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Conserved domains on  [gi|6322598|ref|NP_012672|]
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GTPase-activating protein IML1 [Saccharomyces cerevisiae S288C]

Protein Classification

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 ...
208-484 1.78e-141

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: 436.17  E-value: 1.78e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     208 EFNIKDCLLNRGDMWVLSSKLVDTCVFMDQRLAFLDSIRGTIKGIYRNGKKIVSGYIGEQTRIIFRSESARLIFLIQITD 287
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGSIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     288 EMWNFEETGEQLFQKMVNSFFPKIFKKWKDVDTHHTITIAFAISMDLSDTSFKDLTPGESLKNS--QDYFRIVVDQVSII 365
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGPRDERGRlyKDFYRVVVDQESSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     366 HWVDIMETLREEFMEIRKDLLNKQTDKGYSVAnGRFSPVIKSNFLELVNFATTILTDPFKQLDLRHTTTHVMIISPGSGL 445
Cdd:pfam12257  161 DWTSILVTLKKEFANFQRDILLHHHEKRTRIA-GRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVITPGTGV 239
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 6322598     446 FDVDYSLLRLTGKKLLSLEMTMDLICLSKAPLHIVPLFR 484
Cdd:pfam12257  240 FEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1188-1271 4.79e-36

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: 131.63  E-value: 4.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598  1188 LSKLAYQIQRGEDrITLVNRKWHWKKHEKCFVGSEMVNWLIRNFSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHY 1267
Cdd:cd04449    1 LAEIAEAMRDPSG-IGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFY 79

                 ....
gi 6322598  1268 FYQF 1271
Cdd:cd04449   80 FYYI 83
DEPDC5_CTD super family cl44840
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1346-1506 8.56e-07

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: 52.77  E-value: 8.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598    1346 SLVIDVDPAGKSSKQESCTVHYDRVHNPDHCFHIRLEWLTTTPKLIDDLVGNWSRLCERYGLKMIEIPwEELCTIPSV-- 1423
Cdd:pfam19418   70 TVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVL-EGPFALPSYly 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598    1424 -NPFHSFVEIKLAI------------NPWEDPEFKDRELFAKSKfyyhvyLLKASGFLLDNRASKFlqnqdieFDIMYSw 1490
Cdd:pfam19418  149 gDPLRAQLFIPLNIscllkegsehlfDSFEPETYWDRMHLFQEA------ILHRFGFVQDKYSASA-------FNFPAE- 214
                          170
                   ....*....|....*.
gi 6322598    1491 GKPqfkyvQYIHHTGA 1506
Cdd:pfam19418  215 NKP-----QYIHVTGT 225
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
208-484 1.78e-141

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: 436.17  E-value: 1.78e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     208 EFNIKDCLLNRGDMWVLSSKLVDTCVFMDQRLAFLDSIRGTIKGIYRNGKKIVSGYIGEQTRIIFRSESARLIFLIQITD 287
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGSIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     288 EMWNFEETGEQLFQKMVNSFFPKIFKKWKDVDTHHTITIAFAISMDLSDTSFKDLTPGESLKNS--QDYFRIVVDQVSII 365
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGPRDERGRlyKDFYRVVVDQESSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     366 HWVDIMETLREEFMEIRKDLLNKQTDKGYSVAnGRFSPVIKSNFLELVNFATTILTDPFKQLDLRHTTTHVMIISPGSGL 445
Cdd:pfam12257  161 DWTSILVTLKKEFANFQRDILLHHHEKRTRIA-GRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVITPGTGV 239
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 6322598     446 FDVDYSLLRLTGKKLLSLEMTMDLICLSKAPLHIVPLFR 484
Cdd:pfam12257  240 FEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1188-1271 4.79e-36

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: 131.63  E-value: 4.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598  1188 LSKLAYQIQRGEDrITLVNRKWHWKKHEKCFVGSEMVNWLIRNFSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHY 1267
Cdd:cd04449    1 LAEIAEAMRDPSG-IGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFY 79

                 ....
gi 6322598  1268 FYQF 1271
Cdd:cd04449   80 FYYI 83
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1201-1271 5.54e-25

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: 99.59  E-value: 5.54e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322598    1201 RITLVNRKWHWKKHEKCFVGSEMVNWLIRNFSdIDTREDAIKYGQKVMKEGLFVHVLNKHN-FLDGHYFYQF 1271
Cdd:pfam00610    1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1199-1273 2.42e-20

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: 86.57  E-value: 2.42e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322598     1199 EDRITLVNRKWHWKKHEKCFVGSEMVNWLIRNFsDIDTREDAIKYGQKVMKEGLFVHVL--NKHNFLDGHYFYQFSP 1273
Cdd:smart00049    2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNL-EIIDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFTT 77
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1346-1506 8.56e-07

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: 52.77  E-value: 8.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598    1346 SLVIDVDPAGKSSKQESCTVHYDRVHNPDHCFHIRLEWLTTTPKLIDDLVGNWSRLCERYGLKMIEIPwEELCTIPSV-- 1423
Cdd:pfam19418   70 TVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVL-EGPFALPSYly 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598    1424 -NPFHSFVEIKLAI------------NPWEDPEFKDRELFAKSKfyyhvyLLKASGFLLDNRASKFlqnqdieFDIMYSw 1490
Cdd:pfam19418  149 gDPLRAQLFIPLNIscllkegsehlfDSFEPETYWDRMHLFQEA------ILHRFGFVQDKYSASA-------FNFPAE- 214
                          170
                   ....*....|....*.
gi 6322598    1491 GKPqfkyvQYIHHTGA 1506
Cdd:pfam19418  215 NKP-----QYIHVTGT 225
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
208-484 1.78e-141

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: 436.17  E-value: 1.78e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     208 EFNIKDCLLNRGDMWVLSSKLVDTCVFMDQRLAFLDSIRGTIKGIYRNGKKIVSGYIGEQTRIIFRSESARLIFLIQITD 287
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLSSELVGTCVYVGQKISFLGSIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     288 EMWNFEETGEQLFQKMVNSFFPKIFKKWKDVDTHHTITIAFAISMDLSDTSFKDLTPGESLKNS--QDYFRIVVDQVSII 365
Cdd:pfam12257   81 EMWDFDEDGELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGPRDERGRlyKDFYRVVVDQESSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598     366 HWVDIMETLREEFMEIRKDLLNKQTDKGYSVAnGRFSPVIKSNFLELVNFATTILTDPFKQLDLRHTTTHVMIISPGSGL 445
Cdd:pfam12257  161 DWTSILVTLKKEFANFQRDILLHHHEKRTRIA-GRNSPAIKGNILEAINLALNLFEDHYIDRDLRRTGTSIIVITPGTGV 239
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 6322598     446 FDVDYSLLRLTGKKLLSLEMTMDLICLSKAPLHIVPLFR 484
Cdd:pfam12257  240 FEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
1188-1271 4.79e-36

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: 131.63  E-value: 4.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598  1188 LSKLAYQIQRGEDrITLVNRKWHWKKHEKCFVGSEMVNWLIRNFSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHY 1267
Cdd:cd04449    1 LAEIAEAMRDPSG-IGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFY 79

                 ....
gi 6322598  1268 FYQF 1271
Cdd:cd04449   80 FYYI 83
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
1201-1271 5.54e-25

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: 99.59  E-value: 5.54e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322598    1201 RITLVNRKWHWKKHEKCFVGSEMVNWLIRNFSdIDTREDAIKYGQKVMKEGLFVHVLNKHN-FLDGHYFYQF 1271
Cdd:pfam00610    1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
1191-1270 6.38e-23

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: 93.94  E-value: 6.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598  1191 LAYQIQRGEDRITLVNRKWHWKKHEKCFVGSEMVNWLIRNFSDIDtREDAIKYGQKVMKEGLFVHVLN-KHNFLDGHYFY 1269
Cdd:cd04371    2 LVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAIT-REEAVELGQALLKHGLIHHVSDdKHTFRDSYALY 80

                 .
gi 6322598  1270 Q 1270
Cdd:cd04371   81 R 81
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
1199-1273 2.42e-20

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: 86.57  E-value: 2.42e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322598     1199 EDRITLVNRKWHWKKHEKCFVGSEMVNWLIRNFsDIDTREDAIKYGQKVMKEGLFVHVL--NKHNFLDGHYFYQFSP 1273
Cdd:smart00049    2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNL-EIIDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFTT 77
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
1207-1272 6.76e-13

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: 66.98  E-value: 6.76e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322598  1207 RKWHWKKHEKCFVGSEMVNWLIRNFSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHYFYQFS 1272
Cdd:cd04437   20 RKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQFYRFS 85
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
1207-1271 5.73e-12

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown.


Pssm-ID: 239888  Cd Length: 85  Bit Score: 62.83  E-value: 5.73e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322598  1207 RKWHWKKHEKCFVGSEMVNWLIRNfSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHYFYQF 1271
Cdd:cd04441   22 REEEGVKYERTFVGSEFIDWLLQE-GEAESRREAVQLCRRLLEHGIIQHVSNKHHFFDSNLLYQF 85
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
1207-1271 3.90e-11

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like proteins, also known as PGR22, contain an N-terminal permease domain, a central transmembrane region and a C-terminal DEP domain. They are orphan receptors of the class B G protein-coupled receptors. Their function is unknown.


Pssm-ID: 239890 [Multi-domain]  Cd Length: 83  Bit Score: 60.42  E-value: 3.90e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322598  1207 RKWHWKKHEKCFVGSEMVNWLI-RNFSDidTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHYFYQF 1271
Cdd:cd04443   20 RRCGLRTYKGVFCGCDLVSWLIeVGLAQ--DRGEAVLYGRRLLQGGVLQHITNEHHFRDENLLYRF 83
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
1206-1271 1.71e-08

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: 52.97  E-value: 1.71e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322598  1206 NRKWHWKKHEKCFVGSEMVNWLIRNfSDIDTREDAIKYGQKVMKEGLFVHVLNKH-NFLDGHYFYQF 1271
Cdd:cd04442   17 DRRHHLRTYPNCFVGKELIDWLIEH-KEASDRETAIKIMQKLLDHSIIHHVCDEHkEFKDAKLFYRF 82
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
1216-1271 1.05e-07

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and by the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity.


Pssm-ID: 239886  Cd Length: 81  Bit Score: 50.64  E-value: 1.05e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322598  1216 KCFVGSEMVNWLIRNfSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHYFYQF 1271
Cdd:cd04439   27 KCFLGNEFVSWLLEI-GEISKPEEGVNLGQALLENGIIHHVSDKHQFKNEQVLYRF 81
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
1194-1270 1.20e-07

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: 50.52  E-value: 1.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322598  1194 QIQRGEDRITLVNRKWHWKKHEKCFVGSEMVNWLIRNfSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHYFYQ 1270
Cdd:cd04448    5 KICRSSTGIEFQDHRYRLRTYTNCILGKELVNWLIRQ-GKAATRVQAIAIGQALLDAGWIECVSDDDLFRDEYALYK 80
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
1346-1506 8.56e-07

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: 52.77  E-value: 8.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598    1346 SLVIDVDPAGKSSKQESCTVHYDRVHNPDHCFHIRLEWLTTTPKLIDDLVGNWSRLCERYGLKMIEIPwEELCTIPSV-- 1423
Cdd:pfam19418   70 TVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVL-EGPFALPSYly 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322598    1424 -NPFHSFVEIKLAI------------NPWEDPEFKDRELFAKSKfyyhvyLLKASGFLLDNRASKFlqnqdieFDIMYSw 1490
Cdd:pfam19418  149 gDPLRAQLFIPLNIscllkegsehlfDSFEPETYWDRMHLFQEA------ILHRFGFVQDKYSASA-------FNFPAE- 214
                          170
                   ....*....|....*.
gi 6322598    1491 GKPqfkyvQYIHHTGA 1506
Cdd:pfam19418  215 NKP-----QYIHVTGT 225
DEP_dishevelled cd04438
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in dishevelled-like proteins. ...
1206-1262 1.33e-06

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: 47.72  E-value: 1.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322598  1206 NRKWHWKKHEKCFVGSEMVNWLIRNFSDIDTREDAIKYGQKVMKEGLFVHVLNKHNF 1262
Cdd:cd04438   18 DRMWLKITIPNSFIGSDLVDWLLSHVEGLTDRREARKYASSLLKLGYIRHTVNKITF 74
DEP_2_P-Rex cd04440
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex ...
1206-1274 4.15e-06

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity.


Pssm-ID: 239887  Cd Length: 93  Bit Score: 46.84  E-value: 4.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322598  1206 NRKWHWKKHEKCFVGSEMVNWLIRNfSDIDTREDAIKYGQKVMKEGLFVHVLNKHNFLDGHYFYQFSPE 1274
Cdd:cd04440   26 DRDYHLKTYKSVVPASKLVDWLLAQ-GDCRTREEAVILGVGLCNNGFMHHVLEKSEFKDEPLLFRFYAD 93
 
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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