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Conserved domains on  [gi|530410838|ref|XP_005256948|]
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rho GTPase-activating protein 44 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
13-260 2.18e-172

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07619:

Pssm-ID: 472257  Cd Length: 248  Bit Score: 494.18  E-value: 2.18e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  13 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLG 92
Cdd:cd07619    1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  93 KMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPA 172
Cdd:cd07619   81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 173 GAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPS 252
Cdd:cd07619  161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                 ....*...
gi 530410838 253 FGKPLEEH 260
Cdd:cd07619  241 YGKPLEEH 248
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
249-449 1.89e-102

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


The actual alignment was detected with superfamily member cd04386:

Pssm-ID: 470621  Cd Length: 203  Bit Score: 312.85  E-value: 1.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 249 EKPSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 326
Cdd:cd04386    1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 327 LKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVL 406
Cdd:cd04386   81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530410838 407 GPNLLWPQAEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEI 449
Cdd:cd04386  161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
471-686 7.47e-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: 43.22  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  471 SMPSP-----DMDPADRRQPEQARRPLSvatdnmmlefykkdgTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQ 545
Cdd:pfam03154 147 SIPSPqdnesDSDSSAQQQILQTQPPVL---------------QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  546 PGASPSPSQPPADQSPHTLRKVSKKLApiPPKVPfgQPGAMADQSAGQPSPVSLSPTPPSTPSPYGLSYPQGYSLASGQL 625
Cdd:pfam03154 212 PATSQPPNQTQSTAAPHTLIQQTPTLH--PQRLP--SPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS 287
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410838  626 SPAAAPPLASPSVfTSTLSKSRPTPKPRQRPTLPPPQPPTVNLSASSPQSTEAPMLDGMSP 686
Cdd:pfam03154 288 HMQHPVPPQPFPL-TPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP 347
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-260 2.18e-172

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: 494.18  E-value: 2.18e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  13 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLG 92
Cdd:cd07619    1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  93 KMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPA 172
Cdd:cd07619   81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 173 GAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPS 252
Cdd:cd07619  161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                 ....*...
gi 530410838 253 FGKPLEEH 260
Cdd:cd07619  241 YGKPLEEH 248
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-449 1.89e-102

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: 312.85  E-value: 1.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 249 EKPSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 326
Cdd:cd04386    1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 327 LKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVL 406
Cdd:cd04386   81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530410838 407 GPNLLWPQAEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEI 449
Cdd:cd04386  161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-242 4.93e-69

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: 226.45  E-value: 4.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838    1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLME 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   81 GSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAeVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTS 160
Cdd:pfam03114  80 AGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  161 KSSGLSSSLQPagakadALREEMEEAANRVEICRDQLSADMYSFVAKEIDY-ANYFQTLIEVQAEYHRKSLTLLQAVLPQ 239
Cdd:pfam03114 159 KKKSSKAKDES------QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQ 232

                  ...
gi 530410838  240 IKA 242
Cdd:pfam03114 233 LGK 235
BAR smart00721
BAR domain;
1-242 3.36e-60

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 203.00  E-value: 3.36e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838     1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLME 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838    81 GSAI--LGDDTLLGKMLKLCGETEDKLAQELIHFeLQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQ 158
Cdd:smart00721  81 GDDGegLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   159 TskssgLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEID-YANYFQTLIEVQAEYHRKSLTLLQAVL 237
Cdd:smart00721 160 A-----KKSKEKKKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQ 234

                   ....*
gi 530410838   238 PQIKA 242
Cdd:smart00721 235 QQLDK 239
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
266-441 1.62e-59

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 198.64  E-value: 1.62e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   266 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSeYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   345 DEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEGNITEMMT 424
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 530410838   425 TvslQIVGIIEPIIQHA 441
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
270-415 3.38e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 183.13  E-value: 3.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  270 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-VVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWI 348
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530410838  349 QASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQA 415
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
471-686 7.47e-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: 43.22  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  471 SMPSP-----DMDPADRRQPEQARRPLSvatdnmmlefykkdgTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQ 545
Cdd:pfam03154 147 SIPSPqdnesDSDSSAQQQILQTQPPVL---------------QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  546 PGASPSPSQPPADQSPHTLRKVSKKLApiPPKVPfgQPGAMADQSAGQPSPVSLSPTPPSTPSPYGLSYPQGYSLASGQL 625
Cdd:pfam03154 212 PATSQPPNQTQSTAAPHTLIQQTPTLH--PQRLP--SPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS 287
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410838  626 SPAAAPPLASPSVfTSTLSKSRPTPKPRQRPTLPPPQPPTVNLSASSPQSTEAPMLDGMSP 686
Cdd:pfam03154 288 HMQHPVPPQPFPL-TPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP 347
PHA03378 PHA03378
EBNA-3B; Provisional
434-596 1.30e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.36  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 434 IEPIIQHADWFFPGEIEFNitgnygsPVHVNHNANY----------------SSMPSPDMDPADRRQPEQA--RRPLSVA 495
Cdd:PHA03378 657 VEITPYKPTWTQIGHIPYQ-------PSPTGANTMLpiqwapgtmqppprapTPMRPPAAPPGRAQRPAAAtgRARPPAA 729
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 496 TDNMMLEFYKKDGTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQPGASPSPSQPPadqsphtlrkvskKLAPIP 575
Cdd:PHA03378 730 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRP-------------RGAPTP 796
                        170       180
                 ....*....|....*....|....
gi 530410838 576 PKVPFGQPGAM---ADQSAGQPSP 596
Cdd:PHA03378 797 QPPPQAGPTSMqlmPRAAPGQQGP 820
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
13-260 2.18e-172

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: 494.18  E-value: 2.18e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  13 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLG 92
Cdd:cd07619    1 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGAAVLGDDSLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  93 KMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPA 172
Cdd:cd07619   81 KMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 173 GAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPS 252
Cdd:cd07619  161 GAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPS 240

                 ....*...
gi 530410838 253 FGKPLEEH 260
Cdd:cd07619  241 YGKPLEEH 248
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
13-260 3.63e-119

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: 357.81  E-value: 3.63e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  13 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLG 92
Cdd:cd07618    1 NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGSAQLGEESLIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  93 KMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPa 172
Cdd:cd07618   81 KMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMP- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 173 gAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPS 252
Cdd:cd07618  160 -SKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPA 238

                 ....*...
gi 530410838 253 FGKPLEEH 260
Cdd:cd07618  239 FGTPLEEH 246
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
13-260 1.47e-114

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: 345.47  E-value: 1.47e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  13 NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLG 92
Cdd:cd07595    1 DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLPEYGLAQSMLESSKELPDDSLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  93 KMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTskssGLSSSLQPA 172
Cdd:cd07595   81 KVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAA----HKSSGGQGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 173 GAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPS 252
Cdd:cd07595  157 AAKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPV 236

                 ....*...
gi 530410838 253 FGKPLEEH 260
Cdd:cd07595  237 FGQPLEEH 244
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-449 1.89e-102

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: 312.85  E-value: 1.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 249 EKPSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 326
Cdd:cd04386    1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 327 LKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVL 406
Cdd:cd04386   81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530410838 407 GPNLLWPQAEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEI 449
Cdd:cd04386  161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-242 4.93e-69

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: 226.45  E-value: 4.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838    1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLME 80
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTK-LDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQPEELLAESMIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   81 GSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAeVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTS 160
Cdd:pfam03114  80 AGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  161 KSSGLSSSLQPagakadALREEMEEAANRVEICRDQLSADMYSFVAKEIDY-ANYFQTLIEVQAEYHRKSLTLLQAVLPQ 239
Cdd:pfam03114 159 KKKSSKAKDES------QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQ 232

                  ...
gi 530410838  240 IKA 242
Cdd:pfam03114 233 LGK 235
BAR smart00721
BAR domain;
1-242 3.36e-60

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 203.00  E-value: 3.36e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838     1 MKKQFNRMRQLANQTVGRAEKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLME 80
Cdd:smart00721   2 FKKQFNRAKQKVGEKVGKAEKTK-LDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838    81 GSAI--LGDDTLLGKMLKLCGETEDKLAQELIHFeLQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQ 158
Cdd:smart00721  81 GDDGegLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   159 TskssgLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEID-YANYFQTLIEVQAEYHRKSLTLLQAVL 237
Cdd:smart00721 160 A-----KKSKEKKKDEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQ 234

                   ....*
gi 530410838   238 PQIKA 242
Cdd:smart00721 235 QQLDK 239
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
266-441 1.62e-59

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 198.64  E-value: 1.62e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   266 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSeYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838   345 DEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEGNITEMMT 424
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 530410838   425 TvslQIVGIIEPIIQHA 441
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
20-241 4.26e-59

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: 200.55  E-value: 4.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  20 EKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLGKMLKLCG 99
Cdd:cd07620    8 DATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESFKDFDAESSIRRVLEMCC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 100 ETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGA----- 174
Cdd:cd07620   88 FMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVGehqgi 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410838 175 ----KADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIK 241
Cdd:cd07620  168 rranKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELK 238
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
271-440 1.65e-54

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


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 184.81  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 271 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQA 350
Cdd:cd00159    3 IIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 351 SNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEgniTEMMTTVSLQI 430
Cdd:cd00159   83 AKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDS---DDELLEDIKKL 159
                        170
                 ....*....|
gi 530410838 431 VGIIEPIIQH 440
Cdd:cd00159  160 NEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
270-415 3.38e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 183.13  E-value: 3.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  270 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-VVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWI 348
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530410838  349 QASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQA 415
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-414 1.52e-36

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


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 135.93  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEeHLTISGRE---IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSaDPHAIAGALK 328
Cdd:cd04404    6 FGVSLQ-FLKEKNPEqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEpVDFDQYE-DVHLPAVILK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 329 SYLRELPEPLMTFELYDEWIQASNVQEQDKkLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGP 408
Cdd:cd04404   84 TFLRELPEPLLTFDLYDDIVGFLNVDKEER-VERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162

                 ....*.
gi 530410838 409 NLLWPQ 414
Cdd:cd04404  163 NLLWAK 168
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
252-445 4.43e-33

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: 126.36  E-value: 4.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 252 SFGKPLEEHLTISGRE-IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL-----DCCVVDvqEYSADPHAIAG 325
Cdd:cd04395    1 TFGVPLDDCPPSSENPyVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELnrggfDIDLQD--PRWRDVNVVSS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 326 ALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIV 405
Cdd:cd04395   79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530410838 406 LGPNLLWPqAEGNITEMMTTVSLQiVGIIEPIIQHADWFF 445
Cdd:cd04395  159 FGPTLVRT-SDDNMETMVTHMPDQ-CKIVETLIQHYDWFF 196
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-445 6.18e-33

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: 125.59  E-value: 6.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDV-----QEYSADPHAIAGAL 327
Cdd:cd04398    1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVllispEDYESDIHSVASLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 328 KSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLG 407
Cdd:cd04398   81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530410838 408 PNLLwPQAEGNITEMmttvSLQIVgIIEPIIQHADWFF 445
Cdd:cd04398  161 PTLM-NAAPDNAADM----SFQSR-VIETLLDNAYQIF 192
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
253-444 1.31e-32

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: 124.86  E-value: 1.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTIS---GREIAfPI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGAL 327
Cdd:cd04390    3 FGQRLEDTVAYErkfGPRLV-PIlvEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 328 KSYLRELPEPLMTFELYDEWIQASNV--QEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIV 405
Cdd:cd04390   82 KLYLRELPEPVIPWAQYEDFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATV 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530410838 406 LGPNLLWPQAEGNITEMMTTVSLQIVGIIEpIIQHADWF 444
Cdd:cd04390  162 FGPNILRPKVEDPATIMEGTPQIQQLMTVM-ISKHEPLF 199
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
283-438 1.75e-32

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


Pssm-ID: 239842  Cd Length: 186  Bit Score: 124.09  E-value: 1.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 283 GMQEEGLFRVAPSASKLKKLKAALDCCV--VDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKL 360
Cdd:cd04377   30 GLYTEGIYRKSGSANKIKELRQGLDTDPdsVNLEDYPI--HVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERV 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530410838 361 QALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEGNITEMMTTVSLQiVGIIEPII 438
Cdd:cd04377  108 RALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRCPDTADPLQSLQDVSKT-TTCVETLI 184
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
271-432 8.37e-32

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


Pssm-ID: 239867  Cd Length: 192  Bit Score: 122.41  E-value: 8.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 271 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEWIQ 349
Cdd:cd04402   18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVeVDLKAEPV--LLLASVLKDFLRNIPGSLLSSDLYEEWMS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 350 ASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWP------QAEGN----- 418
Cdd:cd04402   96 ALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPpasselQNEDLkkvts 175
                        170
                 ....*....|....
gi 530410838 419 ITEMMTTVSLQIVG 432
Cdd:cd04402  176 LVQFLIENCQEIFG 189
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-445 2.68e-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: 121.08  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDV-QEYSADPHAIAGALKS 329
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDrdGEKADIsATVYPDINVITGALKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 330 YLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPN 409
Cdd:cd04372   81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530410838 410 LLWPqAEGNITEMMTTVSLQIVgIIEPIIQHADWFF 445
Cdd:cd04372  161 LMRP-PEDSALTTLNDMRYQIL-IVQLLITNEDVLF 194
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
272-440 7.28e-31

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: 120.19  E-value: 7.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL------DCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYD 345
Cdd:cd04374   32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 346 EWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEgNITEMMTT 425
Cdd:cd04374  112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEE-TVAAIMDI 190
                        170
                 ....*....|....*
gi 530410838 426 VSLQIVgiIEPIIQH 440
Cdd:cd04374  191 KFQNIV--VEILIEN 203
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
283-422 2.74e-30

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: 117.79  E-value: 2.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 283 GMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQA 362
Cdd:cd04407   30 GLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQA 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410838 363 LWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL-WPQAEGNITEM 422
Cdd:cd04407  110 IYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLrCPDSSDPLTSM 170
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
272-434 2.87e-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: 112.10  E-value: 2.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKaaldcCVVDVQEYSA-------DPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:cd04403   20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLR-----FAVDHDEKLDlddskweDIHVITGALKLFFRELPEPLFPYSLF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 345 DEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAE-GNITEMM 423
Cdd:cd04403   95 NDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQEtGNIAVHM 174
                        170
                 ....*....|.
gi 530410838 424 TTVSlQIVGII 434
Cdd:cd04403  175 VYQN-QIVELI 184
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
253-410 5.21e-28

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: 111.30  E-value: 5.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTIS-----GREIAFPIEACVTMLLECG-MQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSA--DPHAI 323
Cdd:cd04400    2 FGSPLEEAVELSshkynGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYdVDLFSSSLypDVHTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 324 AGALKSYLRELPEPLMTFELYDEWIQASNVQEQD-KKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNM 402
Cdd:cd04400   82 AGLLKLYLRELPTLILGGELHNDFKRLVEENHDRsQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNV 161

                 ....*...
gi 530410838 403 AIVLGPNL 410
Cdd:cd04400  162 CIVFSPTL 169
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-439 8.20e-28

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


Pssm-ID: 239838  Cd Length: 185  Bit Score: 110.62  E-value: 8.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEhLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYSADPHAIAGALKSYL 331
Cdd:cd04373    1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQdHNLDLVSKDFTVNAVAGALKSFF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 332 RELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 411
Cdd:cd04373   80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLM 159
                        170       180
                 ....*....|....*....|....*...
gi 530410838 412 WPQAEgNITEMMTTVSLQIvgIIEPIIQ 439
Cdd:cd04373  160 RPDFT-SMEALSATRIYQT--IIETFIQ 184
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-440 1.19e-27

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: 110.67  E-value: 1.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 251 PSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEeGLFRVAPSASKLKKLKAALD---CCVVDVQEYSADPHAIAGAL 327
Cdd:cd04384    1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDseqIPDLTKDVYIQDIHSVSSLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 328 KSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLG 407
Cdd:cd04384   80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530410838 408 PNLLWPQ----AEGNITEMMTTVSLQIVgIIEPIIQH 440
Cdd:cd04384  160 PNLLRSKqiesACFSGTAAFMEVRIQSV-VVEFILNH 195
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
267-413 8.77e-26

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


Pssm-ID: 239843  Cd Length: 203  Bit Score: 105.58  E-value: 8.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 267 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC--CVVDVQEYSadPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:cd04378   15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENgkDLVELSELS--PHDISSVLKLFLRQLPEPLILFRLY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 345 DEWIQAS----NVQEQDKK----------LQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNL 410
Cdd:cd04378   93 NDFIALAkeiqRDTEEDKApntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTL 172

                 ...
gi 530410838 411 LWP 413
Cdd:cd04378  173 IRP 175
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
272-440 1.29e-25

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


Pssm-ID: 239850  Cd Length: 184  Bit Score: 104.31  E-value: 1.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQ----EYSadPHAIAGALKSYLRELPEPLMTFELYDEW 347
Cdd:cd04385   19 VDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQlregEYT--VHDVADVLKRFLRDLPDPLLTSELHAEW 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 348 IQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQaegnitEMMTTVS 427
Cdd:cd04385   97 IEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTD------EHSVGQT 170
                        170
                 ....*....|...
gi 530410838 428 LQIVGIIEPIIQH 440
Cdd:cd04385  171 SHEVKVIEDLIDN 183
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
261-413 1.49e-25

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: 104.62  E-value: 1.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 261 LTISGRE---IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEY--SADPHAIAGALKSYLRELP 335
Cdd:cd04387    6 STVTKRErskVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMlsEMDVNAIAGTLKLYFRELP 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530410838 336 EPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWP 413
Cdd:cd04387   86 EPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRP 163
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-411 6.73e-25

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


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 102.94  E-value: 6.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLE----EHLTISGREIAFPIEACVTmlLECGMQEEGLFRVAPSASKLKKLKAALD---CCVvdvqeYSADPHAIAG 325
Cdd:cd04394    2 FGVPLHslphSTVPEYGNVPKFLVDACTF--LLDHLSTEGLFRKSGSVVRQKELKAKLEggeACL-----SSALPCDVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 326 ALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIV 405
Cdd:cd04394   75 LLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVI 154

                 ....*.
gi 530410838 406 LGPNLL 411
Cdd:cd04394  155 FAPNLF 160
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
272-449 9.89e-24

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


Pssm-ID: 239841  Cd Length: 206  Bit Score: 99.82  E-value: 9.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 272 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQAS 351
Cdd:cd04376   13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFIGTA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 352 --NVQEQDKKLQALWNAcekLPKANHNNIRYLIKFLSKLSEY-QDV----------NKMTPSNMAIVLGPNLLWPQAEGN 418
Cdd:cd04376   93 llEPDEQLEALQLLIYL---LPPCNCDTLHRLLKFLHTVAEHaADSidedgqevsgNKMTSLNLATIFGPNLLHKQKSGE 169
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530410838 419 ITEMMTTVSLQ----IVGIIEPIIQHADWFF--PGEI 449
Cdd:cd04376  170 REFVQASLRIEestaIINVVQTMIDNYEELFmvSPEL 206
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-411 5.05e-23

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


Pssm-ID: 239848  Cd Length: 188  Bit Score: 97.11  E-value: 5.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL---DCCVVDVQEYSaDPHAIAGALKS 329
Cdd:cd04383    3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFergEDPLADDQNDH-DINSVAGVLKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 330 YLRELPEPLMTFELYD---EWIQASNVQEQDKKLQALwnaCEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVL 406
Cdd:cd04383   82 YFRGLENPLFPKERFEdlmSCVKLENPTERVHQIREI---LSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICF 158

                 ....*
gi 530410838 407 GPNLL 411
Cdd:cd04383  159 GPTLM 163
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-418 1.90e-22

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: 96.28  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLE---------EHLTISGREIAFP--IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSAD-P 320
Cdd:cd04397    1 FGVPLEilvekfgadSTLGVGPGKLRIPalIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 321 HAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDV-----N 395
Cdd:cd04397   81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgS 160
                        170       180
                 ....*....|....*....|...
gi 530410838 396 KMTPSNMAIVLGPNLLWPQAEGN 418
Cdd:cd04397  161 KMDIHNLATVITPNILYSKTDNP 183
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
279-418 2.28e-22

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


Pssm-ID: 239856  Cd Length: 216  Bit Score: 95.88  E-value: 2.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 279 LLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQ 356
Cdd:cd04391   33 LEERGLETEGILRIPGSAQRVKFLCQELEakFYEGTFLWDQVKQHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSK 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410838 357 DKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEGN 418
Cdd:cd04391  113 KDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMIMAPNLFPPRGKHS 174
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-411 4.20e-22

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


Pssm-ID: 239871  Cd Length: 186  Bit Score: 94.30  E-value: 4.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEhLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLR 332
Cdd:cd04406    1 FGVELSR-LTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530410838 333 ELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 411
Cdd:cd04406   80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-414 1.20e-21

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


Pssm-ID: 239874  Cd Length: 211  Bit Score: 93.72  E-value: 1.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC--VVDVQEYSadPHAIAGALKSY 330
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGkdLVELSELS--PHDISNVLKLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 331 LRELPEPLMTFELYDEWI----QASNVQEQD---KKLQALW-NAC--------------EKLPKANHNNIRYLIKFLSKL 388
Cdd:cd04409   79 LRQLPEPLILFRLYNEFIglakESQHVNETQeakKNSDKKWpNMCtelnrillkskdllRQLPAPNYNTLQFLIVHLHRV 158
                        170       180
                 ....*....|....*....|....*.
gi 530410838 389 SEYQDVNKMTPSNMAIVLGPNLLWPQ 414
Cdd:cd04409  159 SEQAEENKMSASNLGIIFGPTLIRPR 184
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
251-410 4.63e-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: 4.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 251 PSFGKPLEE--HLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALK 328
Cdd:cd04393    1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 329 SYLRELPEPLMTFELYDEWIQ----ASNVQEQDKKLQALwnaCEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAI 404
Cdd:cd04393   81 LFLQELPEGLIPASLQIRLMQlyqdYNGEDEFGRKLRDL---LQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAA 157

                 ....*.
gi 530410838 405 VLGPNL 410
Cdd:cd04393  158 VFGPDV 163
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
267-420 1.16e-20

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


Pssm-ID: 239873  Cd Length: 200  Bit Score: 90.65  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 267 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC--CVVDVQEYSadPHAIAGALKSYLRELPEPLMTFELY 344
Cdd:cd04408   15 EVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENgrDLVDLSGHS--PHDITSVLKHFLKELPEPVLPFQLY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 345 DEWIQ-ASNVQEQDKK-----------LQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLW 412
Cdd:cd04408   93 DDFIAlAKELQRDSEKaaespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLR 172

                 ....*...
gi 530410838 413 PQAEGNIT 420
Cdd:cd04408  173 PLVGGDVS 180
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
275-410 1.10e-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: 87.73  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 275 CVTMLLECGMQEEGLFRVAPSASKLKKL-------KAALDCCVVDVqeysadpHAIAGALKSYLRELPEPLMTFELYDEW 347
Cdd:cd04382   24 CVNEIEARGLTEEGLYRVSGSEREVKALkekflrgKTVPNLSKVDI-------HVICGCLKDFLRSLKEPLITFALWKEF 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530410838 348 IQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEyQDVNKMTPSNMAIVLGPNL 410
Cdd:cd04382   97 MEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTI 158
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-410 1.16e-19

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


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 87.11  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTIS----GREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYsaDPHAIAGAL 327
Cdd:cd04381    1 FGASLSLAVERSrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRrESPNLEEY--EPPTVASLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 328 KSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLG 407
Cdd:cd04381   79 KQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLS 158

                 ...
gi 530410838 408 PNL 410
Cdd:cd04381  159 PTV 161
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
37-239 1.51e-19

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: 87.11  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  37 ELVKQVSHSTHKKLTACLQGQQGAEAdkrskklplttLAQCLMEGSAILGD--DTLLGKMLKLCGETEDKLAQELIHFEL 114
Cdd:cd07307    7 KLLKKLIKDTKKLLDSLKELPAAAEK-----------LSEALQELGKELPDlsNTDLGEALEKFGKIQKELEEFRDQLEQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 115 QVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAgakadalREEMEEAANRVEICR 194
Cdd:cd07307   76 KLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLAEA-------EEELQEAKEKYEELR 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530410838 195 DQLSADMYSFVA-KEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQ 239
Cdd:cd07307  149 EELIEDLNKLEEkRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
253-416 1.73e-18

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: 84.44  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEE--HLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL--DCCVVDVQEYS-ADPHAIAGAL 327
Cdd:cd04379    1 FGVPLSRlvEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFerNSAAVELSEELyPDINVITGVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 328 KSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNA---CEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAI 404
Cdd:cd04379   81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTlsiIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                        170
                 ....*....|..
gi 530410838 405 VLGPNLLWPQAE 416
Cdd:cd04379  161 CFGPVLMFCSQE 172
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
283-416 2.05e-18

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: 83.59  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 283 GMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSaDPHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLqa 362
Cdd:cd04389   37 GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGLE-DPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKAVEI-- 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530410838 363 lwnaCEKLPKANHNNIRYLIKFLSKLSEYQDV--NKMTPSNMAIVLGPNLLWPQAE 416
Cdd:cd04389  114 ----VQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNILRCTSD 165
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
249-410 1.37e-17

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: 82.08  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 249 EKPSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDVQEYSAdpHAIAGA 326
Cdd:cd04375    1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIEssTDNVNYDGQQA--YDVADM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 327 LKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVL 406
Cdd:cd04375   79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCL 158

                 ....
gi 530410838 407 GPNL 410
Cdd:cd04375  159 APSL 162
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
253-431 2.63e-17

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


Pssm-ID: 239857  Cd Length: 208  Bit Score: 80.97  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPL--EEHLTISgREIAFpieacvtmlLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYSADPHAIAGALKS 329
Cdd:cd04392    1 FGAPLteEGIAQIY-QLIEY---------LEKNLRVEGLFRKPGNSARQQELRDLLNSgTDLDLESGGFHAHDCATVLKG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 330 YLRELPEPLMTFELY------------DEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKM 397
Cdd:cd04392   71 FLGELPEPLLTHAHYpahlqiadlcqfDEKGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKM 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530410838 398 TPSNMAIVLGPNLLWP------QAEGNITEMMTTVSLQIV 431
Cdd:cd04392  151 SADNLALLFTPHLICPrnltpeDLHENAQKLNSIVTFMIK 190
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
253-444 4.11e-12

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 66.28  E-value: 4.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 253 FGKPLEEHLTISGREIAF-------------PI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-----VVD 312
Cdd:cd04396    2 FGVSLEESLKYASVAISIvdedgeqyvygyiPVvvAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdygkSFD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 313 VQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEW-----------------IQASNVQEQDKKLQALWNACEKLPKANH 375
Cdd:cd04396   82 WDGYTV--HDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkgrINEPLNTDIDQAIKEYRDLITRLPNLNR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 376 NNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLW-PQAEGNITEMMTTVSlqivgIIEPIIQHADWF 444
Cdd:cd04396  160 QLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILShPDHEMDPKEYKLSRL-----VVEFLIEHQDKF 224
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
20-236 6.24e-11

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: 62.71  E-value: 6.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  20 EKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEA-------------DKRSKKLPLTT--LAQCLMEGSAI 84
Cdd:cd07592    1 EGTK-LDDEFLEMERKTDATSKLVEDLIPKTKEYLQPNPAARAklamqntyskirgQAKSTKYPQPEglLGEVMLKYGRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  85 LGDDTLLGKMLKLCGETEDKLAQelIHFELQ--VERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqtsks 162
Cdd:cd07592   80 LGEDSNFGQALVEVGEALKQLAE--VKDSLDdnVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYDYKKRK------- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410838 163 sglssslqpaGAKA--DALREEMEEAANRVEICrdqlSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAV 236
Cdd:cd07592  151 ----------QGKGpdEELKQAEEKFEESKELA----ENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEEL 212
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
279-411 7.50e-11

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


Pssm-ID: 239845  Cd Length: 220  Bit Score: 62.36  E-value: 7.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 279 LLECGMQEEGLFR----VAPSASKLKKLKAALDCCVVDVQeySADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQ 354
Cdd:cd04380   61 LYTRGLAQEGLFEepglPSEPGELLAEIRDALDTGSPFNS--PGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANN 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410838 355 EQDKKlQALWNAcekLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 411
Cdd:cd04380  139 EEDKR-QVIRIS---LPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLL 191
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
10-240 1.42e-10

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


Pssm-ID: 153278  Cd Length: 229  Bit Score: 62.02  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  10 QLANQTVGRAEKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADK-------RSKKLPLT---TLAQCLM 79
Cdd:cd07594    1 QFTEEKLGTAEKTE-YDAHFENLLQRADKTKVWTEKILKQTEAVLQPNPNVRVEDfiyekldRKKPDRLSnleQLGQAMI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  80 EGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQT 159
Cdd:cd07594   80 EAGNDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACKTRVKKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 160 SKSSGLSsslqpagaKADA-LREEMEEAANRVEICRDQLSADMYSFvakeidyANYFQTL---IEVQAEYHRKSLTLLQA 235
Cdd:cd07594  160 KSAEAIE--------QAEQdLRVAQSEFDRQAEITKLLLEGISSTH-------ANHLRCLrdfVEAQMTYYAQCYQYMDD 224

                 ....*
gi 530410838 236 VLPQI 240
Cdd:cd07594  225 LQRQL 229
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
25-234 1.09e-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: 59.26  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  25 LSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEA-------------DKRSKKLPLTT--LAQCLMEGSAILGDDT 89
Cdd:cd07615    5 LDDDFQEMERKIDVTNKVVAELLSKTTEYLQPNPAYRAklgmlntvskirgQVKTTGYPQTEglLGDCMLRYGRELGEES 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  90 LLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqtskssglsssl 169
Cdd:cd07615   85 TFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFDYKKKR-------------- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530410838 170 qpAGAKADalrEEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQ 234
Cdd:cd07615  151 --QGKIPD---EEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILE 210
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
70-241 1.05e-07

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


Pssm-ID: 153298  Cd Length: 223  Bit Score: 53.18  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  70 PLTTLAQCLMEGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDM 149
Cdd:cd07614   65 SEGLLGETMIRYGKELGDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDF 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 150 DSSRTRwqqtskssglssslqpAGAKADalrEEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKS 229
Cdd:cd07614  145 DYKKKR----------------QGKIPD---EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQA 205
                        170
                 ....*....|..
gi 530410838 230 LTLLQAVLPQIK 241
Cdd:cd07614  206 VQILDELAEKLK 217
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
72-241 1.17e-07

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: 53.08  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  72 TTLAQCLMEGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDS 151
Cdd:cd07613   67 ALLAEAMLKFGRELGDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 152 SRTRwqqtskssglssslqpAGAKADalrEEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLT 231
Cdd:cd07613  147 KKKR----------------QGKIPD---EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQ 207
                        170
                 ....*....|
gi 530410838 232 LLQAVLPQIK 241
Cdd:cd07613  208 ILQQVTVKLE 217
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
283-411 1.19e-07

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 52.57  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 283 GMQEEGLFRvAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQ-ASNVQEQDKKLQ 361
Cdd:cd04388   30 GLESSTLYR-TQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMISrAQEVQSSDEYAQ 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530410838 362 ALWNA--CEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 411
Cdd:cd04388  109 LLRKLirSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
10-224 6.74e-06

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


Pssm-ID: 153300  Cd Length: 229  Bit Score: 48.15  E-value: 6.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  10 QLANQTVGRAEKTEvLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEAD-----KRSKKLPL-----TTLAQCLM 79
Cdd:cd07616    1 QFTEEKFGQAEKTE-LDAHLENLLSKAECTKHWTEKIMKQTEVLLQPNPNARIEefvyeKLDRKAPSrmnnpELLGQYMI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  80 EGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQT 159
Cdd:cd07616   80 DAGNEFGPGTAYGNALIKCGETQKQIGTADRELIQTSAINFLTPLRNFIEGDYKTITKERKLLQNKRLDLDAAKTRLKKA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410838 160 SKSSGLSSSLQpagakadALREEMEEAANRVEICR---DQLSAD-------MYSFVAKEIDY-ANYFQTLIEVQAE 224
Cdd:cd07616  160 KVAEARAAAEQ-------ELRITQSEFDRQAEITRlllEGISSThahhlrcLNDFVEAQMTYyAQCYQYMLDLQKQ 228
BAR_Endophilin_B2 cd07617
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid ...
10-159 2.46e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes.


Pssm-ID: 153301  Cd Length: 220  Bit Score: 43.09  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  10 QLANQTVGRAEKTEVLS--EDLLqveKRLELVKQVSHSTHKKLTACLQGQQGAEAD-----KRSKKLP--LTT---LAQC 77
Cdd:cd07617    1 QFTEEKLGQAEKTELDAhfENLL---ARADSTKNWTEKILRQTEVLLQPNPSARVEeflyeKLDRKVPsrVTNaelLGQY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  78 LMEGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQ 157
Cdd:cd07617   78 MTEAANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLK 157

                 ..
gi 530410838 158 QT 159
Cdd:cd07617  158 KA 159
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
471-686 7.47e-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: 43.22  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  471 SMPSP-----DMDPADRRQPEQARRPLSvatdnmmlefykkdgTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQ 545
Cdd:pfam03154 147 SIPSPqdnesDSDSSAQQQILQTQPPVL---------------QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  546 PGASPSPSQPPADQSPHTLRKVSKKLApiPPKVPfgQPGAMADQSAGQPSPVSLSPTPPSTPSPYGLSYPQGYSLASGQL 625
Cdd:pfam03154 212 PATSQPPNQTQSTAAPHTLIQQTPTLH--PQRLP--SPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS 287
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410838  626 SPAAAPPLASPSVfTSTLSKSRPTPKPRQRPTLPPPQPPTVNLSASSPQSTEAPMLDGMSP 686
Cdd:pfam03154 288 HMQHPVPPQPFPL-TPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP 347
PHA03378 PHA03378
EBNA-3B; Provisional
434-596 1.30e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.36  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 434 IEPIIQHADWFFPGEIEFNitgnygsPVHVNHNANY----------------SSMPSPDMDPADRRQPEQA--RRPLSVA 495
Cdd:PHA03378 657 VEITPYKPTWTQIGHIPYQ-------PSPTGANTMLpiqwapgtmqppprapTPMRPPAAPPGRAQRPAAAtgRARPPAA 729
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 496 TDNMMLEFYKKDGTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQPGASPSPSQPPadqsphtlrkvskKLAPIP 575
Cdd:PHA03378 730 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRP-------------RGAPTP 796
                        170       180
                 ....*....|....*....|....
gi 530410838 576 PKVPFGQPGAM---ADQSAGQPSP 596
Cdd:PHA03378 797 QPPPQAGPTSMqlmPRAAPGQQGP 820
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
37-240 1.44e-03

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: 40.80  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  37 ELVKQVSHSTHKKLTACLQGQQGAEADK------RSKKLPlTTLAQCL----MEGSAILG-----DDTLLGKMLKLCGET 101
Cdd:cd07600   37 ESISDFSKTIGSKVSELSKATSPTEAQKvllgtpAPAKLP-KTLNHALsraaLASSLELKslepeDEDPLSKALGKYSDA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 102 EDKLAQelihfeLQVERD------VIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSkssglssslqpAGAK 175
Cdd:cd07600  116 EEKIAE------ARLEQDqliqkeFNAKLRETLNTSFQKAHKARKKVEDKRLQLDTARAELKSAE-----------PAEK 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530410838 176 ADALREEMEEAanrvEICRDQLSADMYSFVAKEIDYANY---FQTLIEVQAEYHRKSLTLLQAVLPQI 240
Cdd:cd07600  179 QEAARVEVETA----EDEFVSATEEAVELMKEVLDNPEPlqlLKELVKAQLAYHKTAAELLEELLSVL 242
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
469-580 3.90e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 469 YSSMPSPDMDPADRRQPEQARRPlsvatdnmmlefykKDGTTKSKELSPgsaqkGSPGSSQGTACAGTQPGAQPGAQPGA 548
Cdd:PTZ00449 575 LSKKPEFPKDPKHPKDPEEPKKP--------------KRPRSAQRPTRP-----KSPKLPELLDIPKSPKRPESPKSPKR 635
                         90       100       110
                 ....*....|....*....|....*....|..
gi 530410838 549 SPSPSQPPADQSPHTLRKVSKKLAPIPPKVPF 580
Cdd:PTZ00449 636 PPPPQRPSSPERPEGPKIIKSPKPPKSPKPPF 667
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
74-245 7.45e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153274  Cd Length: 225  Bit Score: 38.50  E-value: 7.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838  74 LAQCLMEGSAILGDDTLLGKMLKLCGETE--DKLAQELIHfelQVERDVIEPLFLLAEV--EIPN-IQKQRKHLAKLvld 148
Cdd:cd07590   51 LSQDLASGPLCEDNDELRNLVEALDSVTTqlDKTVQELVN---LIQKTFIEPLKRLRSVfpSVNAaIKRREQSLQEY--- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410838 149 mdssrTRWQQTSKSSGLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYAN-YFQTLIEVQAEYHR 227
Cdd:cd07590  125 -----ERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQpCFEALIKSQVLYYS 199
                        170
                 ....*....|....*...
gi 530410838 228 KSLTLLQAVLPQIKAQQE 245
Cdd:cd07590  200 QSTKIFTQLAPNLDNPIE 217
 
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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