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Conserved domains on  [gi|148679897|gb|EDL11844|]
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DEP domain containing 1a, isoform CRA_b [Mus musculus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10241509)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_BRCC3-like cd04405
RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 182-407 5.75e-99

RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of BRCC3-like proteins. This subgroup also contains two groups of closely related proteins, BRCC3 and DEPDC7, which both contain a C-terminal RhoGAP-like domain and an N-terminal DEP (Disheveled, Egl-10, and Pleckstrin) domain. The function(s) of BRCC3 and DEPDC7 are 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: 239870  Cd Length: 235  Bit Score: 298.86  E-value: 5.75e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 182 ISQEDVEEVWRYVIMIYLQTILSLPSIEELLNPNQVIPQYIMYNM------ANTSKHGVVILQDKSDdLPHWVLSAMKCL 255
Cdd:cd04405    1 LSPEVVEEIWKEQTLIRLLQLVGLPLLEELLDPALVNPKHISYNMdpdvytSNYLDREVVKLFSKSQ-LDHWLLSAMDCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 256 ANWPRS--NDTNNLTYV------GFERDVFKTIADYFLNLPEPLLTFEYYELFVNILGLLQPHLERVAINALQLCCLLLP 327
Cdd:cd04405   80 ANWPDQlvVDVSRPLYSqhdmlsGFKRLLFKTIAKYYGQLKEPLLTFHLFDIFVGILELLGNGKEEVALEALQLCLLLLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 328 PPNRRKLQLLMRMISRMSQNvDMPKLHEQIGTRSLMINTFSRCVLCCAeevDLDELLASRLVSFLMDHHQEILQVPTYLQ 407
Cdd:cd04405  160 PASRRELRRLLRFMARAAKN-DMPRLHKEIENRMLVKQTFSRAILCSK---DLDEGLADLLVLFLMDHHQDIFKVPGSLH 235
DEP super family cl02442
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 15-106 1.33e-58

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.


The actual alignment was detected with superfamily member cd04447:

Pssm-ID: 470580  Cd Length: 92  Bit Score: 189.29  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897  15 KLWNEVTTSFRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDLLRSNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGS 94
Cdd:cd04447    1 KLWNEVTELFRAGMPLRKHRQHFKSYENCFTASEAVDWLHELLRSNSNFGPEVTRQQTVQLLKKFLKNHVIEDIKGRWGK 80

                         90
                 ....*....|..
gi 148679897  95 ESLDDNNQLFRF 106
Cdd:cd04447   81 EDLEDNNHLYRF 92
 
Name Accession Description Interval E-value
RhoGAP_BRCC3-like cd04405
RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 182-407 5.75e-99

RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of BRCC3-like proteins. This subgroup also contains two groups of closely related proteins, BRCC3 and DEPDC7, which both contain a C-terminal RhoGAP-like domain and an N-terminal DEP (Disheveled, Egl-10, and Pleckstrin) domain. The function(s) of BRCC3 and DEPDC7 are 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: 239870  Cd Length: 235  Bit Score: 298.86  E-value: 5.75e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 182 ISQEDVEEVWRYVIMIYLQTILSLPSIEELLNPNQVIPQYIMYNM------ANTSKHGVVILQDKSDdLPHWVLSAMKCL 255
Cdd:cd04405    1 LSPEVVEEIWKEQTLIRLLQLVGLPLLEELLDPALVNPKHISYNMdpdvytSNYLDREVVKLFSKSQ-LDHWLLSAMDCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 256 ANWPRS--NDTNNLTYV------GFERDVFKTIADYFLNLPEPLLTFEYYELFVNILGLLQPHLERVAINALQLCCLLLP 327
Cdd:cd04405   80 ANWPDQlvVDVSRPLYSqhdmlsGFKRLLFKTIAKYYGQLKEPLLTFHLFDIFVGILELLGNGKEEVALEALQLCLLLLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 328 PPNRRKLQLLMRMISRMSQNvDMPKLHEQIGTRSLMINTFSRCVLCCAeevDLDELLASRLVSFLMDHHQEILQVPTYLQ 407
Cdd:cd04405  160 PASRRELRRLLRFMARAAKN-DMPRLHKEIENRMLVKQTFSRAILCSK---DLDEGLADLLVLFLMDHHQDIFKVPGSLH 235
DEP_BRCC3 cd04447
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in BBRC3-like proteins. BBRC3, also ...
 15-106 1.33e-58

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in BBRC3-like proteins. BBRC3, also known as DEPDC1B, is a DEP containing protein of unknown function.


Pssm-ID: 239894  Cd Length: 92  Bit Score: 189.29  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897  15 KLWNEVTTSFRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDLLRSNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGS 94
Cdd:cd04447    1 KLWNEVTELFRAGMPLRKHRQHFKSYENCFTASEAVDWLHELLRSNSNFGPEVTRQQTVQLLKKFLKNHVIEDIKGRWGK 80

                         90
                 ....*....|..
gi 148679897  95 ESLDDNNQLFRF 106
Cdd:cd04447   81 EDLEDNNHLYRF 92
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 27-106 2.04e-16

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: 73.78  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897   27 GMPLRKHRQHLKKYSNCFTAVEAIDWLYDLlrsnsnfGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGseSLDDNNQLFRF 106
Cdd:pfam00610   1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDN-------LEIITREEAVELGQLLLDQGLIHHVGDKHG--LFKDSYYFYRF 71
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 24-107 8.36e-15

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: 69.23  E-value: 8.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897    24 FRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDLLrsnsnfgPEVTRQQTIQLLRKFLKNHVIEDIKGrWGSESLDDNNQL 103
Cdd:smart00049   1 PETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNL-------EIIDREEAVHLGQLLLDEGLIHHVNG-PNKHTFKDSKAL 72


                   ....
gi 148679897   104 FRFP 107
Cdd:smart00049  73 YRFT 76
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 275-352 1.37e-04

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 42.15  E-value: 1.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148679897  275 DVFKtiaDYFLNLPEPLLTFEYYELFVNILGLlqpHLERVAINALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPK 352
Cdd:pfam00620  58 SLLK---LFLRELPEPLLTFELYEEFIEAAKL---PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNK 129
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 275-349 5.63e-04

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: 40.71  E-value: 5.63e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148679897   275 DVFKTiadYFLNLPEPLLTFEYYELFVNILgLLQPHLERvaINALQLCCLLLPPPNRRKLQLLMRMISRMSQNVD 349
Cdd:smart00324  61 GLLKL---FLRELPEPLITYELYEEFIEAA-KLEDETER--LRALRELLSLLPPANRATLRYLLAHLNRVAEHSE 129
 
Name Accession Description Interval E-value
RhoGAP_BRCC3-like cd04405
RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 182-407 5.75e-99

RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of BRCC3-like proteins. This subgroup also contains two groups of closely related proteins, BRCC3 and DEPDC7, which both contain a C-terminal RhoGAP-like domain and an N-terminal DEP (Disheveled, Egl-10, and Pleckstrin) domain. The function(s) of BRCC3 and DEPDC7 are 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: 239870  Cd Length: 235  Bit Score: 298.86  E-value: 5.75e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 182 ISQEDVEEVWRYVIMIYLQTILSLPSIEELLNPNQVIPQYIMYNM------ANTSKHGVVILQDKSDdLPHWVLSAMKCL 255
Cdd:cd04405    1 LSPEVVEEIWKEQTLIRLLQLVGLPLLEELLDPALVNPKHISYNMdpdvytSNYLDREVVKLFSKSQ-LDHWLLSAMDCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 256 ANWPRS--NDTNNLTYV------GFERDVFKTIADYFLNLPEPLLTFEYYELFVNILGLLQPHLERVAINALQLCCLLLP 327
Cdd:cd04405   80 ANWPDQlvVDVSRPLYSqhdmlsGFKRLLFKTIAKYYGQLKEPLLTFHLFDIFVGILELLGNGKEEVALEALQLCLLLLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 328 PPNRRKLQLLMRMISRMSQNvDMPKLHEQIGTRSLMINTFSRCVLCCAeevDLDELLASRLVSFLMDHHQEILQVPTYLQ 407
Cdd:cd04405  160 PASRRELRRLLRFMARAAKN-DMPRLHKEIENRMLVKQTFSRAILCSK---DLDEGLADLLVLFLMDHHQDIFKVPGSLH 235
DEP_BRCC3 cd04447
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in BBRC3-like proteins. BBRC3, also ...
 15-106 1.33e-58

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in BBRC3-like proteins. BBRC3, also known as DEPDC1B, is a DEP containing protein of unknown function.


Pssm-ID: 239894  Cd Length: 92  Bit Score: 189.29  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897  15 KLWNEVTTSFRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDLLRSNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGS 94
Cdd:cd04447    1 KLWNEVTELFRAGMPLRKHRQHFKSYENCFTASEAVDWLHELLRSNSNFGPEVTRQQTVQLLKKFLKNHVIEDIKGRWGK 80

                         90
                 ....*....|..
gi 148679897  95 ESLDDNNQLFRF 106
Cdd:cd04447   81 EDLEDNNHLYRF 92
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 27-106 2.04e-16

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: 73.78  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897   27 GMPLRKHRQHLKKYSNCFTAVEAIDWLYDLlrsnsnfGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGseSLDDNNQLFRF 106
Cdd:pfam00610   1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDN-------LEIITREEAVELGQLLLDQGLIHHVGDKHG--LFKDSYYFYRF 71
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 24-107 8.36e-15

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: 69.23  E-value: 8.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897    24 FRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDLLrsnsnfgPEVTRQQTIQLLRKFLKNHVIEDIKGrWGSESLDDNNQL 103
Cdd:smart00049   1 PETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNL-------EIIDREEAVHLGQLLLDEGLIHHVNG-PNKHTFKDSKAL 72


                   ....
gi 148679897   104 FRFP 107
Cdd:smart00049  73 YRFT 76
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 24-105 4.43e-14

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: 67.37  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897  24 FRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDllrsnsnFGPEVTRQQTIQLLRKFLKNHVIEDIKGrwGSESLDDNNQL 103
Cdd:cd04371    9 SDSGVPIKDRKYHLKTYPNCFTGSELVDWLLD-------NLEAITREEAVELGQALLKHGLIHHVSD--DKHTFRDSYAL 79


                 ..
gi 148679897 104 FR 105
Cdd:cd04371   80 YR 81
DEP_DEPDC4 cd04446
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC4-like proteins. DEPDC4 is a ...
 17-105 3.74e-09

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC4-like proteins. DEPDC4 is a DEP domain containing protein of unknown function.


Pssm-ID: 239893  Cd Length: 95  Bit Score: 53.91  E-value: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897  17 WNEVTTSFRVGMPLRKHRQHLKKYSNCFTAVEAIDWLYDLLRSNSNFG-PEVTRQQTIQLLRKFLKNHVIEDIKGRWGSE 95
Cdd:cd04446    1 WNSIIDALQTQVEVKKRRHNLKSYHDCFLGSEAVDVVLAHLMQNKYFGdVDVPRAKAVRLCQALMDCRVFEAVGTKVFKK 80

                         90
                 ....*....|....*
gi 148679897  96 S-----LDDNNQLFR 105
Cdd:cd04446   81 KkravfEDSSSSLYR 95
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 16-53 8.52e-06

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) PIKfyve-like proteins. PIKfyve contains N-terminal Fyve finger and DEP domains, a central chaperonin-like domain and a C-terminal PIPK (phosphatidylinositol phosphate kinase) domain. PIKfyve-like proteins are important phosphatidylinositol (3)-monophosphate (PtdIns(3)P)-5-kinases, producing PtdIns(3,5)P2, which plays a major role in multivesicular body (MVB) sorting and control of retrograde traffic from the vacuole back to the endosome and/or Golgi. PIKfyve itself has been shown to be play a role in regulating early-endosome-to-trans-Golgi network (TGN) retrograde trafficking.


Pssm-ID: 239895  Cd Length: 81  Bit Score: 43.97  E-value: 8.52e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 148679897  16 LWNEVTTSfRVGMPLRKHRQHLKKYSNCFTAVEAIDWL 53
Cdd:cd04448    2 LWEKICRS-STGIEFQDHRYRLRTYTNCILGKELVNWL 38
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 275-395 1.45e-05

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: 45.37  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 275 DVFKTIADYFLNLPEPLLTFEYYELFVNILGLLQPHlerVAINALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPKLh 354
Cdd:cd00159   54 DVASLLKLYLRELPEPLIPFELYDEFIELAKIEDEE---ERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKM- 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 148679897 355 eqiGTRSLMInTFSRCVLCCAEEVD---LDELLASRLVSFLMDH 395
Cdd:cd00159  130 ---TASNLAI-VFAPTLLRPPDSDDellEDIKKLNEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 275-352 1.37e-04

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 42.15  E-value: 1.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148679897  275 DVFKtiaDYFLNLPEPLLTFEYYELFVNILGLlqpHLERVAINALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPK 352
Cdd:pfam00620  58 SLLK---LFLRELPEPLLTFELYEEFIEAAKL---PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNK 129
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 275-349 5.63e-04

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: 40.71  E-value: 5.63e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148679897   275 DVFKTiadYFLNLPEPLLTFEYYELFVNILgLLQPHLERvaINALQLCCLLLPPPNRRKLQLLMRMISRMSQNVD 349
Cdd:smart00324  61 GLLKL---FLRELPEPLITYELYEEFIEAA-KLEDETER--LRALRELLSLLPPANRATLRYLLAHLNRVAEHSE 129
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 234-406 6.14e-04

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: 41.25  E-value: 6.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 234 VVILQDKSDDLPHWVLSAMKclanWPRSN--------------------------DTNNLTYVGFER-DVFKTIADYFLN 286
Cdd:cd04375   10 LVNLQRTGQPLPRSIQQAMR----WLRNNaldqvglfrksgvksriqklrsmiesSTDNVNYDGQQAyDVADMLKQYFRD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 287 LPEPLLTFEYYELFVNILGLLQPHLERVAINALQLCCLLLpppNRRKLQLLMRMISRMSQNVDM-------------PKL 353
Cdd:cd04375   86 LPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDE---NREVLQTLLYFLSDVAANSQEnqmtatnlavclaPSL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148679897 354 -HEQIGTRSLMINTFSRCV---LCCAEEVDLDELLASRL-VSFLMDHHQEILQVPTYL 406
Cdd:cd04375  163 fHLNTSRRENSSPARRMQRkksLGKPDQKELSENKAAHQcLAYMIEECNTLFMVPKEM 220
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 30-88 6.17e-04

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown.


Pssm-ID: 239889 [Multi-domain]  Cd Length: 82  Bit Score: 38.72  E-value: 6.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148679897  30 LRKHRQHLKKYSNCFTAVEAIDWLYDLLRSNSnfgpevtRQQTIQLLRKFLKNHVIEDI 88
Cdd:cd04442   15 IKDRRHHLRTYPNCFVGKELIDWLIEHKEASD-------RETAIKIMQKLLDHSIIHHV 66
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 34-91 1.19e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in human also known as KIAA0645, is a DEP domain containing protein of unknown function.


Pssm-ID: 239896  Cd Length: 83  Bit Score: 38.03  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148679897  34 RQHLKKYSNCFTAVEAIDWLYDllrsnsNFGPEVTRQQTIQLLRKFLKNHVIEDIKGR 91
Cdd:cd04449   20 SWHKGLPSNCFIGSEAVSWLIN------NFEDVDTREEAVELGQELMNEGLIEHVSGR 71
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 283-379 3.89e-03

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: 38.57  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897 283 YFLNLPEPLLTFEYYELFVNILGLLQPHlERVAinALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPKLheqiGTRSL 362
Cdd:cd04377   77 WLRELPEPLMTFELYENFLRAMELEEKQ-ERVR--ALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRM----SANAL 149

                         90
                 ....*....|....*..
gi 148679897 363 MInTFSRCVLCCAEEVD 379
Cdd:cd04377  150 AI-VFAPCILRCPDTAD 165
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 29-107 7.70e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange proteins directly activated by cAMP) proteins are GEFs (guanine-nucleotide-exchange factors) for the small GTPases, Rap1 and Rap2. They are directly regulated by cyclic AMP, a second messenger that plays a role in the control of diverse cellular processes, such as cell adhesion and insulin secretion. Epac-like proteins share a common domain architecture, containing RasGEF, DEP and CAP-effector (cAMP binding) domains. The DEP domain is involved in membrane localization.


Pssm-ID: 239884  Cd Length: 125  Bit Score: 36.55  E-value: 7.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148679897  29 PLRKHRQHLKKYSNCFTAVEAIDWLYDLlrsnsnfGPEV-TRQQTIQLLRKFLKNHVIEDIKGRWGsesLDDNNQLFRFP 107
Cdd:cd04437   16 LIRDRKYHLRTYRQCCVGTELVDWLLQQ-------SPCVqSRSQAVGMWQVLLEEGVLLHVDQELH---FQDKYQFYRFS 85
 
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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