NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046858820|ref|XP_017454703|]
View 

GATOR1 complex protein DEPDC5 isoform X13 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
101-381 4.05e-158

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: 479.69  E-value: 4.05e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEETRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEvnrasiQQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAG------PRDERGRLYKDFYRVVV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1046858820  338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEPDC5_CTD super family cl44840
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1275-1458 2.14e-106

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.


The actual alignment was detected with superfamily member pfam19418:

Pssm-ID: 466071  Cd Length: 303  Bit Score: 340.90  E-value: 2.14e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1275 WHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQRTVTLD 1354
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1355 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 1434
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154
                          170       180
                   ....*....|....*....|....
gi 1046858820 1435 QLFIPLNLGCLLKEGSEHLFDSLD 1458
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFE 178
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1176-1257 3.80e-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: 120.46  E-value: 3.80e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1176 EILEAMKHPST-GVQLLSEQKGLSPCCFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLIAHASGeaWRTFVYGFYF 1254
Cdd:cd04449      3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGFYF 80

                   ...
gi 1046858820 1255 YKI 1257
Cdd:cd04449     81 YYI 83
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
101-381 4.05e-158

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: 479.69  E-value: 4.05e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEETRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEvnrasiQQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAG------PRDERGRLYKDFYRVVV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1046858820  338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1275-1458 2.14e-106

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: 340.90  E-value: 2.14e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1275 WHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQRTVTLD 1354
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1355 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 1434
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154
                          170       180
                   ....*....|....*....|....
gi 1046858820 1435 QLFIPLNLGCLLKEGSEHLFDSLD 1458
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFE 178
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1176-1257 3.80e-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: 120.46  E-value: 3.80e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1176 EILEAMKHPST-GVQLLSEQKGLSPCCFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLIAHASGeaWRTFVYGFYF 1254
Cdd:cd04449      3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGFYF 80

                   ...
gi 1046858820 1255 YKI 1257
Cdd:cd04449     81 YYI 83
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1184-1259 5.05e-13

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: 65.77  E-value: 5.05e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046858820  1184 PSTGVQLLSEQKGLS--PCCFISAEVVHWLMNNVEgVQTQAMGIDIMQKMLEEQLIAHASGEAWRTFVYGFYFYKIVT 1259
Cdd:smart00049    1 PETGLKLRDRKYFLKtyPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1187-1257 1.10e-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: 61.84  E-value: 1.10e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046858820 1187 GVQLLSEQKGLS--PCCFISAEVVHWLMNNVEgVQTQAMGIDIMQKMLEEQLIAHASGEaWRTFVYGFYFYKI 1257
Cdd:pfam00610    1 GVKLKDRRKHLKtyPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDK-HGLFKDSYYFYRF 71
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
101-381 4.05e-158

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: 479.69  E-value: 4.05e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEETRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEvnrasiQQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAG------PRDERGRLYKDFYRVVV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820  260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1046858820  338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1275-1458 2.14e-106

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: 340.90  E-value: 2.14e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1275 WHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASyasrhsSFSRSFGGRSQAAALLAATVPEQRTVTLD 1354
Cdd:pfam19418    1 WSTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRRHS------SFSRSFGGRSQAAAYLAATVPEQRTVTLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1355 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 1434
Cdd:pfam19418   75 VDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRA 154
                          170       180
                   ....*....|....*....|....
gi 1046858820 1435 QLFIPLNLGCLLKEGSEHLFDSLD 1458
Cdd:pfam19418  155 QLFIPLNISCLLKEGSEHLFDSFE 178
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1176-1257 3.80e-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: 120.46  E-value: 3.80e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1176 EILEAMKHPST-GVQLLSEQKGLSPCCFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLIAHASGeaWRTFVYGFYF 1254
Cdd:cd04449      3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG--RHPFLDGFYF 80

                   ...
gi 1046858820 1255 YKI 1257
Cdd:cd04449     81 YYI 83
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
1176-1256 4.69e-13

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: 65.82  E-value: 4.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858820 1176 EILEAMKHPSTGVQL--LSEQKGLSPCCFISAEVVHWLMNNVEGVqTQAMGIDIMQKMLEEQLIAHASGEAWrTFVYGFY 1253
Cdd:cd04371      1 DLVRIMLDSDSGVPIkdRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVSDDKH-TFRDSYA 78

                   ...
gi 1046858820 1254 FYK 1256
Cdd:cd04371     79 LYR 81
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1184-1259 5.05e-13

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: 65.77  E-value: 5.05e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046858820  1184 PSTGVQLLSEQKGLS--PCCFISAEVVHWLMNNVEgVQTQAMGIDIMQKMLEEQLIAHASGEAWRTFVYGFYFYKIVT 1259
Cdd:smart00049    1 PETGLKLRDRKYFLKtyPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1187-1257 1.10e-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: 61.84  E-value: 1.10e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046858820 1187 GVQLLSEQKGLS--PCCFISAEVVHWLMNNVEgVQTQAMGIDIMQKMLEEQLIAHASGEaWRTFVYGFYFYKI 1257
Cdd:pfam00610    1 GVKLKDRRKHLKtyPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDK-HGLFKDSYYFYRF 71
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
1201-1269 6.71e-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: 6.71e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858820 1201 CFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLIAHASGEawRTFVYGFYFYKIVTDrEPERVAMQ 1269
Cdd:cd04437     30 CCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQE--LHFQDKYQFYRFSDD-ECSPAPLE 95
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH