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Conserved domains on  [gi|768026649|ref|XP_011528867|]
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GATOR1 complex protein DEPDC5 isoform X10 [Homo sapiens]

Protein Classification

IML1 and DEP domain-containing protein( domain architecture ID 11192789)

IML1 and DEP domain-containing protein

Graphical summary

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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 1.09e-160

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: 481.62  E-value: 1.09e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEInrasirQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 768026649   338 PGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFK 381
Cdd:pfam12257  235 PGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP super family cl02442
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 1179-1232 1.05e-18

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 cd04449:

Pssm-ID: 470580  Cd Length: 83  Bit Score: 81.94  E-value: 1.05e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768026649 1179 EILEAMKHPST-GVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQ 1232
Cdd:cd04449     3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQ 57
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 101-381 1.09e-160

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: 481.62  E-value: 1.09e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEInrasirQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 768026649   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 ...
 1179-1232 1.05e-18

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: 81.94  E-value: 1.05e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768026649 1179 EILEAMKHPST-GVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQ 1232
Cdd:cd04449     3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQ 57
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 1187-1232 3.10e-05

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: 43.43  E-value: 3.10e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 768026649   1187 PSTGVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQ 1232
Cdd:smart00049    1 PETGLKLRDRKYFLKtyPNCFTGSELVDWLMDNLE-IIDREEAVHLGQ 47
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 1190-1232 1.60e-03

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: 38.34  E-value: 1.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 768026649  1190 GVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQ 1232
Cdd:pfam00610    1 GVKLKDRRKHLKtyPNCFTGSEAVDWLMDNLE-IITREEAVELGQ 44
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 101-381 1.09e-160

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: 481.62  E-value: 1.09e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   101 ELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAG-IRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSC 179
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGsIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   180 EMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEInrasirQDHKGRFYEDFYKVVV 259
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP------RDERGRLYKDFYRVVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026649   260 QNERREEWTSLLVTIKKLFIQYP--VLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVIT 337
Cdd:pfam12257  155 DQESSGDWTSILVTLKKEFANFQrdILLHHHEKRTRIAGRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVIT 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 768026649   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 ...
 1179-1232 1.05e-18

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: 81.94  E-value: 1.05e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768026649 1179 EILEAMKHPST-GVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQ 1232
Cdd:cd04449     3 EIAEAMRDPSGiGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQ 57
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 1179-1232 4.36e-06

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: 45.79  E-value: 4.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768026649 1179 EILEAMKHPSTGVQL--LSEQKGLSPYCFISAEVVHWLVNHVEgIQTQAMAIDIMQ 1232
Cdd:cd04371     1 DLVRIMLDSDSGVPIkdRKYHLKTYPNCFTGSELVDWLLDNLE-AITREEAVELGQ 55
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 1187-1232 3.10e-05

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: 43.43  E-value: 3.10e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 768026649   1187 PSTGVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQ 1232
Cdd:smart00049    1 PETGLKLRDRKYFLKtyPNCFTGSELVDWLMDNLE-IIDREEAVHLGQ 47
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 1190-1232 1.60e-03

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: 38.34  E-value: 1.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 768026649  1190 GVQLLSEQKGLS--PYCFISAEVVHWLVNHVEgIQTQAMAIDIMQ 1232
Cdd:pfam00610    1 GVKLKDRRKHLKtyPNCFTGSEAVDWLMDNLE-IITREEAVELGQ 44
 
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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