DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1275-1582
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: 570.86 E-value: 0e+00
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
101-381
1.53e-156
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: 1.53e-156
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1176-1257
3.79e-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: 3.79e-32
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1275-1582
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: 570.86 E-value: 0e+00
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
101-381
1.53e-156
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: 1.53e-156
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1176-1257
3.79e-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: 3.79e-32
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1184-1257
4.39e-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: 4.39e-13
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1187-1257
8.02e-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: 62.22 E-value: 8.02e-12
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1275-1582
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: 570.86 E-value: 0e+00
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
101-381
1.53e-156
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: 1.53e-156
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1176-1257
3.79e-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: 3.79e-32
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
1176-1256
4.20e-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: 66.21 E-value: 4.20e-13
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1184-1257
4.39e-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: 4.39e-13
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1187-1257
8.02e-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: 62.22 E-value: 8.02e-12
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
1201-1269
5.58e-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: 41.56 E-value: 5.58e-04
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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