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Conserved domains on  [gi|2024357528|ref|XP_015149957|]
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rho GTPase-activating protein 17 isoform X2 [Gallus gallus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10166313)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
13-258 0e+00

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


:

Pssm-ID: 153302  Cd Length: 246  Bit Score: 528.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQEGSAQLSDETLLG 92
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLGEESLIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  93 KMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKTSGTNFQMHPS 172
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 173 KIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQAHQDKWTEKPAFG 252
Cdd:cd07618   161 KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAFG 240

                  ....*.
gi 2024357528 253 TPLEEH 258
Cdd:cd07618   241 TPLEEH 246
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
247-446 5.97e-128

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: 381.80  E-value: 5.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 247 EKPAFGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQ--LDEFYSDPHAVAGA 324
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 325 LKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024357528 405 GPNLLWAKTEGSLAEMAAATSVHVVAIIEPIIQHADWFFPGD 446
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGE 202
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
563-790 1.90e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 563 SAGTAEQLQSQGNEDVSTSKPKD------STSSATPPPMRNGGHVSTAPNQSASSTNQLSVNQPQNAAGPSPhsmrravk 636
Cdd:pfam03154 114 SEGEGESSDGRSVNDEGSSDPKDidqdnrSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS-------- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 637 kpapappkpaNPPPGQPGSQSSAPAAQPPSISPKPLARSSSPPAQHANQGAAMT--SSSQVSAPRRYSSSLSPIQAPSHP 714
Cdd:pfam03154 186 ----------PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQRLPSPHPPLQPMTQP 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 715 PPQPPTQATPPLQPKANNQASPSAPSSEHGPE--------QPCYTPPQTPT-------PPDTPPLGKHSTTSPPSQPQSS 779
Cdd:pfam03154 256 PPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSQsqvppgpSPAAPGQSQQRIHTPPSQSQLQ 335
                         250
                  ....*....|.
gi 2024357528 780 TQDTSQSHSPP 790
Cdd:pfam03154 336 SQQPPREQPLP 346
 
Name Accession Description Interval E-value
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
13-258 0e+00

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


Pssm-ID: 153302  Cd Length: 246  Bit Score: 528.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQEGSAQLSDETLLG 92
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLGEESLIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  93 KMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKTSGTNFQMHPS 172
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 173 KIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQAHQDKWTEKPAFG 252
Cdd:cd07618   161 KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAFG 240

                  ....*.
gi 2024357528 253 TPLEEH 258
Cdd:cd07618   241 TPLEEH 246
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
247-446 5.97e-128

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: 381.80  E-value: 5.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 247 EKPAFGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQ--LDEFYSDPHAVAGA 324
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 325 LKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024357528 405 GPNLLWAKTEGSLAEMAAATSVHVVAIIEPIIQHADWFFPGD 446
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGE 202
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-240 7.58e-62

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: 208.73  E-value: 7.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528   1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQE 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  81 GSAQLSDETLLGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTeVEIPNIQKQRKQLAKLVLDWDSARGRYNQAH 160
Cdd:pfam03114  80 AGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 161 KTSGTNfqmhPSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEY-AKFFVMLLEAQADYHRKALAVIEKVLPEIQ 239
Cdd:pfam03114 159 KKKSSK----AKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQLG 234

                  .
gi 2024357528 240 A 240
Cdd:pfam03114 235 K 235
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
264-439 1.03e-58

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: 197.87  E-value: 1.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  264 REIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTS-QLDEFYSDPHAVAGALKSYLRELPEPLMTYALY 342
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  343 EEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKTEGSLAEMAa 422
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD- 159
                          170
                   ....*....|....*..
gi 2024357528  423 atSVHVVAIIEPIIQHA 439
Cdd:smart00324 160 --IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
268-413 6.67e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 188.91  E-value: 6.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 268 IPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALD-CSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALYEEWT 346
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDrGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024357528 347 QAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKT 413
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
BAR smart00721
BAR domain;
1-240 3.49e-53

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 184.90  E-value: 3.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528    1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQE 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528   81 GSA--QLSDETLLGKMLDTCGDAENKLALELSQHeVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQ 158
Cdd:smart00721  81 GDDgeGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  159 AHKTSGTNFQmhpSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKE-GEYAKFFVMLLEAQADYHRKALAVIEKVLPE 237
Cdd:smart00721 160 AKKSKEKKKD---EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRvDFFVNCLQALIEAQLNFHRESYKLLQQLQQQ 236

                   ...
gi 2024357528  238 IQA 240
Cdd:smart00721 237 LDK 239
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
563-790 1.90e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 563 SAGTAEQLQSQGNEDVSTSKPKD------STSSATPPPMRNGGHVSTAPNQSASSTNQLSVNQPQNAAGPSPhsmrravk 636
Cdd:pfam03154 114 SEGEGESSDGRSVNDEGSSDPKDidqdnrSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS-------- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 637 kpapappkpaNPPPGQPGSQSSAPAAQPPSISPKPLARSSSPPAQHANQGAAMT--SSSQVSAPRRYSSSLSPIQAPSHP 714
Cdd:pfam03154 186 ----------PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQRLPSPHPPLQPMTQP 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 715 PPQPPTQATPPLQPKANNQASPSAPSSEHGPE--------QPCYTPPQTPT-------PPDTPPLGKHSTTSPPSQPQSS 779
Cdd:pfam03154 256 PPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSQsqvppgpSPAAPGQSQQRIHTPPSQSQLQ 335
                         250
                  ....*....|.
gi 2024357528 780 TQDTSQSHSPP 790
Cdd:pfam03154 336 SQQPPREQPLP 346
PHA03247 PHA03247
large tegument protein UL36; Provisional
523-748 1.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  523 PAFQPPLPPTEAGV-LAHSGVEQHSQAAVAETSPVGAGFALSAGTAEQLQSQGNEDVSTSKPKDSTSSATPPPMRN---- 597
Cdd:PHA03247  2619 PDTHAPDPPPPSPSpAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSltsl 2698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  598 ------GGHVSTAPNQSASSTNQLSVNQPQNAAGPSPHSMRRAVKKPAPAPPKPANPPPGQPGSQSSAPAAQPPSISPKP 671
Cdd:PHA03247  2699 adppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024357528  672 LARSSSPPAqhanqgAAMTSSSQVSAPRRYSSSLSPIQAPSHPPPQPPTQATPPLQPKANNqASPSAPSSEHGPEQP 748
Cdd:PHA03247  2779 PPRRLTRPA------VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS-AQPTAPPPPPGPPPP 2848
 
Name Accession Description Interval E-value
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
13-258 0e+00

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


Pssm-ID: 153302  Cd Length: 246  Bit Score: 528.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQEGSAQLSDETLLG 92
Cdd:cd07618     1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLGEESLIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  93 KMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKTSGTNFQMHPS 172
Cdd:cd07618    81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 173 KIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQAHQDKWTEKPAFG 252
Cdd:cd07618   161 KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAFG 240

                  ....*.
gi 2024357528 253 TPLEEH 258
Cdd:cd07618   241 TPLEEH 246
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
247-446 5.97e-128

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: 381.80  E-value: 5.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 247 EKPAFGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQ--LDEFYSDPHAVAGA 324
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSlpLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 325 LKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024357528 405 GPNLLWAKTEGSLAEMAAATSVHVVAIIEPIIQHADWFFPGD 446
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGE 202
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
13-258 4.80e-116

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: 352.41  E-value: 4.80e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQEGSAQLSDETLLG 92
Cdd:cd07595     1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLPEYGLAQSMLESSKELPDDSLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  93 KMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKTSGtnFQMHPS 172
Cdd:cd07595    81 KVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSG--GQGAAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 173 KIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQAHQDKWTEKPAFG 252
Cdd:cd07595   159 KVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPVFG 238

                  ....*.
gi 2024357528 253 TPLEEH 258
Cdd:cd07595   239 QPLEEH 244
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-258 9.33e-115

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: 349.34  E-value: 9.33e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  13 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQEGSAQLSDETLLG 92
Cdd:cd07619     1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  93 KMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKTSG--TNFQMH 170
Cdd:cd07619    81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGlsSNLQPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 171 PSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQAHQDKWTEKPA 250
Cdd:cd07619   161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                  ....*...
gi 2024357528 251 FGTPLEEH 258
Cdd:cd07619   241 YGKPLEEH 248
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-240 7.58e-62

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: 208.73  E-value: 7.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528   1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQE 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  81 GSAQLSDETLLGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTeVEIPNIQKQRKQLAKLVLDWDSARGRYNQAH 160
Cdd:pfam03114  80 AGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 161 KTSGTNfqmhPSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEY-AKFFVMLLEAQADYHRKALAVIEKVLPEIQ 239
Cdd:pfam03114 159 KKKSSK----AKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQLG 234

                  .
gi 2024357528 240 A 240
Cdd:pfam03114 235 K 235
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
20-239 2.78e-61

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


Pssm-ID: 153304  Cd Length: 257  Bit Score: 207.87  E-value: 2.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  20 EKTEVLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQEGSAQLSDETLLGKMLDTCG 99
Cdd:cd07620     8 DATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDAESSIRRVLEMCC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 100 DAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKTSGTNFQMH--------- 170
Cdd:cd07620    88 FMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSeevgehqgi 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024357528 171 --PSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQ 239
Cdd:cd07620   168 rrANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELK 238
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
264-439 1.03e-58

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: 197.87  E-value: 1.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  264 REIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTS-QLDEFYSDPHAVAGALKSYLRELPEPLMTYALY 342
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  343 EEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKTEGSLAEMAa 422
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD- 159
                          170
                   ....*....|....*..
gi 2024357528  423 atSVHVVAIIEPIIQHA 439
Cdd:smart00324 160 --IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
268-413 6.67e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 188.91  E-value: 6.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 268 IPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALD-CSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALYEEWT 346
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDrGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024357528 347 QAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKT 413
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
BAR smart00721
BAR domain;
1-240 3.49e-53

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 184.90  E-value: 3.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528    1 MKKQFNRMKQLANQTVGRAEKTEvLSEDLLQIERRLDTVRSVFHIAQKRLIACFQGQYGTDPDKRHKKLPLTALAQNMQE 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528   81 GSA--QLSDETLLGKMLDTCGDAENKLALELSQHeVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYNQ 158
Cdd:smart00721  81 GDDgeGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  159 AHKTSGTNFQmhpSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKE-GEYAKFFVMLLEAQADYHRKALAVIEKVLPE 237
Cdd:smart00721 160 AKKSKEKKKD---EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRvDFFVNCLQALIEAQLNFHRESYKLLQQLQQQ 236

                   ...
gi 2024357528  238 IQA 240
Cdd:smart00721 237 LDK 239
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
268-438 1.50e-52

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: 180.58  E-value: 1.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 268 IPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALYEEWTQ 347
Cdd:cd00159     2 LIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 348 AANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKTEGslaEMAAATSVH 427
Cdd:cd00159    82 LAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSD---DELLEDIKK 158
                         170
                  ....*....|.
gi 2024357528 428 VVAIIEPIIQH 438
Cdd:cd00159   159 LNEIVEFLIEN 169
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-421 4.93e-38

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


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 140.55  E-value: 4.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEeHLKRSGREI-AIP--IEACVMMLLETGMREEGLFRIAAGASKLKKLKA----ALDCSTSQldefYSDPHAVAG 323
Cdd:cd04404     6 FGVSLQ-FLKEKNPEQePIPpvVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQkynmGEPVDFDQ----YEDVHLPAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 324 ALKSYLRELPEPLMTYALYEEWTQAANIqDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIV 403
Cdd:cd04404    81 ILKTFLRELPEPLLTFDLYDDIVGFLNV-DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVV 159
                         170
                  ....*....|....*....
gi 2024357528 404 LGPNLLWAK-TEGSLAEMA 421
Cdd:cd04404   160 FGPNLLWAKdASMSLSAIN 178
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-443 3.91e-36

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: 135.22  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDC-STSQL----DEFYSDPHAVAGAL 325
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKdPLNVLlispEDYESDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 326 KSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLG 405
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024357528 406 PNLLWAKTEgSLAEMAAATSVhvvaiIEPIIQHADWFF 443
Cdd:cd04398   161 PTLMNAAPD-NAADMSFQSRV-----IETLLDNAYQIF 192
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
251-442 2.08e-34

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: 130.26  E-value: 2.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEE---HLKRSGREIA-IPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALK 326
Cdd:cd04390     3 FGQRLEDtvaYERKFGPRLVpILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 327 SYLRELPEPLMTYALYEEWTQAANI--QDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04390    83 LYLRELPEPVIPWAQYEDFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVF 162
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2024357528 405 GPNLLWAKTEGSLAEMAAATSV-HVVAIIepIIQHADWF 442
Cdd:cd04390   163 GPNILRPKVEDPATIMEGTPQIqQLMTVM--ISKHEPLF 199
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
250-443 7.46e-34

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


Pssm-ID: 239860  Cd Length: 196  Bit Score: 128.67  E-value: 7.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 250 AFGTPLEEHLKRSGRE-IAIPIEACVMMLLETGMREEGLFRI---AAGASKLKK-LKAALDCSTSQlDEFYSDPHAVAGA 324
Cdd:cd04395     1 TFGVPLDDCPPSSENPyVPLIVEVCCNIVEARGLETVGIYRVpgnNAAISALQEeLNRGGFDIDLQ-DPRWRDVNVVSSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 325 LKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04395    80 LKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVF 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2024357528 405 GPNLLwAKTEGSLAEMAAATSvHVVAIIEPIIQHADWFF 443
Cdd:cd04395   160 GPTLV-RTSDDNMETMVTHMP-DQCKIVETLIQHYDWFF 196
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-443 4.11e-31

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


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 120.70  E-value: 4.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLD---EFYSDPHAVAGALKS 327
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADisaTVYPDINVITGALKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 328 YLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPN 407
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2024357528 408 LLWAKTEGSLAEMAAATsvHVVAIIEPIIQHADWFF 443
Cdd:cd04372   161 LMRPPEDSALTTLNDMR--YQILIVQLLITNEDVLF 194
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-409 6.63e-31

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: 119.87  E-value: 6.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEhLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTS-QLDEFYSDPHAVAGALKSYL 329
Cdd:cd04373     1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNlDLVSKDFTVNAVAGALKSFF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 330 RELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLL 409
Cdd:cd04373    80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLM 159
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
269-439 1.15e-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: 116.63  E-value: 1.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 269 PIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDcsTSQLDEFYSDP-HAVAGALKSYLRELPEPLMTYALYEEWTQ 347
Cdd:cd04402    18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLN--SGVEVDLKAEPvLLLASVLKDFLRNIPGSLLSSDLYEEWMS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 348 AANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWaktEGSLAEMAAATSVH 427
Cdd:cd04402    96 ALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLW---PPASSELQNEDLKK 172
                         170
                  ....*....|..
gi 2024357528 428 VVAIIEPIIQHA 439
Cdd:cd04402   173 VTSLVQFLIENC 184
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-432 3.68e-28

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


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 112.21  E-value: 3.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 249 PAFGTPLEEHLKRSGREIAIPIEACVMMLLETGMrEEGLFRIAAGASKLKKLKAALD---CSTSQLDEFYSDPHAVAGAL 325
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDseqIPDLTKDVYIQDIHSVSSLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 326 KSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLG 405
Cdd:cd04384    80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2024357528 406 PNLLWAK------TEGSLAEMAAATSVHVVAII 432
Cdd:cd04384   160 PNLLRSKqiesacFSGTAAFMEVRIQSVVVEFI 192
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
251-418 6.80e-28

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


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 111.33  E-value: 6.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDC--STSQLDEFYSDPHAVAGALKSY 328
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHdeKLDLDDSKWEDIHVITGALKLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 329 LRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNL 408
Cdd:cd04403    81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160
                         170
                  ....*....|.
gi 2024357528 409 LWAKTE-GSLA 418
Cdd:cd04403   161 LRPEQEtGNIA 171
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
281-409 9.88e-28

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: 110.61  E-value: 9.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 281 GMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQE 360
Cdd:cd04377    30 GLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERVRA 109
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2024357528 361 LWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLL 409
Cdd:cd04377   110 LYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCIL 158
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
251-408 3.43e-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: 109.37  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRS-----GREIAIPIEACVMMLLETG-MREEGLFRIAAGASKLKKLKAALD-------CSTSQldefYSD 317
Cdd:cd04400     2 FGSPLEEAVELSshkynGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNteydvdlFSSSL----YPD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 318 PHAVAGALKSYLRELPEPLMTYALYEEWTQAANIQ-DQDKKLQELWKICNKLPkhyHANF---RYLIKFLAKLAQNSDVN 393
Cdd:cd04400    78 VHTVAGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLP---QANYdllYVLFSFLRKIIEHSDVN 154
                         170
                  ....*....|....*
gi 2024357528 394 KMTPSNVAIVLGPNL 408
Cdd:cd04400   155 KMNLRNVCIVFSPTL 169
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
267-438 1.31e-26

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


Pssm-ID: 239850  Cd Length: 184  Bit Score: 107.39  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 267 AIPI--EACVMMLLETGMREEGLFRIAAGASKLKKLKAAL--DCSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALY 342
Cdd:cd04385    14 DIPVivDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 343 EEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKtegslaEMAA 422
Cdd:cd04385    94 AEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTD------EHSV 167
                         170
                  ....*....|....*.
gi 2024357528 423 ATSVHVVAIIEPIIQH 438
Cdd:cd04385   168 GQTSHEVKVIEDLIDN 183
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
72-237 2.14e-26

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: 107.15  E-value: 2.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  72 TALAQNMQEGSAQLSDETL--LGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDW 149
Cdd:cd07307    31 EKLSEALQELGKELPDLSNtdLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 150 DSARGRYNQAHKTSGTnfqmhPSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGE-YAKFFVMLLEAQADYHRKAL 228
Cdd:cd07307   111 DAAREKLKKLRKKKKD-----SSKLAEAEEELQEAKEKYEELREELIEDLNKLEEKRKElFLSLLLSFIEAQSEFFKEVL 185

                  ....*....
gi 2024357528 229 AVIEKVLPE 237
Cdd:cd07307   186 KILEQLLPY 194
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
256-420 4.16e-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: 106.71  E-value: 4.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 256 EEHLKRSGREIaipIEACVMMLLETGMREEGLFRIAAGASKLKKLKAAL----DCSTSQLDEFYS--DPHAVAGALKSYL 329
Cdd:cd04374    21 EAQLDDIGFKF---VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDNSewEIKTITSALKTYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 330 RELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLL 409
Cdd:cd04374    98 RNLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLL 177
                         170
                  ....*....|.
gi 2024357528 410 WAKTEGSLAEM 420
Cdd:cd04374   178 RPQEETVAAIM 188
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
281-409 2.96e-25

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


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 103.53  E-value: 2.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 281 GMREEGLFRIAAGASKLKKLKAAL--DCSTSQLDEFysdP-HAVAGALKSYLRELPEPLMTYALYEEWTQAANIQDQDKK 357
Cdd:cd04407    30 GLYTEGIYRKSGSANRMKELHQLLqaDPENVKLENY---PiHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQ 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024357528 358 LQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLL 409
Cdd:cd04407   107 LQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLL 158
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
251-438 2.47e-24

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


Pssm-ID: 239848  Cd Length: 188  Bit Score: 100.96  E-value: 2.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQL--DEFYSDPHAVAGALKSY 328
Cdd:cd04383     3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLadDQNDHDINSVAGVLKLY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 329 LRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNL 408
Cdd:cd04383    83 FRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTL 162
                         170       180       190
                  ....*....|....*....|....*....|
gi 2024357528 409 LWAKTEGSLAEMAAatsvHVVAIIEPIIQH 438
Cdd:cd04383   163 MPVPEGQDQVSCQA----HVNELIKTIIIH 188
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-439 3.99e-24

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


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 101.01  E-value: 3.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLE----EHLKRSGREIAIPIEACvmMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYsdPHAVAGALK 326
Cdd:cd04394     2 FGVPLHslphSTVPEYGNVPKFLVDAC--TFLLDHLSTEGLFRKSGSVVRQKELKAKLEGGEACLSSAL--PCDVAGLLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 327 SYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGP 406
Cdd:cd04394    78 QFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAP 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2024357528 407 NLLwaKTEGSLAEMAAATSV---HVVAIIEPIIQHA 439
Cdd:cd04394   158 NLF--QSEEGGEKMSSSTEKrlrLQAAVVQTLIDNA 191
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
251-408 4.56e-24

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


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 100.20  E-value: 4.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRS----GREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTS-QLDEFysDPHAVAGAL 325
Cdd:cd04381     1 FGASLSLAVERSrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESpNLEEY--EPPTVASLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 326 KSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLG 405
Cdd:cd04381    79 KQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLS 158

                  ...
gi 2024357528 406 PNL 408
Cdd:cd04381   159 PTV 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-444 2.14e-23

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


Pssm-ID: 239856  Cd Length: 216  Bit Score: 99.34  E-value: 2.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGR---EIAIPI--EACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCstsqldEFYSD-------- 317
Cdd:cd04391     2 FGVPLSTLLERDQKkvpGSKVPLifQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEA------KFYEGtflwdqvk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 318 PHAVAGALKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTP 397
Cdd:cd04391    76 QHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024357528 398 SNVAIVLGPNL-----LWAKTEGSLAE---MAAATSVhvvaIIEPIIQHAD--WFFP 444
Cdd:cd04391   156 WNVAMIMAPNLfpprgKHSKDNESLQEevnMAAGCAN----IMRLLIRYQDllWTVP 208
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
251-409 2.54e-23

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: 98.46  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYS--DPHAVAGALKSY 328
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSemDVNAIAGTLKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 329 LRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNL 408
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160

                  .
gi 2024357528 409 L 409
Cdd:cd04387   161 L 161
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
270-443 3.62e-23

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


Pssm-ID: 239841  Cd Length: 206  Bit Score: 98.28  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 270 IEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTS-QLDEFYSdPHAVAGALKSYLRELPEPLMTYALYEEWTQA 348
Cdd:cd04376    13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDvVLDENHS-VHDVAALLKEFFRDMPDPLLPRELYTAFIGT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 349 A--NIQDQDKKLQELWKIcnkLPKHYHANFRYLIKFLAKLAQNSDV-----------NKMTPSNVAIVLGPNLL----WA 411
Cdd:cd04376    92 AllEPDEQLEALQLLIYL---LPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLhkqkSG 168
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2024357528 412 KTEGSLAEMAAATSVHVVAIIEPIIQHADWFF 443
Cdd:cd04376   169 EREFVQASLRIEESTAIINVVQTMIDNYEELF 200
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
251-433 9.25e-23

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: 97.15  E-value: 9.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSG--REIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLD---EFYSDPHAVAGAL 325
Cdd:cd04379     1 FGVPLSRLVEREGesRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVElseELYPDINVITGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 326 KSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQE---LWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAI 402
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNthlTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2024357528 403 VLGPNLLWAKTEGSLAEMAAATSVHVVAIIE 433
Cdd:cd04379   161 CFGPVLMFCSQEFSRYGISPTSKMAAVSTVD 191
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-416 9.94e-23

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: 97.05  E-value: 9.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGRE-----------IAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSD-P 318
Cdd:cd04397     1 FGVPLEILVEKFGADstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 319 HAVAGALKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDV-----N 393
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgS 160
                         170       180
                  ....*....|....*....|...
gi 2024357528 394 KMTPSNVAIVLGPNLLWAKTEGS 416
Cdd:cd04397   161 KMDIHNLATVITPNILYSKTDNP 183
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-408 6.47e-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: 91.37  E-value: 6.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 249 PAFGTPLEEhLKRSGR---EIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGAL 325
Cdd:cd04393     1 KVFGVPLQE-LQQAGQpenGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 326 KSYLRELPEPLMTYALYEEWTQA-ANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04393    80 RLFLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVF 159

                  ....
gi 2024357528 405 GPNL 408
Cdd:cd04393   160 GPDV 163
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
251-438 8.65e-21

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


Pssm-ID: 239843  Cd Length: 203  Bit Score: 91.33  E-value: 8.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLR 330
Cdd:cd04378     1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 331 ELPEPLMTYALYEEW------TQAANIQDQDKK--------LQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMT 396
Cdd:cd04378    81 QLPEPLILFRLYNDFialakeIQRDTEEDKAPNtpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2024357528 397 PSNVAIVLGPNLLWAK-TEGSLAEMAAATSVHVVAIIEPIIQH 438
Cdd:cd04378   161 PNNLGIVFGPTLIRPRpGDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
251-409 3.50e-20

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: 88.90  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEhLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLR 330
Cdd:cd04406     1 FGVELSR-LTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024357528 331 ELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLL 409
Cdd:cd04406    80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
247-408 2.28e-19

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


Pssm-ID: 239840  Cd Length: 220  Bit Score: 87.47  E-value: 2.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 247 EKPAFGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDefYSDPHA--VAGA 324
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVN--YDGQQAydVADM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 325 LKSYLRELPEPLMTYALYEEWTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVL 404
Cdd:cd04375    79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCL 158

                  ....
gi 2024357528 405 GPNL 408
Cdd:cd04375   159 APSL 162
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
268-408 4.94e-19

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: 85.81  E-value: 4.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 268 IP--IEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALYEEW 345
Cdd:cd04382    17 IPalIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKEF 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024357528 346 TQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQnSDVNKMTPSNVAIVLGPNL 408
Cdd:cd04382    97 MEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTI 158
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-438 6.99e-18

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


Pssm-ID: 239874  Cd Length: 211  Bit Score: 82.93  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTS--QLDEFYsdPHAVAGALKSY 328
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDlvELSELS--PHDISNVLKLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 329 LRELPEPLMTYALYEEW------TQAANIQDQDKKLQ---------ELWKICNK-------LPKHYHANFRYLIKFLAKL 386
Cdd:cd04409    79 LRQLPEPLILFRLYNEFiglakeSQHVNETQEAKKNSdkkwpnmctELNRILLKskdllrqLPAPNYNTLQFLIVHLHRV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024357528 387 AQNSDVNKMTPSNVAIVLGPNLLWAK-TEGSLAEMAAATSVHVVAIIEPIIQH 438
Cdd:cd04409   159 SEQAEENKMSASNLGIIFGPTLIRPRpTDATVSLSSLVDYPHQARLVELLITY 211
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
281-409 4.13e-17

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


Pssm-ID: 239854  Cd Length: 187  Bit Score: 80.13  E-value: 4.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 281 GMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFySDPHAVAGALKSYLRELPEPLMTYALYEEWTQAANIQDQDKklqe 360
Cdd:cd04389    37 GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGL-EDPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKAV---- 111
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024357528 361 lwKICNKLPKHYHANFRYLIKFLAKLAQNSDV--NKMTPSNVAIVLGPNLL 409
Cdd:cd04389   112 --EIVQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNIL 160
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
251-438 9.98e-17

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


Pssm-ID: 239873  Cd Length: 200  Bit Score: 79.48  E-value: 9.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIAIPIEACVMMLLETGMREEGLFRIAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLR 330
Cdd:cd04408     1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 331 ELPEPLMTYALYEEWT------QAANIQDQDKK------LQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPS 398
Cdd:cd04408    81 ELPEPVLPFQLYDDFIalakelQRDSEKAAESPsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2024357528 399 NVAIVLGPNLLWAKTEGSLAEMAAATSVHVVAIIEPIIQH 438
Cdd:cd04408   161 NLGIVFGPTLLRPLVGGDVSMICLLDTGYQAQLVEFLISN 200
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
251-442 1.71e-15

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 76.68  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEEHLKRSGREIA-------------IPI--EACVMMLLETGMREEGLFRIAAGASKLKKLKAAL----DCSTSQL 311
Cdd:cd04396     2 FGVSLEESLKYASVAISivdedgeqyvygyIPVvvAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFstppDYGKSFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 312 DEFYSdPHAVAGALKSYLRELPEPLMTYALYEEW----TQAANIQ-------------DQDKKLQELWKICNKLPKHYHA 374
Cdd:cd04396    82 WDGYT-VHDAASVLRRYLNNLPEPLVPLDLYEEFrnplRKRPRILqymkgrineplntDIDQAIKEYRDLITRLPNLNRQ 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024357528 375 NFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLW-AKTEGSLAEMAAATSVhvvaiIEPIIQHADWF 442
Cdd:cd04396   161 LLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILShPDHEMDPKEYKLSRLV-----VEFLIEHQDKF 224
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
278-443 2.16e-15

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: 75.96  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 278 LETGMREEGLFRIAAGASKLKKLKAALDCSTS-QLDEFYSDPHAVAGALKSYLRELPEPLMTYALY------------EE 344
Cdd:cd04392    20 LEKNLRVEGLFRKPGNSARQQELRDLLNSGTDlDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYpahlqiadlcqfDE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 345 WTQAANIQDQDKKLQELWKICNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLLWAKTEGslAEMAAAT 424
Cdd:cd04392   100 KGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLT--PEDLHEN 177
                         170
                  ....*....|....*....
gi 2024357528 425 SVHVVAIIEPIIQHADWFF 443
Cdd:cd04392   178 AQKLNSIVTFMIKHSQKLF 196
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
251-423 1.02e-14

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: 73.91  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 251 FGTPLEE--HLKRSGREI------------------AIPIE--ACVMMLLETGMREEGLFRIAAGASKLKKLKA----AL 304
Cdd:cd04380    13 FGSSLETliRLPDPGIRNlidqlelgdnpdysevplSIPKEiwRLVDYLYTRGLAQEGLFEEPGLPSEPGELLAeirdAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 305 DCSTSqlDEFYSDPHAVAGALKSYLRELPEPLMTYALYEEWTQAANIQDQDKKlqelWKICNKLPKHYHANFRYLIKFLA 384
Cdd:cd04380    93 DTGSP--FNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNEEDKR----QVIRISLPPVHRNVFVYLCSFLR 166
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2024357528 385 KLAQNSDVNKMTPSNVAIVLGPNLLWAKTEGSLAEMAAA 423
Cdd:cd04380   167 ELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAE 205
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
280-409 2.92e-12

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 66.44  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 280 TGMREEGLFRiAAGASKLKKLKAALDCSTSQLDEFYSDPHAVAGALKSYLRELPEPLMTYALY-EEWTQAANIQDQDKKL 358
Cdd:cd04388    29 KGLESSTLYR-TQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYsEMISRAQEVQSSDEYA 107
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024357528 359 QELWKI--CNKLPKHYHANFRYLIKFLAKLAQNSDVNKMTPSNVAIVLGPNLL 409
Cdd:cd04388   108 QLLRKLirSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
20-234 4.02e-10

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


Pssm-ID: 153276  Cd Length: 223  Bit Score: 60.79  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  20 EKTEvLSEDLLQIERRLDTVRSVFHIAQKRLIACFQgqygTDPDKRHK--------KLPLTA-----------LAQNMQE 80
Cdd:cd07592     1 EGTK-LDDEFLEMERKTDATSKLVEDLIPKTKEYLQ----PNPAARAKlamqntysKIRGQAkstkypqpeglLGEVMLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  81 GSAQLSDETLLGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDsargrYNQAH 160
Cdd:cd07592    76 YGRELGEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYD-----YKKRK 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024357528 161 KTSGTNfqmhpskidslkEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKV 234
Cdd:cd07592   151 QGKGPD------------EELKQAEEKFEESKELAENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEEL 212
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
70-234 1.44e-09

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


Pssm-ID: 153298  Cd Length: 223  Bit Score: 58.96  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  70 PLTALAQNMQEGSAQLSDETLLGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDW 149
Cdd:cd07614    65 SEGLLGETMIRYGKELGDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDF 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 150 DSARGRynqahktsgtnfqmhPSKIDSlkEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALA 229
Cdd:cd07614   145 DYKKKR---------------QGKIPD--EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQ 207

                  ....*
gi 2024357528 230 VIEKV 234
Cdd:cd07614   208 ILDEL 212
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
25-239 3.13e-09

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: 58.09  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  25 LSEDLLQIERRLDTV-RSVFHIAQKRlIACFQgqygTDPDKRHK--------------KLP-----LTALAQNMQEGSAQ 84
Cdd:cd07613     5 LDDDFKEMERKVDVTsRAVMEIMTKT-IEYLQ----PNPASRAKlsmintmskirgqeKGPgypqaEALLAEAMLKFGRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  85 LSDETLLGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRynQAHKTsg 164
Cdd:cd07613    80 LGDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKR--QGKIP-- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024357528 165 tnfqmhpskidslKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQ 239
Cdd:cd07613   156 -------------DEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLE 217
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
25-239 7.40e-09

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: 56.95  E-value: 7.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  25 LSEDLLQIERRLD-TVRSVFHIAQK------------------RLIACFQGQYGTDPDKRHKKLpltaLAQNMQEGSAQL 85
Cdd:cd07615     5 LDDDFQEMERKIDvTNKVVAELLSKtteylqpnpayraklgmlNTVSKIRGQVKTTGYPQTEGL----LGDCMLRYGREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  86 SDETLLGKMLDTCGDAENKLALELSQHEVQIEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSARGRYnqahktsgt 165
Cdd:cd07615    81 GEESTFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFDYKKKRQ--------- 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024357528 166 nfqmhpSKIDSlkEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQADYHRKALAVIEKVLPEIQ 239
Cdd:cd07615   152 ------GKIPD--EEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILEDLQSKLQ 217
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
10-159 3.69e-07

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


Pssm-ID: 153278  Cd Length: 229  Bit Score: 52.01  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  10 QLANQTVGRAEKTEvLSEDLLQIERRLDTVRsvfhIAQKRLIACFQGQYGTDPDKR-----------HKKLPLTA---LA 75
Cdd:cd07594     1 QFTEEKLGTAEKTE-YDAHFENLLQRADKTK----VWTEKILKQTEAVLQPNPNVRvedfiyekldrKKPDRLSNleqLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  76 QNMQEGSAQLSDETLLGKMLDTCGDAENKLALelSQHEVQ--IEKDILEPLNTLTEVEIPNIQKQRKQLAKLVLDWDSAR 153
Cdd:cd07594    76 QAMIEAGNDFGPGTAYGSALIKVGQAQKKLGQ--AEREFIqtSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACK 153

                  ....*.
gi 2024357528 154 GRYNQA 159
Cdd:cd07594   154 TRVKKA 159
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
67-238 2.42e-06

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: 49.66  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  67 KKLPLT---ALAQNMQEGSAQLS-----DETLLGKMLDTCGDAENKLA-LELSQhEVQIEKDILEPLNTLTEVEIPNIQK 137
Cdd:cd07600    73 AKLPKTlnhALSRAALASSLELKslepeDEDPLSKALGKYSDAEEKIAeARLEQ-DQLIQKEFNAKLRETLNTSFQKAHK 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 138 QRKQLAKLVLDWDSARGRYNQAHKtsgtnfqmhPSKIDSLKEEMdeagnkvEQCKDQLAAD-------MYNfVSKEGEYA 210
Cdd:cd07600   152 ARKKVEDKRLQLDTARAELKSAEP---------AEKQEAARVEV-------ETAEDEFVSAteeavelMKE-VLDNPEPL 214
                         170       180
                  ....*....|....*....|....*...
gi 2024357528 211 KFFVMLLEAQADYHRKALAVIEKVLPEI 238
Cdd:cd07600   215 QLLKELVKAQLAYHKTAAELLEELLSVL 242
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
140-237 7.74e-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: 44.65  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 140 KQLAKLVLDWDSARGRYN----QAHKTSGTNFQmHPSKIDSLKEEMDEAGNKVEQCKDQLAADMYNFV--------SKEG 207
Cdd:cd07596   110 DDRADALLTLQSLKKDLAskkaQLEKLKAAPGI-KPAKVEELEEELEEAESALEEARKRYEEISERLKeelkrfheERAR 188
                          90       100       110
                  ....*....|....*....|....*....|
gi 2024357528 208 EYAKFFVMLLEAQADYHRKALAVIEKVLPE 237
Cdd:cd07596   189 DLKAALKEFARLQVQYAEKIAEAWESLLPE 218
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
563-790 1.90e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 563 SAGTAEQLQSQGNEDVSTSKPKD------STSSATPPPMRNGGHVSTAPNQSASSTNQLSVNQPQNAAGPSPhsmrravk 636
Cdd:pfam03154 114 SEGEGESSDGRSVNDEGSSDPKDidqdnrSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS-------- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 637 kpapappkpaNPPPGQPGSQSSAPAAQPPSISPKPLARSSSPPAQHANQGAAMT--SSSQVSAPRRYSSSLSPIQAPSHP 714
Cdd:pfam03154 186 ----------PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQRLPSPHPPLQPMTQP 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 715 PPQPPTQATPPLQPKANNQASPSAPSSEHGPE--------QPCYTPPQTPT-------PPDTPPLGKHSTTSPPSQPQSS 779
Cdd:pfam03154 256 PPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSQsqvppgpSPAAPGQSQQRIHTPPSQSQLQ 335
                         250
                  ....*....|.
gi 2024357528 780 TQDTSQSHSPP 790
Cdd:pfam03154 336 SQQPPREQPLP 346
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
63-250 3.14e-04

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


Pssm-ID: 153277  Cd Length: 215  Bit Score: 43.11  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  63 DKRHKKLPLTALAQNMQEGSAQLSDETLLGKMLDTCGDAENKLAlELSQHEVQIEKDI-LEPL-NTLteVEIPNIQKQRK 140
Cdd:cd07593    45 DDKDKCLPVEALGLVMINHGEEFPQDSEYGSCLSKLGRAHCKIG-TLQEEFADRLSDTfLANIeRSL--AEMKEYHSARK 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 141 QLAKLVLDWDSARGRYNQAHKTSGtnfqmhpskidSLKEEMDEAGNKVEQCKDQLAADMYNFVSKEGEYAKFFVMLLEAQ 220
Cdd:cd07593   122 KLESRRLAYDAALTKSQKAKKEDS-----------RLEEELRRAKAKYEESSEDVEARMVAIKESEADQYRDLTDLLDAE 190
                         170       180       190
                  ....*....|....*....|....*....|
gi 2024357528 221 ADYHRKALAVIEKVlpeiqahQDKWTEKPA 250
Cdd:cd07593   191 LDYHQQSLDVLREV-------RQSWPSKSS 213
PHA03247 PHA03247
large tegument protein UL36; Provisional
523-748 1.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  523 PAFQPPLPPTEAGV-LAHSGVEQHSQAAVAETSPVGAGFALSAGTAEQLQSQGNEDVSTSKPKDSTSSATPPPMRN---- 597
Cdd:PHA03247  2619 PDTHAPDPPPPSPSpAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSltsl 2698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  598 ------GGHVSTAPNQSASSTNQLSVNQPQNAAGPSPHSMRRAVKKPAPAPPKPANPPPGQPGSQSSAPAAQPPSISPKP 671
Cdd:PHA03247  2699 adppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024357528  672 LARSSSPPAqhanqgAAMTSSSQVSAPRRYSSSLSPIQAPSHPPPQPPTQATPPLQPKANNqASPSAPSSEHGPEQP 748
Cdd:PHA03247  2779 PPRRLTRPA------VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS-AQPTAPPPPPGPPPP 2848
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
521-794 1.86e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 521 TSPAFQP---PLPPTEAGVLAHSGVEQHSQAAvAETSPVGAGFALSAGTAEQLQSQGNEDVSTSKPKDSTSSATPPPMRN 597
Cdd:pfam05109 430 TSPTLNTtgfAAPNTTTGLPSSTHVPTNLTAP-ASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTS 508
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 598 GGHVSTAPNQSASSTNQLSVNQPQNAAGPS--PHSMRRAVKKPAPAPPKPAnpppgqPGSQSSAPAAQPPSI-------- 667
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNATSPTlgKTSPTSAVTTPTPNATSPT------PAVTTPTPNATIPTLgktsptsa 582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 668 --SPKPLARS-----SSPPAQHANQGAAMTSSSQV--SAPRRYSSSLSpiqaPSHPPPQPPTQATPPLQPKANNQA-SPS 737
Cdd:pfam05109 583 vtTPTPNATSptvgeTSPQANTTNHTLGGTSSTPVvtSPPKNATSAVT----TGQHNITSSSTSSMSLRPSSISETlSPS 658
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024357528 738 AP--SSEHGP----EQPCYTPPQTPTPPDTPPLGKHSTTSPPSQPQSstqdTSQSHSPPHSGT 794
Cdd:pfam05109 659 TSdnSTSHMPlltsAHPTGGENITQVTPASTSTHHVSTSSPAPRPGT----TSQASGPGNSST 717
PHA03247 PHA03247
large tegument protein UL36; Provisional
523-790 1.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  523 PAFQPPLPPTEAGVLAHSGVEQHSQAAVAETS-----PVGAGFALSAGTAEQLQSQgnedvSTSKPkdstSSATPPPMRN 597
Cdd:PHA03247  2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAapappAVPAGPATPGGPARPARPP-----TTAGP----PAPAPPAAPA 2776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  598 GGHVSTAPNQSASStnqLSVNQPQNAAGPSPHSMRRAVKKPAPAPPKPANPPPGQPGSQSSAPAAQP----PSISPKPLA 673
Cdd:PHA03247  2777 AGPPRRLTRPAVAS---LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPpppgPPPPSLPLG 2853
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528  674 RSSSPPAQHANQGAAMTSSSQVSAPRRYSSSLSPiqapshpppqpPTQATPPLQPKANNQASPSAPSSEHGPEQPcyTPP 753
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA-----------RPAVSRSTESFALPPDQPERPPQPQAPPPP--QPQ 2920
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2024357528  754 QTPTPPDTPPLGKHSTTSPPSQPQSSTQDTSQSHSPP 790
Cdd:PHA03247  2921 PQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
RhoGAP_fMSB1 cd04401
RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
312-411 6.15e-03

RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal MSB1-like proteins. Msb1 was originally identified as a multicopy suppressor of temperature sensitive cdc42 mutation. Msb1 is a positive regulator of the Pkc1p-MAPK pathway and 1,3-beta-glucan synthesis, both pathways involve Rho1 regulation. 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: 239866  Cd Length: 198  Bit Score: 38.87  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024357528 312 DEFYSDPHAVAGALKSYLRELPEPLMT-YALYEEWTQAANIQDQDKK-LQELWKICnkLPKHYHANFRY-LIKFLAKLAQ 388
Cdd:cd04401    64 ELRYADPHTLILVLKWIWSRLPGSKVIwWEVYEEFKARERRSNYPADaFLDLLPQC--LSSPAHASILYdFFDLLSSIAA 141
                          90       100
                  ....*....|....*....|...
gi 2024357528 389 NSDVNKMTPSNVAIVLGPnllWA 411
Cdd:cd04401   142 HSSVNGMSGRKLSKMAGP---WA 161
 
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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