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Conserved domains on  [gi|339276033|ref|NP_001229826|]
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GATOR1 complex protein DEPDC5 isoform 5 [Homo sapiens]

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 ...
 1178-1485 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: 580.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1178 WHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQRTVTLD 1257
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1258 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 1337
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1338 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 1417
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAILHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 234

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1418 RKFSGQQRRRRNSTsSTNQNMF--CEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDN 1485
Cdd:pfam19418  235 RKTSGQQRRRSNSE-EYITRHFsgAEERVGYLWAYNTMLTKRWRTPATGDETFADRLLKDFTDFCANEDN 303
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 101-381 3.22e-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: 476.61  E-value: 3.22e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEInrasirQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 339276033   338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 1079-1160 6.01e-33

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: 122.77  E-value: 6.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033 1079 EILEAMKHPST-GVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGeaWRTFIYGFYF 1157
Cdd:cd04449     3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGFYF 80


                  ...
gi 339276033 1158 YKI 1160
Cdd:cd04449    81 YYI 83
 
Name Accession Description Interval E-value
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
 1178-1485 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: 580.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1178 WHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQRTVTLD 1257
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1258 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 1337
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1338 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 1417
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAILHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 234

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1418 RKFSGQQRRRRNSTsSTNQNMF--CEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDN 1485
Cdd:pfam19418  235 RKTSGQQRRRSNSE-EYITRHFsgAEERVGYLWAYNTMLTKRWRTPATGDETFADRLLKDFTDFCANEDN 303
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 101-381 3.22e-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: 476.61  E-value: 3.22e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEInrasirQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 339276033   338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 1079-1160 6.01e-33

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: 122.77  E-value: 6.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033 1079 EILEAMKHPST-GVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGeaWRTFIYGFYF 1157
Cdd:cd04449     3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGFYF 80


                  ...
gi 339276033 1158 YKI 1160
Cdd:cd04449    81 YYI 83
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 1087-1162 6.79e-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: 70.78  E-value: 6.79e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339276033   1087 PSTGVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVT 1162
Cdd:smart00049    1 PETGLKLRDRKYFLKtyPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 1090-1160 5.35e-12

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: 62.61  E-value: 5.35e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339276033  1090 GVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQKMLEEQLITHASGEaWRTFIYGFYFYKI 1160
Cdd:pfam00610    1 GVKLKDRRKHLKtyPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDK-HGLFKDSYYFYRF 71
 
Name Accession Description Interval E-value
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
 1178-1485 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: 580.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1178 WHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQRTVTLD 1257
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1258 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 1337
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1338 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 1417
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAILHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSK 234

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033  1418 RKFSGQQRRRRNSTsSTNQNMF--CEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDN 1485
Cdd:pfam19418  235 RKTSGQQRRRSNSE-EYITRHFsgAEERVGYLWAYNTMLTKRWRTPATGDETFADRLLKDFTDFCANEDN 303
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 101-381 3.22e-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: 476.61  E-value: 3.22e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEInrasirQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033   260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 339276033   338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 1079-1160 6.01e-33

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: 122.77  E-value: 6.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033 1079 EILEAMKHPST-GVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGeaWRTFIYGFYF 1157
Cdd:cd04449     3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGFYF 80


                  ...
gi 339276033 1158 YKI 1160
Cdd:cd04449    81 YYI 83
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 1087-1162 6.79e-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: 70.78  E-value: 6.79e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339276033   1087 PSTGVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVT 1162
Cdd:smart00049    1 PETGLKLRDRKYFLKtyPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRFTT 77
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 1079-1159 5.55e-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: 68.52  E-value: 5.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339276033 1079 EILEAMKHPSTGVQL--LSEQKGLSPYCFISAEVVHWLVNHVEgIQTQAMAIDIMQKMLEEQLITHASGEAWrTFIYGFY 1156
Cdd:cd04371     1 DLVRIMLDSDSGVPIkdRKYHLKTYPNCFTGSELVDWLLDNLE-AITREEAVELGQALLKHGLIHHVSDDKH-TFRDSYA 78


                  ...
gi 339276033 1157 FYK 1159
Cdd:cd04371    79 LYR 81
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 1090-1160 5.35e-12

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: 62.61  E-value: 5.35e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339276033  1090 GVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQKMLEEQLITHASGEaWRTFIYGFYFYKI 1160
Cdd:pfam00610    1 GVKLKDRRKHLKtyPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDK-HGLFKDSYYFYRF 71
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 1104-1172 4.06e-05

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: 44.64  E-value: 4.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339276033 1104 CFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEawRTFIYGFYFYKIVTDkEPDRVAMQ 1172
Cdd:cd04437    30 CCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQE--LHFQDKYQFYRFSDD-ECSPAPLE 95
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 1102-1146 4.74e-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: 43.34  E-value: 4.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 339276033 1102 PYCFISAEVVHWLVNHVEGiQTQAMAIDIMQKMLEEQLITHASGE 1146
Cdd:cd04442    26 PNCFVGKELIDWLIEHKEA-SDRETAIKIMQKLLDHSIIHHVCDE 69
DEP_dishevelled cd04438
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in dishevelled-like proteins. ...
 1102-1151 8.14e-04

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: 39.63  E-value: 8.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 339276033 1102 PYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEawRTF 1151
Cdd:cd04438    27 PNSFIGSDLVDWLLSHVEGLTDRREARKYASSLLKLGYIRHTVNK--ITF 74
 
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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