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Conserved domains on  [gi|1207108914|ref|XP_021334979|]
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GATOR1 complex protein DEPDC5 isoform X5 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1267-1575 0e+00

DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues 1,291-1,603) of the DEPDC5 protein. It contains two structurally similar lobes and has a pseudo-2-fold rotational symmetry. Each half consists of a five-stranded beta-sheet, with an alpha-helix covering one side. The CTD is located in the core of DEPDC5 and contacts all the other domains of DEPDC5 except the NTD, making it the central organizer of this multi-domain protein.


:

Pssm-ID: 466071  Cd Length: 303  Bit Score: 553.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1267 WSAAALEDFALFQRKWFEVAFVMEERRPCDLPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQKTVTLD 1346
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1347 VDVNNRSDRTEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKAASCGFLLVPVLEVPFALSSYLYGDPLRA 1426
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1427 QLFIPLNIQCLLKEGSDNLFEGFEPETYWDRMQLFQEAILTRFGFVQDKFSASAFNFPSENKPQYIHVTGTVFLQLPYSK 1506
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAILHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108914 1507 RKYSSGQRRRRNSTTSTNQSLFGSEERVGYNWAYNTMLTKAWRTGVLGDEKLADRLLRDFTDFCANKDN 1575
Cdd:pfam19418  235 RKTSGQQRRRSNSEEYITRHFSGAEERVGYLWAYNTMLTKRWRTPATGDETFADRLLKDFTDFCANEDN 303
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
105-385 8.02e-157

Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which is a globular domain of about 80 residues. This entry includes vacuolar membrane-associated protein Iml1 and DEP domain-containing protein 5/DDB_G0279099. In Saccharomyces cerevisiae, Iml1 is a subunit of both the SEA (Seh1-associated) and Iml1 complexes (Iml1-Npr2-Npr3). SEA complex is associates dynamically with the vacuole and is involved in autophagy. Iml1 complex is required for non-nitrogen-starvation (NNS)-induced autophagy.


:

Pssm-ID: 463510  Cd Length: 278  Bit Score: 477.38  E-value: 8.02e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  105 ELTFKDQYIGRGDMWRLKKSLVSTCAYVTQKVEFAG-IRAQASELWVKGEKVTCGYISEDTRVVFRSTSAMVYIFIQMSC 183
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  184 EMWDFDIYGDLYFEKAVNGFLSDLFAKWKEKNCSHEVTVVLFSRTFYSAKTLEEFPESqrasvrQDHEGRYYEDFYRVVA 263
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  264 QNERRDEWMSLLVTIKKLFIQYP--VLVRLKGADGFPCGHNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 341
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1207108914  342 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 385
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1163-1246 1.35e-32

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: 121.61  E-value: 1.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1163 LMEILEAIKHPTT-GVQLLPEQRGLPPNCFVSAEVVHWLVSTVENVATQGIAVEIMQKMLEEGLITHASGdaMRTFVYGF 1241
Cdd:cd04449      1 LAEIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGF 78

                   ....*
gi 1207108914 1242 YFYRI 1246
Cdd:cd04449     79 YFYYI 83
 
Name Accession Description Interval E-value
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1267-1575 0e+00

DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues 1,291-1,603) of the DEPDC5 protein. It contains two structurally similar lobes and has a pseudo-2-fold rotational symmetry. Each half consists of a five-stranded beta-sheet, with an alpha-helix covering one side. The CTD is located in the core of DEPDC5 and contacts all the other domains of DEPDC5 except the NTD, making it the central organizer of this multi-domain protein.


Pssm-ID: 466071  Cd Length: 303  Bit Score: 553.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1267 WSAAALEDFALFQRKWFEVAFVMEERRPCDLPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQKTVTLD 1346
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1347 VDVNNRSDRTEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKAASCGFLLVPVLEVPFALSSYLYGDPLRA 1426
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1427 QLFIPLNIQCLLKEGSDNLFEGFEPETYWDRMQLFQEAILTRFGFVQDKFSASAFNFPSENKPQYIHVTGTVFLQLPYSK 1506
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAILHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108914 1507 RKYSSGQRRRRNSTTSTNQSLFGSEERVGYNWAYNTMLTKAWRTGVLGDEKLADRLLRDFTDFCANKDN 1575
Cdd:pfam19418  235 RKTSGQQRRRSNSEEYITRHFSGAEERVGYLWAYNTMLTKRWRTPATGDETFADRLLKDFTDFCANEDN 303
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
105-385 8.02e-157

Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which is a globular domain of about 80 residues. This entry includes vacuolar membrane-associated protein Iml1 and DEP domain-containing protein 5/DDB_G0279099. In Saccharomyces cerevisiae, Iml1 is a subunit of both the SEA (Seh1-associated) and Iml1 complexes (Iml1-Npr2-Npr3). SEA complex is associates dynamically with the vacuole and is involved in autophagy. Iml1 complex is required for non-nitrogen-starvation (NNS)-induced autophagy.


Pssm-ID: 463510  Cd Length: 278  Bit Score: 477.38  E-value: 8.02e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  105 ELTFKDQYIGRGDMWRLKKSLVSTCAYVTQKVEFAG-IRAQASELWVKGEKVTCGYISEDTRVVFRSTSAMVYIFIQMSC 183
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  184 EMWDFDIYGDLYFEKAVNGFLSDLFAKWKEKNCSHEVTVVLFSRTFYSAKTLEEFPESqrasvrQDHEGRYYEDFYRVVA 263
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  264 QNERRDEWMSLLVTIKKLFIQYP--VLVRLKGADGFPCGHNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 341
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1207108914  342 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 385
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1163-1246 1.35e-32

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: 121.61  E-value: 1.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1163 LMEILEAIKHPTT-GVQLLPEQRGLPPNCFVSAEVVHWLVSTVENVATQGIAVEIMQKMLEEGLITHASGdaMRTFVYGF 1241
Cdd:cd04449      1 LAEIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGF 78

                   ....*
gi 1207108914 1242 YFYRI 1246
Cdd:cd04449     79 YFYYI 83
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1173-1248 1.83e-12

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: 64.23  E-value: 1.83e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108914  1173 PTTGVQLLP--EQRGLPPNCFVSAEVVHWLVSTVEnVATQGIAVEIMQKMLEEGLITHASGDAMRTFVYGFYFYRIVD 1248
Cdd:smart00049    1 PETGLKLRDrkYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1188-1246 7.85e-11

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: 59.14  E-value: 7.85e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108914 1188 PNCFVSAEVVHWLVSTVEnVATQGIAVEIMQKMLEEGLITHASGDAmRTFVYGFYFYRI 1246
Cdd:pfam00610   15 PNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKH-GLFKDSYYFYRF 71
 
Name Accession Description Interval E-value
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1267-1575 0e+00

DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues 1,291-1,603) of the DEPDC5 protein. It contains two structurally similar lobes and has a pseudo-2-fold rotational symmetry. Each half consists of a five-stranded beta-sheet, with an alpha-helix covering one side. The CTD is located in the core of DEPDC5 and contacts all the other domains of DEPDC5 except the NTD, making it the central organizer of this multi-domain protein.


Pssm-ID: 466071  Cd Length: 303  Bit Score: 553.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1267 WSAAALEDFALFQRKWFEVAFVMEERRPCDLPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQKTVTLD 1346
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1347 VDVNNRSDRTEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKAASCGFLLVPVLEVPFALSSYLYGDPLRA 1426
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1427 QLFIPLNIQCLLKEGSDNLFEGFEPETYWDRMQLFQEAILTRFGFVQDKFSASAFNFPSENKPQYIHVTGTVFLQLPYSK 1506
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAILHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108914 1507 RKYSSGQRRRRNSTTSTNQSLFGSEERVGYNWAYNTMLTKAWRTGVLGDEKLADRLLRDFTDFCANKDN 1575
Cdd:pfam19418  235 RKTSGQQRRRSNSEEYITRHFSGAEERVGYLWAYNTMLTKRWRTPATGDETFADRLLKDFTDFCANEDN 303
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
105-385 8.02e-157

Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which is a globular domain of about 80 residues. This entry includes vacuolar membrane-associated protein Iml1 and DEP domain-containing protein 5/DDB_G0279099. In Saccharomyces cerevisiae, Iml1 is a subunit of both the SEA (Seh1-associated) and Iml1 complexes (Iml1-Npr2-Npr3). SEA complex is associates dynamically with the vacuole and is involved in autophagy. Iml1 complex is required for non-nitrogen-starvation (NNS)-induced autophagy.


Pssm-ID: 463510  Cd Length: 278  Bit Score: 477.38  E-value: 8.02e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  105 ELTFKDQYIGRGDMWRLKKSLVSTCAYVTQKVEFAG-IRAQASELWVKGEKVTCGYISEDTRVVFRSTSAMVYIFIQMSC 183
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  184 EMWDFDIYGDLYFEKAVNGFLSDLFAKWKEKNCSHEVTVVLFSRTFYSAKTLEEFPESqrasvrQDHEGRYYEDFYRVVA 263
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914  264 QNERRDEWMSLLVTIKKLFIQYP--VLVRLKGADGFPCGHNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 341
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1207108914  342 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 385
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1163-1246 1.35e-32

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: 121.61  E-value: 1.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1163 LMEILEAIKHPTT-GVQLLPEQRGLPPNCFVSAEVVHWLVSTVENVATQGIAVEIMQKMLEEGLITHASGdaMRTFVYGF 1241
Cdd:cd04449      1 LAEIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGF 78

                   ....*
gi 1207108914 1242 YFYRI 1246
Cdd:cd04449     79 YFYYI 83
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
1165-1245 4.15e-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: 68.91  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1165 EILEAIKHPTTGVQL--LPEQRGLPPNCFVSAEVVHWLVSTVENVaTQGIAVEIMQKMLEEGLITHASGDaMRTFVYGFY 1242
Cdd:cd04371      1 DLVRIMLDSDSGVPIkdRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVSDD-KHTFRDSYA 78

                   ...
gi 1207108914 1243 FYR 1245
Cdd:cd04371     79 LYR 81
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1173-1248 1.83e-12

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: 64.23  E-value: 1.83e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108914  1173 PTTGVQLLP--EQRGLPPNCFVSAEVVHWLVSTVEnVATQGIAVEIMQKMLEEGLITHASGDAMRTFVYGFYFYRIVD 1248
Cdd:smart00049    1 PETGLKLRDrkYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1188-1246 7.85e-11

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: 59.14  E-value: 7.85e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108914 1188 PNCFVSAEVVHWLVSTVEnVATQGIAVEIMQKMLEEGLITHASGDAmRTFVYGFYFYRI 1246
Cdd:pfam00610   15 PNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKH-GLFKDSYYFYRF 71
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
1188-1245 2.41e-05

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: 44.12  E-value: 2.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108914 1188 PNCFVSAEVVHWLVSTVEnVATQGIAVEIMQKMLEEGLITHASgDAMRTFVYGFYFYR 1245
Cdd:cd04442     26 PNCFVGKELIDWLIEHKE-ASDRETAIKIMQKLLDHSIIHHVC-DEHKEFKDAKLFYR 81
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
1165-1245 2.03e-04

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: 41.66  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108914 1165 EILEAIKHPTTGVQLLPEQRGLP--PNCFVSAEVVHWLVsTVENVATQGIAVEIMQKMLEEGLITHASGDamRTFVYGFY 1242
Cdd:cd04448      1 DLWEKICRSSTGIEFQDHRYRLRtyTNCILGKELVNWLI-RQGKAATRVQAIAIGQALLDAGWIECVSDD--DLFRDEYA 77

                   ...
gi 1207108914 1243 FYR 1245
Cdd:cd04448     78 LYK 80
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
1189-1256 6.35e-04

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: 41.17  E-value: 6.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108914 1189 NCFVSAEVVHWLVSTVENVATQGIAVEIMQKMLEEGLITHASGDamRTFVYGFYFYRIVDKDNEKAPL 1256
Cdd:cd04437     29 QCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQE--LHFQDKYQFYRFSDDECSPAPL 94
DEP_dishevelled cd04438
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in dishevelled-like proteins. ...
1188-1229 2.51e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in dishevelled-like proteins. Dishevelled-like proteins play a key role in the transduction of the Wnt signal from the cell surface to the nucleus, which in turn is an important regulatory pathway for cellular development and growth. They contain an N-terminal DIX domain, a central PDZ domain, and a C-terminal DEP domain.


Pssm-ID: 239885  Cd Length: 84  Bit Score: 38.48  E-value: 2.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207108914 1188 PNCFVSAEVVHWLVSTVENVATQGIAVEIMQKMLEEGLITHA 1229
Cdd:cd04438     27 PNSFIGSDLVDWLLSHVEGLTDRREARKYASSLLKLGYIRHT 68
 
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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