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Conserved domains on  [gi|758993295|ref|XP_962296|]
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vacuolar membrane-associated protein iml-1 [Neurospora crassa OR74A]

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 ...
 199-506 1.32e-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: 487.78  E-value: 1.32e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   199 ELCFRDQYMSRSDMWQLAvRELSEKTVYKGQMVLFMGTLKAQVTAVYVEGRKVPSAFFGHNTKPIFRSESARYVLFIQMA 278
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLS-SELVGTCVYVGQKISFLGSIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   279 REMWDFDSDGsgEIMFNKVVNGFLPALFKKWASLKVRHLVSIVLFARVEYDTGISTELGNPdvqndyytgVQSSGDRrpY 358
Cdd:pfam12257   80 REMWDFDEDG--ELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP---------RDERGRL--Y 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   359 KDFYRVVVSEMGSGEWTKILYQLKREFNYFRRDISTFHQKAMhsfsssddpadqqaalNRITAEASRAIYGNFLEAINMA 438
Cdd:pfam12257  147 KDFYRVVVDQESSGDWTSILVTLKKEFANFQRDILLHHHEKR----------------TRIAGRNSPAIKGNILEAINLA 210

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758993295   439 TSLFAHDYIDRDLMRTGISVVVISPSPGIFEVEYDALRRTTEALVGNGIGIDLICIPKAPLHSVPLFR 506
Cdd:pfam12257  211 LNLFEDHYIDRDLRRTGTSIIVITPGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 1318-1420 2.44e-34

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: 127.01  E-value: 2.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1318 LAALAEAIQQPVengGIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDLEDREEAEELGNRLMVTsddkskdeskdgrkd 1397
Cdd:cd04449     1 LAEIAEAMRDPS---GIGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNE--------------- 62

                          90       100
                  ....*....|....*....|...
gi 758993295 1398 ggGLFVHVERRHPFRDGQYFYQI 1420
Cdd:cd04449    63 --GLIEHVSGRHPFLDGFYFYYI 83
DEPDC5_CTD super family cl44840
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
 1468-1665 5.25e-16

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: 80.89  E-value: 5.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1468 EDSSPTSGTVTPTAAMMAGGKKPRVVLskvmkYDVDHRKRSYRPEVVDLHYDRLHNPDNCYHIRIDWMNVTAKLIEDAIE 1547
Cdd:pfam19418   46 SFSRSFGGRSQAAAYLAATVPEQRTVT-----LDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1548 AWAREAALYGLRLVEVPINEACDITEI--NPFRRPYMIKLAVQPPNQQPITYFDpNSFTPQAQPGR-HFYQRALLRKFDF 1624
Cdd:pfam19418  121 GWHRKATSCGFLLVPVLEGPFALPSYLygDPLRAQLFIPLNISCLLKEGSEHLF-DSFEPETYWDRmHLFQEAILHRFGF 199

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 758993295  1625 VLDMEPASSFPYTVDvsyswGKPdfkytQFIHRSGTLIAEI 1665
Cdd:pfam19418  200 VQDKYSASAFNFPAE-----NKP-----QYIHVTGTVFLQL 230
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1714-1874 1.24e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1714 ISTPGLYGPNAHPDQPNAVSSPlvkpttaflspalrPHLIGPLASGPPSTNGFGTTGQPLNRSTVTVPVTPviqDPEVIK 1793
Cdd:pfam05109  434 LNTTGFAAPNTTTGLPSSTHVP--------------TNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP---SPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1794 DELESFCRDRSALEAfyrellerEAHPPAPNTTPGLAPVKIPSTTATKDS------TLAFATPHLGAGQNTTSTGHTVPD 1867
Cdd:pfam05109  497 NGTESKAPDMTSPTS--------AVTTPTPNATSPTPAVTTPTPNATSPTlgktspTSAVTTPTPNATSPTPAVTTPTPN 568


                   ....*..
gi 758993295  1868 TNIPSLG 1874
Cdd:pfam05109  569 ATIPTLG 575
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 199-506 1.32e-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: 487.78  E-value: 1.32e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   199 ELCFRDQYMSRSDMWQLAvRELSEKTVYKGQMVLFMGTLKAQVTAVYVEGRKVPSAFFGHNTKPIFRSESARYVLFIQMA 278
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLS-SELVGTCVYVGQKISFLGSIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   279 REMWDFDSDGsgEIMFNKVVNGFLPALFKKWASLKVRHLVSIVLFARVEYDTGISTELGNPdvqndyytgVQSSGDRrpY 358
Cdd:pfam12257   80 REMWDFDEDG--ELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP---------RDERGRL--Y 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   359 KDFYRVVVSEMGSGEWTKILYQLKREFNYFRRDISTFHQKAMhsfsssddpadqqaalNRITAEASRAIYGNFLEAINMA 438
Cdd:pfam12257  147 KDFYRVVVDQESSGDWTSILVTLKKEFANFQRDILLHHHEKR----------------TRIAGRNSPAIKGNILEAINLA 210

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758993295   439 TSLFAHDYIDRDLMRTGISVVVISPSPGIFEVEYDALRRTTEALVGNGIGIDLICIPKAPLHSVPLFR 506
Cdd:pfam12257  211 LNLFEDHYIDRDLRRTGTSIIVITPGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 1318-1420 2.44e-34

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: 127.01  E-value: 2.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1318 LAALAEAIQQPVengGIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDLEDREEAEELGNRLMVTsddkskdeskdgrkd 1397
Cdd:cd04449     1 LAEIAEAMRDPS---GIGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNE--------------- 62

                          90       100
                  ....*....|....*....|...
gi 758993295 1398 ggGLFVHVERRHPFRDGQYFYQI 1420
Cdd:cd04449    63 --GLIEHVSGRHPFLDGFYFYYI 83
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 1333-1420 4.41e-20

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: 85.72  E-value: 4.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1333 GIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDlEDREEAEELGNRLMvtsddkskdeskdgrkdGGGLFVHVERRH-PF 1411
Cdd:pfam00610    1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDNLEI-ITREEAVELGQLLL-----------------DQGLIHHVGDKHgLF 62


                   ....*....
gi 758993295  1412 RDGQYFYQI 1420
Cdd:pfam00610   63 KDSYYFYRF 71
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
 1468-1665 5.25e-16

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: 80.89  E-value: 5.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1468 EDSSPTSGTVTPTAAMMAGGKKPRVVLskvmkYDVDHRKRSYRPEVVDLHYDRLHNPDNCYHIRIDWMNVTAKLIEDAIE 1547
Cdd:pfam19418   46 SFSRSFGGRSQAAAYLAATVPEQRTVT-----LDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1548 AWAREAALYGLRLVEVPINEACDITEI--NPFRRPYMIKLAVQPPNQQPITYFDpNSFTPQAQPGR-HFYQRALLRKFDF 1624
Cdd:pfam19418  121 GWHRKATSCGFLLVPVLEGPFALPSYLygDPLRAQLFIPLNISCLLKEGSEHLF-DSFEPETYWDRmHLFQEAILHRFGF 199

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 758993295  1625 VLDMEPASSFPYTVDvsyswGKPdfkytQFIHRSGTLIAEI 1665
Cdd:pfam19418  200 VQDKYSASAFNFPAE-----NKP-----QYIHVTGTVFLQL 230
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 1333-1422 3.63e-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: 71.93  E-value: 3.63e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   1333 GIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEdLEDREEAEELGNRLMvtsddkskDEskdgrkdggGLFVHV--ERRHP 1410
Cdd:smart00049    4 GLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLL--------DE---------GLIHHVngPNKHT 65

                            90
                    ....*....|..
gi 758993295   1411 FRDGQYFYQISS 1422
Cdd:smart00049   66 FKDSKALYRFTT 77
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1714-1874 1.24e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1714 ISTPGLYGPNAHPDQPNAVSSPlvkpttaflspalrPHLIGPLASGPPSTNGFGTTGQPLNRSTVTVPVTPviqDPEVIK 1793
Cdd:pfam05109  434 LNTTGFAAPNTTTGLPSSTHVP--------------TNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP---SPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1794 DELESFCRDRSALEAfyrellerEAHPPAPNTTPGLAPVKIPSTTATKDS------TLAFATPHLGAGQNTTSTGHTVPD 1867
Cdd:pfam05109  497 NGTESKAPDMTSPTS--------AVTTPTPNATSPTPAVTTPTPNATSPTlgktspTSAVTTPTPNATSPTPAVTTPTPN 568


                   ....*..
gi 758993295  1868 TNIPSLG 1874
Cdd:pfam05109  569 ATIPTLG 575
 
Name Accession Description Interval E-value
IML1 pfam12257
Vacuolar membrane-associated protein Iml1; Proteins in this family contain a DEP domain, which ...
 199-506 1.32e-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: 487.78  E-value: 1.32e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   199 ELCFRDQYMSRSDMWQLAvRELSEKTVYKGQMVLFMGTLKAQVTAVYVEGRKVPSAFFGHNTKPIFRSESARYVLFIQMA 278
Cdd:pfam12257    1 ELTFKDQYLSRSDMWRLS-SELVGTCVYVGQKISFLGSIRATVKEIYINGKKVFSGYITENTKIIFRSESARYTIFIQMS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   279 REMWDFDSDGsgEIMFNKVVNGFLPALFKKWASLKVRHLVSIVLFARVEYDTGISTELGNPdvqndyytgVQSSGDRrpY 358
Cdd:pfam12257   80 REMWDFDEDG--ELYFEKVVNGFLPELFKRWKELGTHHLVTIVLFSRVFYDTSEIDDEAGP---------RDERGRL--Y 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   359 KDFYRVVVSEMGSGEWTKILYQLKREFNYFRRDISTFHQKAMhsfsssddpadqqaalNRITAEASRAIYGNFLEAINMA 438
Cdd:pfam12257  147 KDFYRVVVDQESSGDWTSILVTLKKEFANFQRDILLHHHEKR----------------TRIAGRNSPAIKGNILEAINLA 210

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758993295   439 TSLFAHDYIDRDLMRTGISVVVISPSPGIFEVEYDALRRTTEALVGNGIGIDLICIPKAPLHSVPLFR 506
Cdd:pfam12257  211 LNLFEDHYIDRDLRRTGTSIIVITPGTGVFEVDYDLLRLTTERLLDNGIGIDLVCLSKPPLHSVPLFR 278
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 1318-1420 2.44e-34

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: 127.01  E-value: 2.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1318 LAALAEAIQQPVengGIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDLEDREEAEELGNRLMVTsddkskdeskdgrkd 1397
Cdd:cd04449     1 LAEIAEAMRDPS---GIGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNE--------------- 62

                          90       100
                  ....*....|....*....|...
gi 758993295 1398 ggGLFVHVERRHPFRDGQYFYQI 1420
Cdd:cd04449    63 --GLIEHVSGRHPFLDGFYFYYI 83
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 1333-1420 4.41e-20

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: 85.72  E-value: 4.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1333 GIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDlEDREEAEELGNRLMvtsddkskdeskdgrkdGGGLFVHVERRH-PF 1411
Cdd:pfam00610    1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDNLEI-ITREEAVELGQLLL-----------------DQGLIHHVGDKHgLF 62


                   ....*....
gi 758993295  1412 RDGQYFYQI 1420
Cdd:pfam00610   63 KDSYYFYRF 71
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 1333-1419 1.06e-19

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: 85.08  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1333 GIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDlEDREEAEELGNRLMvtsddkskDEskdgrkdggGLFVHVE-RRHPF 1411
Cdd:cd04371    12 GVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEA-ITREEAVELGQALL--------KH---------GLIHHVSdDKHTF 73


                  ....*...
gi 758993295 1412 RDGQYFYQ 1419
Cdd:cd04371    74 RDSYALYR 81
DEPDC5_CTD pfam19418
DEPDC5 protein C-terminal region; This entry represents the C-terminal domain (CTD) (residues ...
 1468-1665 5.25e-16

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: 80.89  E-value: 5.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1468 EDSSPTSGTVTPTAAMMAGGKKPRVVLskvmkYDVDHRKRSYRPEVVDLHYDRLHNPDNCYHIRIDWMNVTAKLIEDAIE 1547
Cdd:pfam19418   46 SFSRSFGGRSQAAAYLAATVPEQRTVT-----LDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1548 AWAREAALYGLRLVEVPINEACDITEI--NPFRRPYMIKLAVQPPNQQPITYFDpNSFTPQAQPGR-HFYQRALLRKFDF 1624
Cdd:pfam19418  121 GWHRKATSCGFLLVPVLEGPFALPSYLygDPLRAQLFIPLNISCLLKEGSEHLF-DSFEPETYWDRmHLFQEAILHRFGF 199

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 758993295  1625 VLDMEPASSFPYTVDvsyswGKPdfkytQFIHRSGTLIAEI 1665
Cdd:pfam19418  200 VQDKYSASAFNFPAE-----NKP-----QYIHVTGTVFLQL 230
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 1333-1422 3.63e-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: 71.93  E-value: 3.63e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295   1333 GIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEdLEDREEAEELGNRLMvtsddkskDEskdgrkdggGLFVHV--ERRHP 1410
Cdd:smart00049    4 GLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLL--------DE---------GLIHHVngPNKHT 65

                            90
                    ....*....|..
gi 758993295   1411 FRDGQYFYQISS 1422
Cdd:smart00049   66 FKDSKALYRFTT 77
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 1336-1429 3.40e-07

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: 50.80  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1336 MQNRRWHLRLHYNCFIGSDMTTWLLENFEDLEDREEAEELGNRLMvtsddkskDEskdgrkdggGLFVHVERRHPFRDGQ 1415
Cdd:cd04437    17 IRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLL--------EE---------GVLLHVDQELHFQDKY 79

                          90
                  ....*....|....
gi 758993295 1416 YFYQISSDYAKPNP 1429
Cdd:cd04437    80 QFYRFSDDECSPAP 93
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
 1318-1419 2.09e-06

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: 47.43  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1318 LAALAEAIQQPVENGGIRMQNrrwhlrlhynCFIGSDMTTWLLENFEdLEDREEAEELGNRLMVTsddkskdeskdgrkd 1397
Cdd:cd04441    11 LMSTENSILQVREEEGVKYER----------TFVGSEFIDWLLQEGE-AESRREAVQLCRRLLEH--------------- 64

                          90       100
                  ....*....|....*....|..
gi 758993295 1398 ggGLFVHVERRHPFRDGQYFYQ 1419
Cdd:cd04441    65 --GIIQHVSNKHHFFDSNLLYQ 84
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
 1339-1418 2.98e-05

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: 44.24  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1339 RRWHLRLHYNCFIGSDMTTWLLEnfEDL-EDREEAEELGNRLMVtsddkskdeskdgrkdgGGLFVHVERRHPFRDGQYF 1417
Cdd:cd04443    20 RRCGLRTYKGVFCGCDLVSWLIE--VGLaQDRGEAVLYGRRLLQ-----------------GGVLQHITNEHHFRDENLL 80


                  .
gi 758993295 1418 Y 1418
Cdd:cd04443    81 Y 81
DEP_dishevelled cd04438
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in dishevelled-like proteins. ...
 1319-1380 5.05e-05

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: 43.49  E-value: 5.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758993295 1319 AALAEAIQQPveNGGIRMQNRRWHLRLHYNCFIGSDMTTWLLENFEDLEDREEAEELGNRLM 1380
Cdd:cd04438     1 NGIPRVMRRP--DSGLEIKDRMWLKITIPNSFIGSDLVDWLLSHVEGLTDRREARKYASSLL 60
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 1336-1380 2.20e-04

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: 41.80  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 758993295 1336 MQNRRWHLRLHYNCFIGSDMTTWLLENFEdLEDREEAEELGNRLM 1380
Cdd:cd04442    15 IKDRRHHLRTYPNCFVGKELIDWLIEHKE-ASDRETAIKIMQKLL 58
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 1331-1390 3.31e-04

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: 41.27  E-value: 3.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758993295 1331 NGGIRMQNRRWHLRLHYNCFIGSDMTTWLLENfEDLEDREEAEELGNRLM-------VTSDDKSKDE 1390
Cdd:cd04448    10 STGIEFQDHRYRLRTYTNCILGKELVNWLIRQ-GKAATRVQAIAIGQALLdagwiecVSDDDLFRDE 75
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1714-1874 1.24e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1714 ISTPGLYGPNAHPDQPNAVSSPlvkpttaflspalrPHLIGPLASGPPSTNGFGTTGQPLNRSTVTVPVTPviqDPEVIK 1793
Cdd:pfam05109  434 LNTTGFAAPNTTTGLPSSTHVP--------------TNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP---SPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295  1794 DELESFCRDRSALEAfyrellerEAHPPAPNTTPGLAPVKIPSTTATKDS------TLAFATPHLGAGQNTTSTGHTVPD 1867
Cdd:pfam05109  497 NGTESKAPDMTSPTS--------AVTTPTPNATSPTPAVTTPTPNATSPTlgktspTSAVTTPTPNATSPTPAVTTPTPN 568


                   ....*..
gi 758993295  1868 TNIPSLG 1874
Cdd:pfam05109  569 ATIPTLG 575
DEP_RGS7-like cd04450
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in RGS (regulator of G-protein ...
 1329-1379 1.39e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in RGS (regulator of G-protein signaling) proteins of the subfamily R7. This subgroup contains RGS7, RGS6, RGS9 and RGS11. They share a common domain architecture, containing, beside the RGS domain, a DEP domain and a GGL (G-protein gamma subunit-like ) domain. RGS proteins are GTPase-activating (GAP) proteins of heterotrimeric G proteins by increasing the rate of GTP hydrolysis of the alpha subunit. The fungal homologs, like yeast Sst2, share a related common domain architecture, containing RGS and DEP domains. Sst2 has been identified as the principal regulator of mating pheromone signaling and recently the DEP domain of Sst2 has been shown to be necessary and sufficient to mediate receptor interaction.


Pssm-ID: 239897  Cd Length: 88  Bit Score: 39.58  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 758993295 1329 VENGGIRMQNRRWHLRLHYNCFIGSDMTTWLLENFeDLEDREEAEELGNRL 1379
Cdd:cd04450     8 DSEVGVRMRTEKSFLTTVPYAFTGKAIVQWLMDCT-DVVDPSEALEIAALF 57
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
 1336-1419 4.77e-03

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: 37.93  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758993295 1336 MQNRRWHLRLHYNCFIGSDMTTWLLENFEdLEDREEAEELGNRLMVTsddkskdeskdgrkdggGLFVHVERRHPFRDGQ 1415
Cdd:cd04439    15 IKDRRRKLSTFPKCFLGNEFVSWLLEIGE-ISKPEEGVNLGQALLEN-----------------GIIHHVSDKHQFKNEQ 76


                  ....
gi 758993295 1416 YFYQ 1419
Cdd:cd04439    77 VLYR 80
 
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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