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Conserved domains on  [gi|2360770259|emb|CAI4441993|]
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ADE_G0016410.mRNA.1.CDS.1 [Saccharomyces cerevisiae]

Protein Classification

BAR domain-containing protein( domain architecture ID 10637163)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 473-708 1.13e-111

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


:

Pssm-ID: 239864  Cd Length: 212  Bit Score: 336.23  E-value: 1.13e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 473 FGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIfdilSTSKL 552
Cdd:cd04399     1 FGVDLETRCRLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVWTDPVSLKETHQLRNLLNKPKKPDKEVI----ILKKF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 553 EPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETalqnstsspenqqdddneegFDTKRIRGLYTTLSSLSK 632
Cdd:cd04399    77 EPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPSQED--------------------SDTARIQGLQSTLSQLPK 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2360770259 633 PHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELK 708
Cdd:cd04399   137 SHIATLDAIITHFYRLIEITKMGESEEEYADKLATSLSREILRPIIESLLTIGDKHGYKFFRDLLTHKDQIFSELK 212
DEP_fRgd2 cd04436
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator ...
 205-289 8.88e-43

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator protein) Rgd2-like proteins. Rgd2-like proteins share a common domain architecture, containing, beside the RhoGAP domain, a DEP and a FCH (Fes/CIP4 homology) domain. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5.


:

Pssm-ID: 239883  Cd Length: 84  Bit Score: 149.41  E-value: 8.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 205 TMKETLQLLLTKLPKTDYKLPLISYSLsNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKK 284
Cdd:cd04436     1 SLKELLAAMLKEIPLADYKVPILGTYQ-NTSSGSEIVSWLQENMPEKDLDAAEAFGQDLLNQGFLRLVGGVGSTFVNSSK 79


                  ....*
gi 2360770259 285 FQYQW 289
Cdd:cd04436    80 FQYQW 84
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 6-96 8.30e-19

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


:

Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 81.62  E-value: 8.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259    6 DYFWSEdLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEagmDNLKAVQEDEDEGVTVSRALRGILQE 85
Cdd:smart00055   1 MGFWSE-LDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLS---KKLRAVRDTEPEYGSLSKAWEVLLSE 76

                           90
                   ....*....|.
gi 2360770259   86 MSQEGTHHLTI 96
Cdd:smart00055  77 TDALAKQHLEL 87
 
Name Accession Description Interval E-value
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 473-708 1.13e-111

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 336.23  E-value: 1.13e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 473 FGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIfdilSTSKL 552
Cdd:cd04399     1 FGVDLETRCRLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVWTDPVSLKETHQLRNLLNKPKKPDKEVI----ILKKF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 553 EPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETalqnstsspenqqdddneegFDTKRIRGLYTTLSSLSK 632
Cdd:cd04399    77 EPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPSQED--------------------SDTARIQGLQSTLSQLPK 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2360770259 633 PHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELK 708
Cdd:cd04399   137 SHIATLDAIITHFYRLIEITKMGESEEEYADKLATSLSREILRPIIESLLTIGDKHGYKFFRDLLTHKDQIFSELK 212
DEP_fRgd2 cd04436
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator ...
 205-289 8.88e-43

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator protein) Rgd2-like proteins. Rgd2-like proteins share a common domain architecture, containing, beside the RhoGAP domain, a DEP and a FCH (Fes/CIP4 homology) domain. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5.


Pssm-ID: 239883  Cd Length: 84  Bit Score: 149.41  E-value: 8.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 205 TMKETLQLLLTKLPKTDYKLPLISYSLsNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKK 284
Cdd:cd04436     1 SLKELLAAMLKEIPLADYKVPILGTYQ-NTSSGSEIVSWLQENMPEKDLDAAEAFGQDLLNQGFLRLVGGVGSTFVNSSK 79


                  ....*
gi 2360770259 285 FQYQW 289
Cdd:cd04436    80 FQYQW 84
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 6-96 8.30e-19

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 81.62  E-value: 8.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259    6 DYFWSEdLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEagmDNLKAVQEDEDEGVTVSRALRGILQE 85
Cdd:smart00055   1 MGFWSE-LDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLS---KKLRAVRDTEPEYGSLSKAWEVLLSE 76

                           90
                   ....*....|.
gi 2360770259   86 MSQEGTHHLTI 96
Cdd:smart00055  77 TDALAKQHLEL 87
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 486-681 1.07e-17

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: 81.16  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  486 KVVPLIISSIFSYMDKIYPDLPNdkvrtsIWTDSVKLSLTHQLRNLLNKqqfhneGEIFDILStSKLEPSTIASVVKIYL 565
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEG------IYRVSGSKSRVKELRDAFDS------GPDPDLDL-SEYDVHDVAGLLKLFL 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  566 LELPDPLIPNDVSDILRVLYldypplvetalqnstsspenqqdddnEEGFDTKRIRGLYTTLSSLSKPHIATLDAITTHF 645
Cdd:smart00324  68 RELPEPLITYELYEEFIEAA--------------------------KLEDETERLRALRELLSLLPPANRATLRYLLAHL 121

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2360770259  646 YRLIK-ILKMGENGNEVADEFTVSISQEFANCIIQSK 681
Cdd:smart00324 122 NRVAEhSEENKMTARNLAIVFGPTLLRPPDGEVASLK 158
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 16-95 7.96e-12

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 61.52  E-value: 7.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  16 GLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKavQEDEDEGVTVSRALRGILQEMSQEGTHHLT 95
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKK--KKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 218-297 6.79e-10

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 55.75  E-value: 6.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  218 PKTDYKLPLISYSLS---NTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGvgntfVNSKKFQYqwKNTAY 294
Cdd:smart00049   1 PETGLKLRDRKYFLKtypNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNG-----PNKHTFKD--SKALY 73


                   ...
gi 2360770259  295 MFA 297
Cdd:smart00049  74 RFT 76
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 217-289 1.18e-09

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 459867  Cd Length: 71  Bit Score: 54.90  E-value: 1.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2360770259 217 LPKTDYKLPLISYSlsNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSkKFQYQW 289
Cdd:pfam00610   2 VKLKDRRKHLKTYP--NCFTGSEAVDWLMDNLEIITREEAVELGQLLLDQGLIHHVGDKHGLFKDS-YYFYRF 71
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 534-650 3.20e-07

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 50.24  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 534 KQQFHNEGEIFDILSTSklEPSTIASVVKIYLLELPDPLIPNDvsdilrvlylDYPPLVETAlqnstsspenQQDDDNEe 613
Cdd:pfam00620  35 REAFDRGPDVDLDLEEE--DVHVVASLLKLFLRELPEPLLTFE----------LYEEFIEAA----------KLPDEEE- 91

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2360770259 614 gfdtkRIRGLYTTLSSLSKPHIATLDAITTHFYRLIK 650
Cdd:pfam00620  92 -----RLEALRELLRKLPPANRDTLRYLLAHLNRVAQ 123
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 16-211 2.10e-05

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 45.79  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  16 GLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIeagmdNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLT 95
Cdd:cd07610     1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKL-----AKKFSKKPESGKTSLGTSWNSLREETESAATVHEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  96 IASNIESLVLQPFskwciehRERIQYSEKTLLTNVNNFRKSKKYVSKLEKEYFNKC-----RQLEEFKRTHF-NEDELAN 169
Cdd:cd07610    76 LSEKLSQLIREPL-------EKVKEDKEQARKKELAEGEKLKKKLQELWAKLAKKAdeeyrEQVEKLNPAQSeYEEEKLN 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2360770259 170 AMKSLKIQNKYEEDVAREKDHRFFNRI-AGIDFDYKTMKETLQ 211
Cdd:cd07610   149 KIQAEQEREEERLEILKDNLKNYINAIkEIPQKIQQELEQSIN 191
 
Name Accession Description Interval E-value
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 473-708 1.13e-111

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 336.23  E-value: 1.13e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 473 FGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIfdilSTSKL 552
Cdd:cd04399     1 FGVDLETRCRLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVWTDPVSLKETHQLRNLLNKPKKPDKEVI----ILKKF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 553 EPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETalqnstsspenqqdddneegFDTKRIRGLYTTLSSLSK 632
Cdd:cd04399    77 EPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPSQED--------------------SDTARIQGLQSTLSQLPK 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2360770259 633 PHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELK 708
Cdd:cd04399   137 SHIATLDAIITHFYRLIEITKMGESEEEYADKLATSLSREILRPIIESLLTIGDKHGYKFFRDLLTHKDQIFSELK 212
DEP_fRgd2 cd04436
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator ...
 205-289 8.88e-43

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator protein) Rgd2-like proteins. Rgd2-like proteins share a common domain architecture, containing, beside the RhoGAP domain, a DEP and a FCH (Fes/CIP4 homology) domain. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5.


Pssm-ID: 239883  Cd Length: 84  Bit Score: 149.41  E-value: 8.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 205 TMKETLQLLLTKLPKTDYKLPLISYSLsNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKK 284
Cdd:cd04436     1 SLKELLAAMLKEIPLADYKVPILGTYQ-NTSSGSEIVSWLQENMPEKDLDAAEAFGQDLLNQGFLRLVGGVGSTFVNSSK 79


                  ....*
gi 2360770259 285 FQYQW 289
Cdd:cd04436    80 FQYQW 84
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 6-96 8.30e-19

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 81.62  E-value: 8.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259    6 DYFWSEdLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEagmDNLKAVQEDEDEGVTVSRALRGILQE 85
Cdd:smart00055   1 MGFWSE-LDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLS---KKLRAVRDTEPEYGSLSKAWEVLLSE 76

                           90
                   ....*....|.
gi 2360770259   86 MSQEGTHHLTI 96
Cdd:smart00055  77 TDALAKQHLEL 87
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 486-681 1.07e-17

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: 81.16  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  486 KVVPLIISSIFSYMDKIYPDLPNdkvrtsIWTDSVKLSLTHQLRNLLNKqqfhneGEIFDILStSKLEPSTIASVVKIYL 565
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEG------IYRVSGSKSRVKELRDAFDS------GPDPDLDL-SEYDVHDVAGLLKLFL 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  566 LELPDPLIPNDVSDILRVLYldypplvetalqnstsspenqqdddnEEGFDTKRIRGLYTTLSSLSKPHIATLDAITTHF 645
Cdd:smart00324  68 RELPEPLITYELYEEFIEAA--------------------------KLEDETERLRALRELLSLLPPANRATLRYLLAHL 121

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2360770259  646 YRLIK-ILKMGENGNEVADEFTVSISQEFANCIIQSK 681
Cdd:smart00324 122 NRVAEhSEENKMTARNLAIVFGPTLLRPPDGEVASLK 158
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 16-95 7.96e-12

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 61.52  E-value: 7.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  16 GLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKavQEDEDEGVTVSRALRGILQEMSQEGTHHLT 95
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKK--KKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 489-699 2.65e-10

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: 59.62  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 489 PLIISSIFSYMDKIYPDLPnDKVRTSIWTDSVKlslthQLRNLLNKQQFHNEGEIFDilstsklePSTIASVVKIYLLEL 568
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTE-GIFRVSGSASKIE-----ELKKKFDRGEDIDDLEDYD--------VHDVASLLKLYLREL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 569 PDPLIPNDVSDILRVLYLDYPPlvetalqnstsspenqqdddneegfdTKRIRGLYTTLSSLSKPHIATLDAITTHFYRL 648
Cdd:cd00159    67 PEPLIPFELYDEFIELAKIEDE--------------------------EERIEALKELLKSLPPENRDLLKYLLKLLHKI 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2360770259 649 IK---ILKMGENgnevadeftvSISQEFANCIIQSKITDDNEI-----GFKIFYDLLTH 699
Cdd:cd00159   121 SQnseVNKMTAS----------NLAIVFAPTLLRPPDSDDELLedikkLNEIVEFLIEN 169
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 218-297 6.79e-10

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 55.75  E-value: 6.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  218 PKTDYKLPLISYSLS---NTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGvgntfVNSKKFQYqwKNTAY 294
Cdd:smart00049   1 PETGLKLRDRKYFLKtypNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNG-----PNKHTFKD--SKALY 73


                   ...
gi 2360770259  295 MFA 297
Cdd:smart00049  74 RFT 76
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 217-289 1.18e-09

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 459867  Cd Length: 71  Bit Score: 54.90  E-value: 1.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2360770259 217 LPKTDYKLPLISYSlsNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSkKFQYQW 289
Cdd:pfam00610   2 VKLKDRRKHLKTYP--NCFTGSEAVDWLMDNLEIITREEAVELGQLLLDQGLIHHVGDKHGLFKDS-YYFYRF 71
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 205-288 2.88e-09

DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first discovered. The function of this domain is still not clear, but it is believed to be important for the membrane association of the signaling proteins in which it is present. New studies show that the DEP domain of Sst2, a yeast RGS protein is necessary and sufficient for receptor interaction.


Pssm-ID: 239836  Cd Length: 81  Bit Score: 54.27  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 205 TMKETLQLLLTKLPKTDYKLPLISYSlsNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKK 284
Cdd:cd04371     1 DLVRIMLDSDSGVPIKDRKYHLKTYP--NCFTGSELVDWLLDNLEAITREEAVELGQALLKHGLIHHVSDDKHTFRDSYA 78


                  ....
gi 2360770259 285 FqYQ 288
Cdd:cd04371    79 L-YR 81
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 534-650 3.20e-07

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 50.24  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 534 KQQFHNEGEIFDILSTSklEPSTIASVVKIYLLELPDPLIPNDvsdilrvlylDYPPLVETAlqnstsspenQQDDDNEe 613
Cdd:pfam00620  35 REAFDRGPDVDLDLEEE--DVHVVASLLKLFLRELPEPLLTFE----------LYEEFIEAA----------KLPDEEE- 91

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2360770259 614 gfdtkRIRGLYTTLSSLSKPHIATLDAITTHFYRLIK 650
Cdd:pfam00620  92 -----RLEALRELLRKLPPANRDTLRYLLAHLNRVAQ 123
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 535-647 1.40e-06

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: 49.73  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 535 QQFHNEGEIFDIlstSKLEPSTIASVVKIYLLELPDPLIPNDvsdilrvLYLDYPPLVETaLQNSTSspenQQDDDNEEG 614
Cdd:cd04378    52 QAFENGKDLVEL---SELSPHDISSVLKLFLRQLPEPLILFR-------LYNDFIALAKE-IQRDTE----EDKAPNTPI 116

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2360770259 615 FDTKRIRGLYTTLSSLSKPHIATLDAITTHFYR 647
Cdd:cd04378   117 EVNRIIRKLKDLLRQLPASNYNTLQHLIAHLYR 149
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 535-648 1.34e-05

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: 46.73  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 535 QQFHNEGEIFDIlstSKLEPSTIASVVKIYLLELPDPLIPNDvsdilrvLYLDYPPLVETALQNSTSSPEnqqdddnEEG 614
Cdd:cd04408    52 QAFENGRDLVDL---SGHSPHDITSVLKHFLKELPEPVLPFQ-------LYDDFIALAKELQRDSEKAAE-------SPS 114

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2360770259 615 FDTKRIRGLYTTLSSLSKPHIATLDAITTHFYRL 648
Cdd:cd04408   115 IVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRV 148
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 16-211 2.10e-05

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 45.79  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  16 GLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIeagmdNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLT 95
Cdd:cd07610     1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKL-----AKKFSKKPESGKTSLGTSWNSLREETESAATVHEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  96 IASNIESLVLQPFskwciehRERIQYSEKTLLTNVNNFRKSKKYVSKLEKEYFNKC-----RQLEEFKRTHF-NEDELAN 169
Cdd:cd07610    76 LSEKLSQLIREPL-------EKVKEDKEQARKKELAEGEKLKKKLQELWAKLAKKAdeeyrEQVEKLNPAQSeYEEEKLN 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2360770259 170 AMKSLKIQNKYEEDVAREKDHRFFNRI-AGIDFDYKTMKETLQ 211
Cdd:cd07610   149 KIQAEQEREEERLEILKDNLKNYINAIkEIPQKIQQELEQSIN 191
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-200 1.26e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 44.18  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  15 SGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGI--EAGmdnlkavqeDEDEGVTVSRALRGILQEMSQEGTH 92
Cdd:cd07671     5 TGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIarKAG---------GQTEINTLKASFDQLKQQIENIGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  93 HLTIAsniesLVLQPFSKWCIEHRERIQYSEKTLLTNVNNFRKSK----KYVSKLEKEYFNKCRQLEEFKRTHFNEDELA 168
Cdd:cd07671    76 HIQLA-----GMLREELKSLEEFRERQKEQRKKYEAVMERVQKSKvslyKKTMESKKTYEQRCREADEAEQTFERSSSTG 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2360770259 169 NAMKSLKIQNKYEE--DVAREKDHRFFNRIAGID 200
Cdd:cd07671   151 NPKQSEKSQNKAKQcrDAATEAERVYKQNIEQLD 184
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 27-165 2.54e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153360 [Multi-domain]  Cd Length: 253  Bit Score: 43.50  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259  27 GCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLTIASNIESLVLQ 106
Cdd:cd07676    17 GIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYAGQHEVISENLASQIIV 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 107 PFSKWCIEHRERiqysektlltnvnnfRKSKKYVSKLEKEYFNKC-RQLEEFKRtHFNED 165
Cdd:cd07676    97 ELTRYVQELKQE---------------RKSHFHDGRKAQQHIETCwKQLESSKR-RFERD 140
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 473-685 3.33e-04

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: 42.04  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 473 FGVDLeTRCRLDKKVVPLIISSIFSY--MDKIYPDlpndkvrtSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIFDIlsts 550
Cdd:cd04377     1 FGVSL-SSLTSEDRSVPLVLEKLLEHieMHGLYTE--------GIYRKSGSANKIKELRQGLDTDPDSVNLEDYPI---- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 551 klepSTIASVVKIYLLELPDPLIPNDV-SDILRVLYLdypplvetalqnstssPENQQdddneegfdtkRIRGLYTTLSS 629
Cdd:cd04377    68 ----HVITSVLKQWLRELPEPLMTFELyENFLRAMEL----------------EEKQE-----------RVRALYSVLEQ 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2360770259 630 LSKPHIATLDAITTHFYRLI---KILKMGENgnevadeftvSISQEFANCIIQSKITDD 685
Cdd:cd04377   117 LPRANLNTLERLIFHLVRVAlqeEVNRMSAN----------ALAIVFAPCILRCPDTAD 165
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 473-649 1.75e-03

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: 40.08  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 473 FGVDLETRCRLDKKVVPLIISSIFSYMDK-------IYPDLPN----DKVRTSIWTDSVKLSLTHQLrnllnkqqfHNEG 541
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENfglnlegIYRLSGNvsrvNKLKELFDKDPLNVLLISPE---------DYES 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 542 EIFdilstsklepsTIASVVKIYLLELPDPLIPNdvsdilrvlyldypplvetALQNSTSSPENQQDddneegfDTKRIR 621
Cdd:cd04398    72 DIH-----------SVASLLKLFFRELPEPLLTK-------------------ALSREFIEAAKIED-------ESRRRD 114

                         170       180
                  ....*....|....*....|....*...
gi 2360770259 622 GLYTTLSSLSKPHIATLDAITTHFYRLI 649
Cdd:cd04398   115 ALHGLINDLPDANYATLRALMFHLARIK 142
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 535-648 1.95e-03

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: 40.18  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360770259 535 QQFHNEGEIFDIlstSKLEPSTIASVVKIYLLELPDPLIP----NDVSDILRvlyldypplvETALQNST-SSPENQQDD 609
Cdd:cd04409    52 QAFENGKDLVEL---SELSPHDISNVLKLYLRQLPEPLILfrlyNEFIGLAK----------ESQHVNETqEAKKNSDKK 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2360770259 610 DNEEGFDTKRIR-GLYTTLSSLSKPHIATLDAITTHFYRL 648
Cdd:cd04409   119 WPNMCTELNRILlKSKDLLRQLPAPNYNTLQFLIVHLHRV 158
 
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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