E-value: 5.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  271 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCG-VMDVQEYSADPHAIAGALKSYLRELPEPLMTFELY 349
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGpDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  350 DEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSEGNMTEMMT 429
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 1207187308  430 TmslQIVGIIEPIIQHA 446
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
276-445 4.05e-53

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: 182.89  E-value: 4.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 276 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQA 355
Cdd:cd00159     3 IIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 356 SNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWtHSEGNMTEMMTTMslQI 435
Cdd:cd00159    83 AKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLR-PPDSDDELLEDIK--KL 159
                         170
                  ....*....|
gi 1207187308 436 VGIIEPIIQH 445
Cdd:cd00159   160 NEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
275-420 1.22e-50

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 175.04  E-value: 1.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 275 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCG-VMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWI 353
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207187308 354 QASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHS 420
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
277-450 6.91e-36

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: 134.84  E-value: 6.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQeySADP-----HAIAGALKSYLRELPEPLMTFELYDE 351
Cdd:cd04395    22 VEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDID--LQDPrwrdvNVVSSLLKSFFRKLPEPLFTNELYPD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 352 WIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWThSEGNMTEMMTTM 431
Cdd:cd04395   100 FIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRT-SDDNMETMVTHM 178
                         170
                  ....*....|....*....
gi 1207187308 432 SLQiVGIIEPIIQHADWFF 450
Cdd:cd04395   179 PDQ-CKIVETLIQHYDWFF 196
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
280-450 7.00e-34

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: 128.99  E-value: 7.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 280 CVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGV-MDVQEYSaDPHAIAGALKSYLRELPEPLMTFELYDEWIQASNI 358
Cdd:cd04404    30 TVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEpVDFDQYE-DVHLPAVILKTFLRELPEPLLTFDLYDDIVGFLNV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 359 QDmDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSegnmtemmTTMSL-QIVG 437
Cdd:cd04404   109 DK-EERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPNLLWAKD--------ASMSLsAINP 179
                         170
                  ....*....|....*.
gi 1207187308 438 I---IEPIIQHADWFF 450
Cdd:cd04404   180 IntfTKFLLDHQDEIF 195
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
288-416 4.32e-30

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: 117.92  E-value: 4.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 288 GMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQA 367
Cdd:cd04377    30 GLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERVRA 109
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207187308 368 LLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04377   110 LYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCIL 158
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
258-449 1.56e-29

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: 116.77  E-value: 1.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 258 YGKALEEHLAIS---GREIAfPI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGAL 332
Cdd:cd04390     3 FGQRLEDTVAYErkfGPRLV-PIlvEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 333 KSYLRELPEPLMTFELYDEWIQASNIQDMD--KRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIV 410
Cdd:cd04390    82 KLYLRELPEPVIPWAQYEDFLSCAQLLSKDeeKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATV 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1207187308 411 LGPNLLWTHSEGNMTEMMTTMSLQIVGIIEpIIQHADWF 449
Cdd:cd04390   162 FGPNILRPKVEDPATIMEGTPQIQQLMTVM-ISKHEPLF 199
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
276-437 7.75e-29

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: 114.32  E-value: 7.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 276 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGV-MDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEWIQ 354
Cdd:cd04402    18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVeVDLKAEPV--LLLASVLKDFLRNIPGSLLSSDLYEEWMS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 355 ASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLW--THSEGNM-------- 424
Cdd:cd04402    96 ALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWppASSELQNedlkkvts 175
                         170
                  ....*....|....
gi 1207187308 425 -TEMMTTMSLQIVG 437
Cdd:cd04402   176 lVQFLIENCQEIFG 189
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
258-450 7.65e-28

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: 111.34  E-value: 7.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 258 YGKALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDV-----QEYSADPHAIAGAL 332
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVllispEDYESDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 333 KSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLG 412
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207187308 413 PNLLWTHSEgNMTEmmttMSLQIVgIIEPIIQHADWFF 450
Cdd:cd04398   161 PTLMNAAPD-NAAD----MSFQSR-VIETLLDNAYQIF 192
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
272-450 8.46e-28

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: 111.45  E-value: 8.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 272 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLD----CGVMDVQEYSaDPHAIAGALKSYLRELPEPLMTFE 347
Cdd:cd04372    15 QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDrdgeKADISATVYP-DINVITGALKLYFRDLPIPVITYD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 348 LYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWThSEGNMTEM 427
Cdd:cd04372    94 TYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRP-PEDSALTT 172
                         170       180
                  ....*....|....*....|...
gi 1207187308 428 MTTMSLQIVgIIEPIIQHADWFF 450
Cdd:cd04372   173 LNDMRYQIL-IVQLLITNEDVLF 194
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
258-415 3.33e-27

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: 109.76  E-value: 3.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 258 YGKALEEHLAIS-----GREIAFPIEACVTMLLECG-MQEEGLFRVAPSASKLKKLKASLDCGV-MDVQEYSA--DPHAI 328
Cdd:cd04400     2 FGSPLEEAVELSshkynGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYdVDLFSSSLypDVHTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 329 AGALKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCT-CEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNI 407
Cdd:cd04400    82 AGLLKLYLRELPTLILGGELHNDFKRLVEENHDRSQRALELKDlVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNV 161

                  ....*...
gi 1207187308 408 AIVLGPNL 415
Cdd:cd04400   162 CIVFSPTL 169
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
288-416 8.84e-27

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: 108.16  E-value: 8.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 288 GMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQA 367
Cdd:cd04407    30 GLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQA 109
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207187308 368 LLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04407   110 IYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLL 158
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
277-445 1.43e-26

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 108.25  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKASL------DCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYD 350
Cdd:cd04374    32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 351 EWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSEgNMTEMMTT 430
Cdd:cd04374   112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEE-TVAAIMDI 190
                         170
                  ....*....|....*
gi 1207187308 431 MSLQIVgiIEPIIQH 445
Cdd:cd04374   191 KFQNIV--VEILIEN 203
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
275-446 5.99e-26

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: 106.40  E-value: 5.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 275 FPIEACVTmlLECGMQEEGLFRVAPSASKLKKLKASLDCGvMDVQEySADPHAIAGALKSYLRELPEPLMTFELYDEWIQ 354
Cdd:cd04394    23 FLVDACTF--LLDHLSTEGLFRKSGSVVRQKELKAKLEGG-EACLS-SALPCDVAGLLKQFFRELPEPLLPYDLHEALLK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 355 ASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSEGNMTEMMTTMSLQ 434
Cdd:cd04394    99 AQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNLFQSEEGGEKMSSSTEKRLR 178
                         170
                  ....*....|...
gi 1207187308 435 I-VGIIEPIIQHA 446
Cdd:cd04394   179 LqAAVVQTLIDNA 191
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
272-416 1.10e-25

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: 105.58  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 272 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGvMDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELYD 350
Cdd:cd04378    15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENG-KDLVELSeLSPHDISSVLKLFLRQLPEPLILFRLYN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 351 EWIQ-ASNIQDMDK----------------RLQALLCtceKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGP 413
Cdd:cd04378    94 DFIAlAKEIQRDTEedkapntpievnriirKLKDLLR---QLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGP 170

                  ...
gi 1207187308 414 NLL 416
Cdd:cd04378   171 TLI 173
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
284-451 4.39e-25

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: 104.35  E-value: 4.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 284 LLECGMQEEGLFRVAPSASKLKKLKASLD--CGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQDM 361
Cdd:cd04391    33 LEERGLETEGILRIPGSAQRVKFLCQELEakFYEGTFLWDQVKQHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 362 DKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSEGNMT------EMmtTMSLQI 435
Cdd:cd04391   113 KDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMIMAPNLFPPRGKHSKDneslqeEV--NMAAGC 190
                         170
                  ....*....|....*...
gi 1207187308 436 VGIIEPIIQHAD--WFFP 451
Cdd:cd04391   191 ANIMRLLIRYQDllWTVP 208
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
277-439 7.09e-25

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: 102.85  E-value: 7.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKL--KASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQ 354
Cdd:cd04403    20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLrfAVDHDEKLDLDDSKWEDIHVITGALKLFFRELPEPLFPYSLFNDFVA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 355 ASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSE-GNMTeMMTTMSL 433
Cdd:cd04403   100 AIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQEtGNIA-VHMVYQN 178

                  ....*.
gi 1207187308 434 QIVGII 439
Cdd:cd04403   179 QIVELI 184
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
277-416 1.09e-24

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


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 102.70  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEY--SADPHAIAGALKSYLRELPEPLMTFELYDEWIQ 354
Cdd:cd04387    20 VRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMlsEMDVNAIAGTLKLYFRELPEPLFTDELYPNFAE 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207187308 355 ASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04387   100 GIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLL 161
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
269-444 4.01e-24

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: 100.61  E-value: 4.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 269 SGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDC-GVMDVQEYSADPHAIAGALKSYLRELPEPLMTFE 347
Cdd:cd04373    11 SEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQdHNLDLVSKDFTVNAVAGALKSFFSELPDPLIPYS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 348 LYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHSEgNMTEM 427
Cdd:cd04373    91 MHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMRPDFT-SMEAL 169
                         170
                  ....*....|....*..
gi 1207187308 428 MTTMSLQIvgIIEPIIQ 444
Cdd:cd04373   170 SATRIYQT--IIETFIQ 184
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
277-445 4.09e-24

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: 100.46  E-value: 4.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQ----EYSadPHAIAGALKSYLRELPEPLMTFELYDEW 352
Cdd:cd04385    19 VDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQlregEYT--VHDVADVLKRFLRDLPDPLLTSELHAEW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 353 IQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWThsegnmTEMMTTMS 432
Cdd:cd04385    97 IEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQT------DEHSVGQT 170
                         170
                  ....*....|...
gi 1207187308 433 LQIVGIIEPIIQH 445
Cdd:cd04385   171 SHEVKVIEDLIDN 183
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
277-454 6.40e-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: 100.59  E-value: 6.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQAS 356
Cdd:cd04376    13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFIGTA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 357 NIQdMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEY-QDS----------NKMTPGNIAIVLGPNLL----WTHSE 421
Cdd:cd04376    93 LLE-PDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaADSidedgqevsgNKMTSLNLATIFGPNLLhkqkSGERE 171
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207187308 422 GNMTEMMTTMSLQIVGIIEPIIQHADWFF--PGEI 454
Cdd:cd04376   172 FVQASLRIEESTAIINVVQTMIDNYEELFmvSPEL 206
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
256-416 3.17e-23

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: 98.34  E-value: 3.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 256 PSYGKALEEHLAISGREIAFPIEACVTMLLECGMQEeGLFRVAPSASKLKKLKASLDCG-VMDVQE--YSADPHAIAGAL 332
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEqIPDLTKdvYIQDIHSVSSLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 333 KSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLG 412
Cdd:cd04384    80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159

                  ....
gi 1207187308 413 PNLL 416
Cdd:cd04384   160 PNLL 163
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
258-416 3.56e-23

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: 97.88  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 258 YGKALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCG---VMDVQEYSaDPHAIAGALKS 334
Cdd:cd04383     3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGedpLADDQNDH-DINSVAGVLKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 335 YLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPN 414
Cdd:cd04383    82 YFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPT 161

                  ..
gi 1207187308 415 LL 416
Cdd:cd04383   162 LM 163
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
77-244 7.87e-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: 97.13  E-value: 7.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  77 TTLAQCMVEGAAVLGDDSL--LGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDM 154
Cdd:cd07307    31 EKLSEALQELGKELPDLSNtdLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 155 DSARTRWQQSSKSSGHPSNVQQggaksdsLREEMEETANRMEICRDQLSADMYNFVA-KEIDYANYFQTLIEVQAEYHRK 233
Cdd:cd07307   111 DAAREKLKKLRKKKKDSSKLAE-------AEEELQEAKEKYEELREELIEDLNKLEEkRKELFLSLLLSFIEAQSEFFKE 183
                         170
                  ....*....|.
gi 1207187308 234 SLEILQSVLPQ 244
Cdd:cd07307   184 VLKILEQLLPY 194
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
273-416 2.32e-21

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: 93.33  E-value: 2.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 273 IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGvMDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELYDE 351
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENG-KDLVELSeLSPHDISNVLKLYLRQLPEPLILFRLYNE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 352 WIQ-ASNIQDMDKRLQAL---------LCT------------CEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAI 409
Cdd:cd04409    95 FIGlAKESQHVNETQEAKknsdkkwpnMCTelnrillkskdlLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGI 174

                  ....*..
gi 1207187308 410 VLGPNLL 416
Cdd:cd04409   175 IFGPTLI 181
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
256-415 4.20e-21

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


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 92.14  E-value: 4.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 256 PSYGKALEE--HLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALK 333
Cdd:cd04393     1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 334 SYLRELPEPLMTFELYDEWIQAS---NIQDMD-KRLQALLctcEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAI 409
Cdd:cd04393    81 LFLQELPEGLIPASLQIRLMQLYqdyNGEDEFgRKLRDLL---QQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAA 157

                  ....*.
gi 1207187308 410 VLGPNL 415
Cdd:cd04393   158 VFGPDV 163
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
271-416 9.74e-21

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: 90.83  E-value: 9.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 271 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYD 350
Cdd:cd04406    13 RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207187308 351 EWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04406    93 EFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
272-416 6.04e-20

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


Pssm-ID: 239873  Cd Length: 200  Bit Score: 89.11  E-value: 6.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 272 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDE 351
Cdd:cd04408    15 EVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLYDD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 352 WI---------------QASNIQDMDKRLQALLCtceKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04408    95 FIalakelqrdsekaaeSPSIVENIIRSLKELLG---RLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLL 171
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
277-426 1.43e-19

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 88.19  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 277 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSAD-PHAIAGALKSYLRELPEPLMTFELYDEWIQA 355
Cdd:cd04397    31 IDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnPVQLAALLKKFLRELPDPLLTFKLYRLWISS 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207187308 356 SNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEY-----QDSNKMTPGNIAIVLGPNLLWT-HSEGNMTE 426
Cdd:cd04397   111 QKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFshideETGSKMDIHNLATVITPNILYSkTDNPNTGD 187
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
261-419 1.87e-19

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


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 87.11  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 261 ALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLDC-GVMDVQEYsaDPHAIAGALKSYLREL 339
Cdd:cd04381     8 AVERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRrESPNLEEY--EPPTVASLLKQYLREL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 340 PEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTH 419
Cdd:cd04381    86 PEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPTVQISN 165
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
280-415 1.59e-18

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


Pssm-ID: 239847  Cd Length: 193  Bit Score: 84.65  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 280 CVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQ 359
Cdd:cd04382    24 CVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKEFMEAAEIL 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207187308 360 DMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDsNKMTPGNIAIVLGPNL 415
Cdd:cd04382   104 DEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTI 158
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
285-450 8.66e-17

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: 80.20  E-value: 8.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 285 LECGMQEEGLFRVAPSASKLKKLKASLDCGV-MDVQEYSADPHAIAGALKSYLRELPEPLMTFELY------------DE 351
Cdd:cd04392    20 LEKNLRVEGLFRKPGNSARQQELRDLLNSGTdLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYpahlqiadlcqfDE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 352 WIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLWTHsegNMT-EMMTT 430
Cdd:cd04392   100 KGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPR---NLTpEDLHE 176
                         170       180
                  ....*....|....*....|
gi 1207187308 431 MSLQIVGIIEPIIQHADWFF 450
Cdd:cd04392   177 NAQKLNSIVTFMIKHSQKLF 196
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
20-241 9.92e-17

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: 80.43  E-value: 9.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  20 EKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQ---------GQQGTeIEKRSVKSPSKKLPLTT--LAQCMVEGAA 88
Cdd:cd07592     1 EGTK-LDDEFLEMERKTDATSKLVEDLIPKTKEYLQpnpaaraklAMQNT-YSKIRGQAKSTKYPQPEglLGEVMLKYGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  89 VLGDDSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRwqqsskss 168
Cdd:cd07592    79 ELGEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYDYKKRK-------- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207187308 169 ghpsnvqQGGAKSDSLREEMEETANRMEICrdqlSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSV 241
Cdd:cd07592   151 -------QGKGPDEELKQAEEKFEESKELA----ENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEEL 212
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
288-421 1.95e-16

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


Pssm-ID: 239854  Cd Length: 187  Bit Score: 78.59  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 288 GMQEEGLFRVAPSASKLKKLKASLDCGVMDVQEYSaDPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLqa 367
Cdd:cd04389    37 GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGLE-DPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKAVEI-- 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207187308 368 llctCEKLPADNLNNFRYLIKFLSKLT--EYQDSNKMTPGNIAIVLGPNLLWTHSE 421
Cdd:cd04389   114 ----VQKLPIINRLVLCYLINFLQVFAqpENVAHTKMDVSNLAMVFAPNILRCTSD 165
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
254-415 2.66e-16

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: 79.00  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 254 EKPSYGKALEEHLAISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLK----ASLDCGVMDVQEysadPHAIA 329
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRsmieSSTDNVNYDGQQ----AYDVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 330 GALKSYLRELPEPLMTFELYDEWIQASNIQDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAI 409
Cdd:cd04375    77 DMLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAV 156

                  ....*.
gi 1207187308 410 VLGPNL 415
Cdd:cd04375   157 CLAPSL 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
269-416 4.81e-15

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: 74.81  E-value: 4.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 269 SGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKASLD---CGVMDVQEYSADPHAIAGALKSYLRELPEPLMT 345
Cdd:cd04379    14 ESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFErnsAAVELSEELYPDINVITGVLKDYLRELPEPLIT 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207187308 346 FELYDEWIQASNI---QDMDKRLQALLCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04379    94 PQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAVCFGPVLM 167
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
25-246 9.18e-15

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: 74.75  E-value: 9.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  25 LSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIE----------KRSVKSPSKKLPLTTLAQCMVEGAAVLGDDS 94
Cdd:cd07614     5 LDDDFKEMEKKVDLTSKAVTEVLARTIEYLQPNPASRAKltmlntvskiRGQVKNPGYPQSEGLLGETMIRYGKELGDES 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  95 LLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRwqqsskssghpsnv 174
Cdd:cd07614    85 NFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKKKR-------------- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207187308 175 qQGGAKSDSLREEMEETANRMEICRdqlsADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIK 246
Cdd:cd07614   151 -QGKIPDEELRQAMEKFEESKEVAE----TSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLK 217
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
25-246 1.34e-14

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: 74.27  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  25 LSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSVKSPSK-----KLP-----LTTLAQCMVEGAAVLGDDS 94
Cdd:cd07613     5 LDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKirgqeKGPgypqaEALLAEAMLKFGRELGDEC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  95 LLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRwqqsskssghpsnv 174
Cdd:cd07613    85 NFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKR-------------- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207187308 175 qQGGAKSDSLREEMEETANRMEICRdqlsADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSVLPQIK 246
Cdd:cd07613   151 -QGKIPDEELRQALEKFDESKEIAE----SSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLE 217
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
10-245 1.41e-14

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: 73.97  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  10 QLANQTVGRAEKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSVKSPSKKLP-----LTTLAQCMV 84
Cdd:cd07594     1 QFTEEKLGTAEKTE-YDAHFENLLQRADKTKVWTEKILKQTEAVLQPNPNVRVEDFIYEKLDRKKPdrlsnLEQLGQAMI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  85 EGAAVLGDDSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRwQQS 164
Cdd:cd07594    80 EAGNDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACKTR-VKK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 165 SKSsghPSNVQQggAKSDsLREEMEETANRMEICRdqlsadmynFVAKEI--DYANYFQTL---IEVQAEYHRKSLEILQ 239
Cdd:cd07594   159 AKS---AEAIEQ--AEQD-LRVAQSEFDRQAEITK---------LLLEGIssTHANHLRCLrdfVEAQMTYYAQCYQYMD 223

                  ....*.
gi 1207187308 240 SVLPQI 245
Cdd:cd07594   224 DLQRQL 229
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
280-449 2.28e-12

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: 67.44  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 280 CVTMLLECGMQEEGLFRVAPSASKLKKLKASLDCG-----VMDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEW-- 352
Cdd:cd04396    39 CGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdygkSFDWDGYTV--HDAASVLRRYLNNLPEPLVPLDLYEEFrn 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 353 ---IQASNIQDMDKRLQALLCT------------CEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLLw 417
Cdd:cd04396   117 plrKRPRILQYMKGRINEPLNTdidqaikeyrdlITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGIL- 195
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207187308 418 THSEGNMTEMMTTMSLQivgIIEPIIQHADWF 449
Cdd:cd04396   196 SHPDHEMDPKEYKLSRL---VVEFLIEHQDKF 224
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
25-241 2.47e-12

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: 67.35  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  25 LSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIEKRSVKSPSK--------KLPLTT--LAQCMVEGAAVLGDDS 94
Cdd:cd07615     5 LDDDFQEMERKIDVTNKVVAELLSKTTEYLQPNPAYRAKLGMLNTVSKirgqvkttGYPQTEglLGDCMLRYGRELGEES 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  95 LLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRwqqsskssghpsnv 174
Cdd:cd07615    85 TFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFDYKKKR-------------- 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207187308 175 qQGGAKSDSLREEMEetanRMEICRDQLSADMYNFVAKEIDYANYFQTLIEVQAEYHRKSLEILQSV 241
Cdd:cd07615   151 -QGKIPDEEIRQAVE----KFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILEDL 212
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
284-416 1.68e-09

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: 58.89  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 284 LLECGMQEEGLFR----VAPSASKLKKLKASLDCGVMDVQeySADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQ 359
Cdd:cd04380    61 LYTRGLAQEGLFEepglPSEPGELLAEIRDALDTGSPFNS--PGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANN 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207187308 360 DMDKRlQALLctcEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04380   139 EEDKR-QVIR---ISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLL 191
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
10-229 2.88e-09

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: 58.55  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  10 QLANQTVGRAEKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQGQQGTEIE-----KRSVKSPSKKLPLTTLAQCMV 84
Cdd:cd07616     1 QFTEEKFGQAEKTE-LDAHLENLLSKAECTKHWTEKIMKQTEVLLQPNPNARIEefvyeKLDRKAPSRMNNPELLGQYMI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  85 EGAAVLGDDSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQS 164
Cdd:cd07616    80 DAGNEFGPGTAYGNALIKCGETQKQIGTADRELIQTSAINFLTPLRNFIEGDYKTITKERKLLQNKRLDLDAAKTRLKKA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207187308 165 SKSSGHPSNVQQggaksdsLREEMEETANRMEICR---DQLSAD-------MYNFVAKEIDY-ANYFQTLIEVQAE 229
Cdd:cd07616   160 KVAEARAAAEQE-------LRITQSEFDRQAEITRlllEGISSThahhlrcLNDFVEAQMTYyAQCYQYMLDLQKQ 228
BAR_Endophilin_B2 cd07617
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid ...
10-164 1.28e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; 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. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes.


Pssm-ID: 153301  Cd Length: 220  Bit Score: 53.49  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  10 QLANQTVGRAEKTEVLS--EDLLqveKRLDLVKQVSHSTHKKLTACLQGQQGTEIE-----KRSVKSPSKKLPLTTLAQC 82
Cdd:cd07617     1 QFTEEKLGQAEKTELDAhfENLL---ARADSTKNWTEKILRQTEVLLQPNPSARVEeflyeKLDRKVPSRVTNAELLGQY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  83 MVEGAAVLGDDSLLGKMLKLCGDTEEKLAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQ 162
Cdd:cd07617    78 MTEAANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLK 157

                  ..
gi 1207187308 163 QS 164
Cdd:cd07617   158 KA 159
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
39-245 2.30e-07

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: 53.13  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  39 VKQVSHSTHKKLTACLQGQQGTEIEKRSV-KSPSKKLPLT---TLAQCMVEGAAVLG-----DDSLLGKMLKLCGDTEEK 109
Cdd:cd07600    39 ISDFSKTIGSKVSELSKATSPTEAQKVLLgTPAPAKLPKTlnhALSRAALASSLELKslepeDEDPLSKALGKYSDAEEK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 110 LAQELLVFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSsghpsnvqqggAKSDSLREEME 189
Cdd:cd07600   119 IAEARLEQDQLIQKEFNAKLRETLNTSFQKAHKARKKVEDKRLQLDTARAELKSAEPA-----------EKQEAARVEVE 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207187308 190 etanRMEICRDQLSADMYNFVAKEIDYANY---FQTLIEVQAEYHRKSLEILQSVLPQI 245
Cdd:cd07600   188 ----TAEDEFVSATEEAVELMKEVLDNPEPlqlLKELVKAQLAYHKTAAELLEELLSVL 242
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
288-416 2.67e-07

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 52.18  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 288 GMQEEGLFRvAPSASKLKKLKASLDCGVMDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQ-ASNIQDMDKRLQ 366
Cdd:cd04388    30 GLESSTLYR-TQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMISrAQEVQSSDEYAQ 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207187308 367 AL--LCTCEKLPADNLNNFRYLIKFLSKLTEYQDSNKMTPGNIAIVLGPNLL 416
Cdd:cd04388   109 LLrkLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
20-241 2.91e-07

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: 52.35  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  20 EKTEvLSEDLLQVEKRLDLVKQVSHSTHKKLTACLQgqqgtEIEKR--SVKSPSKKLPLTTLAQCMVEGAAVLGDDSLLG 97
Cdd:cd07593     1 QKTT-LSEEFLELEKEIELRKEGMERLHRSTEAYVE-----YLSKKkpLLDDKDKCLPVEALGLVMINHGEEFPQDSEYG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  98 KMLKLCGDTEEKLA--QELLVFELQ------IERdvveplyvlAEVEIPNIQKQRKHLAKLVLDMDSARTRWQQSSKSSG 169
Cdd:cd07593    75 SCLSKLGRAHCKIGtlQEEFADRLSdtflanIER---------SLAEMKEYHSARKKLESRRLAYDAALTKSQKAKKEDS 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207187308 170 H-PSNVQQGGAKSDslrEEMEETANRMEICRDqLSADmynfvakeiDYANYFQtLIEVQAEYHRKSLEILQSV 241
Cdd:cd07593   146 RlEEELRRAKAKYE---ESSEDVEARMVAIKE-SEAD---------QYRDLTD-LLDAELDYHQQSLDVLREV 204
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
79-244 6.38e-05

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


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 45.42  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308  79 LAQCMVEGAAVLGD-DSLLGKML-KLCGDTEEKLAQELLVFElqierdvvEPL--YVLAEVEIPNIQKQRK----HLAKL 150
Cdd:cd07596    51 LAKCEEEVGGELGEaLSKLGKAAeELSSLSEAQANQELVKLL--------EPLkeYLRYCQAVKETLDDRAdallTLQSL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 151 VLDMDSARTrwqQSSKSSGHPSNVQqggAKSDSLREEMEETANRMEICRDQLSADMYNFVA--------KEIDYANYFQT 222
Cdd:cd07596   123 KKDLASKKA---QLEKLKAAPGIKP---AKVEELEEELEEAESALEEARKRYEEISERLKEelkrfheeRARDLKAALKE 196
                         170       180
                  ....*....|....*....|..
gi 1207187308 223 LIEVQAEYHRKSLEILQSVLPQ 244
Cdd:cd07596   197 FARLQVQYAEKIAEAWESLLPE 218
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
322-391 8.99e-03

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 38.85  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207187308 322 SADPHAIAGALKSYLRELPEPLMTFELYD------EWIQASNIQDMDKRLQALLCTCEKLPADNL-------NNFRYLIK 388
Cdd:cd04399    75 KFEPSTVASVLKLYLLELPDSLIPHDIYDlirslySAYPPSQEDSDTARIQGLQSTLSQLPKSHIatldaiiTHFYRLIE 154

                  ...
gi 1207187308 389 FLS 391
Cdd:cd04399   155 ITK 157
 
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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