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Conserved domains on  [gi|1907087262|ref|XP_036013266|]
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rap guanine nucleotide exchange factor 5 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
141-264 1.10e-60

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: 196.41  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 141 AGRALRNIIILQAADLVKDRVNLKGFYRRSCVGSELVDWLLEHCPFVQCRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYV 220
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907087262 221 FYQFSSDECSYLY-CEFEREEEWQKGVKLLLELVHLIPARAGICD 264
Cdd:cd04437    81 FYRFSDDECSPAPlEKREAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
410-514 2.76e-23

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


:

Pssm-ID: 214571  Cd Length: 127  Bit Score: 95.48  E-value: 2.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262  410 RYVVVSGTPEKILEHLLndlhlaEVQHKETETLLDDFLLTYTVFMTTDDLCQALLRHYSAKKYQ-GEEENSDVPCRKRKV 488
Cdd:smart00229   2 GGLIKGGTLEALIEHLT------EAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPEsWVEEKVNPRRVKNRV 75
                           90       100
                   ....*....|....*....|....*.
gi 1907087262  489 LHLVSQWISLYKDWLHEDEHSKMFLK 514
Cdd:smart00229  76 LNILRTWVENYWEDFEDDPKLISFLL 101
 
Name Accession Description Interval E-value
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
141-264 1.10e-60

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: 196.41  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 141 AGRALRNIIILQAADLVKDRVNLKGFYRRSCVGSELVDWLLEHCPFVQCRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYV 220
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907087262 221 FYQFSSDECSYLY-CEFEREEEWQKGVKLLLELVHLIPARAGICD 264
Cdd:cd04437    81 FYRFSDDECSPAPlEKREAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
410-514 2.76e-23

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 95.48  E-value: 2.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262  410 RYVVVSGTPEKILEHLLndlhlaEVQHKETETLLDDFLLTYTVFMTTDDLCQALLRHYSAKKYQ-GEEENSDVPCRKRKV 488
Cdd:smart00229   2 GGLIKGGTLEALIEHLT------EAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPEsWVEEKVNPRRVKNRV 75
                           90       100
                   ....*....|....*....|....*.
gi 1907087262  489 LHLVSQWISLYKDWLHEDEHSKMFLK 514
Cdd:smart00229  76 LNILRTWVENYWEDFEDDPKLISFLL 101
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
417-547 1.32e-15

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 73.22  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 417 TPEKILEHLLNDLHLAEvqhketETLLDDFLLTYTVFMTTDDLCQALLRHY-----SAKKYQGEEENSDVPCRKRkVLHL 491
Cdd:cd06224     1 TLEALIEHLTSTFDMPD------PSFVSTFLLTYRSFTTPTELLEKLIERYeiappENLEYNDWDKKKSKPIRLR-VLNV 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087262 492 VSQWISLYKDWLHEDEHSKMFLKscrysllrsELLVDVCSSQLRDVCFQHLLQSLK 547
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLE---------EFLNRLVQEGALLQELKKLLRKLL 120
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
157-224 5.33e-15

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: 69.92  E-value: 5.33e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907087262 157 VKDRVNLKGFYRRSCVGSELVDWLLEHCPfVQCRSMAIGVWQLLLDMGIMSSV-DQHLYFQDNYVFYQF 224
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVgDKHGLFKDSYYFYRF 71
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
412-499 6.94e-13

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


Pssm-ID: 459873  Cd Length: 104  Bit Score: 65.02  E-value: 6.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 412 VVVSGTPEKILEHLLNDLHLAEvqhketETLLDDFLLTYTVFMTTDDLCQALLRHY----SAKKYQGEEENSDV--PCRK 485
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLD------DSFLSTFLLTYRSFTTPAELLELLIERYnippPLDLSSDSYWISKKtlPIRI 74
                          90
                  ....*....|....
gi 1907087262 486 RkVLHLVSQWISLY 499
Cdd:pfam00618  75 R-VLSVLRHWVENY 87
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
157-226 1.62e-11

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: 59.99  E-value: 1.62e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907087262  157 VKDRVNLKGFYRRSCVGSELVDWLLEHCPfVQCRSMAIGVWQLLLDMGIMSSVDQH--LYFQDNYVFYQFSS 226
Cdd:smart00049   7 LRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPnkHTFKDSKALYRFTT 77
 
Name Accession Description Interval E-value
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
141-264 1.10e-60

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: 196.41  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 141 AGRALRNIIILQAADLVKDRVNLKGFYRRSCVGSELVDWLLEHCPFVQCRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYV 220
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907087262 221 FYQFSSDECSYLY-CEFEREEEWQKGVKLLLELVHLIPARAGICD 264
Cdd:cd04437    81 FYRFSDDECSPAPlEKREAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
410-514 2.76e-23

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 95.48  E-value: 2.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262  410 RYVVVSGTPEKILEHLLndlhlaEVQHKETETLLDDFLLTYTVFMTTDDLCQALLRHYSAKKYQ-GEEENSDVPCRKRKV 488
Cdd:smart00229   2 GGLIKGGTLEALIEHLT------EAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPEsWVEEKVNPRRVKNRV 75
                           90       100
                   ....*....|....*....|....*.
gi 1907087262  489 LHLVSQWISLYKDWLHEDEHSKMFLK 514
Cdd:smart00229  76 LNILRTWVENYWEDFEDDPKLISFLL 101
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
143-223 2.78e-16

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: 73.91  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 143 RALRNIIILQAADLVKDRVNLKGFYRRSCVGSELVDWLLEHCPfVQCRSMAIGVWQLLLDMGIMSSV-DQHLYFQDNYVF 221
Cdd:cd04371     1 DLVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLE-AITREEAVELGQALLKHGLIHHVsDDKHTFRDSYAL 79

                  ..
gi 1907087262 222 YQ 223
Cdd:cd04371    80 YR 81
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
417-547 1.32e-15

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 73.22  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 417 TPEKILEHLLNDLHLAEvqhketETLLDDFLLTYTVFMTTDDLCQALLRHY-----SAKKYQGEEENSDVPCRKRkVLHL 491
Cdd:cd06224     1 TLEALIEHLTSTFDMPD------PSFVSTFLLTYRSFTTPTELLEKLIERYeiappENLEYNDWDKKKSKPIRLR-VLNV 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087262 492 VSQWISLYKDWLHEDEHSKMFLKscrysllrsELLVDVCSSQLRDVCFQHLLQSLK 547
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLE---------EFLNRLVQEGALLQELKKLLRKLL 120
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
157-224 5.33e-15

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: 69.92  E-value: 5.33e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907087262 157 VKDRVNLKGFYRRSCVGSELVDWLLEHCPfVQCRSMAIGVWQLLLDMGIMSSV-DQHLYFQDNYVFYQF 224
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVgDKHGLFKDSYYFYRF 71
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
412-499 6.94e-13

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


Pssm-ID: 459873  Cd Length: 104  Bit Score: 65.02  E-value: 6.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 412 VVVSGTPEKILEHLLNDLHLAEvqhketETLLDDFLLTYTVFMTTDDLCQALLRHY----SAKKYQGEEENSDV--PCRK 485
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLD------DSFLSTFLLTYRSFTTPAELLELLIERYnippPLDLSSDSYWISKKtlPIRI 74
                          90
                  ....*....|....
gi 1907087262 486 RkVLHLVSQWISLY 499
Cdd:pfam00618  75 R-VLSVLRHWVENY 87
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
157-226 1.62e-11

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: 59.99  E-value: 1.62e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907087262  157 VKDRVNLKGFYRRSCVGSELVDWLLEHCPfVQCRSMAIGVWQLLLDMGIMSSVDQH--LYFQDNYVFYQFSS 226
Cdd:smart00049   7 LRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNGPnkHTFKDSKALYRFTT 77
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
141-224 7.82e-09

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: 52.59  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 141 AGRALRniIILQAADLVKDRVNLKGFYRRSCVGSELVDWLLEHCPFVQcRSMAIGVWQLLLDMGIMSSV-DQHLYFQDNY 219
Cdd:cd04442     1 TGEQLR--LRLHEAKVIKDRRHHLRTYPNCFVGKELIDWLIEHKEASD-RETAIKIMQKLLDHSIIHHVcDEHKEFKDAK 77

                  ....*
gi 1907087262 220 VFYQF 224
Cdd:cd04442    78 LFYRF 82
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
167-224 6.64e-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: 44.34  E-value: 6.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907087262 167 YRRSCVGSELVDWLLEHCPfVQCRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYVFYQF 224
Cdd:cd04441    29 YERTFVGSEFIDWLLQEGE-AESRREAVQLCRRLLEHGIIQHVSNKHHFFDSNLLYQF 85
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
154-224 1.44e-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: 43.47  E-value: 1.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907087262 154 ADLVKDRVNLKGFYRRSCVGSELVDWLLEhCPFVQCRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYVFYQF 224
Cdd:cd04443    14 QDIVKDRRCGLRTYKGVFCGCDLVSWLIE-VGLAQDRGEAVLYGRRLLQGGVLQHITNEHHFRDENLLYRF 83
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
151-224 1.77e-05

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: 43.03  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087262 151 LQAADLVKDRVNLKGFYRR-------SC-VGSELVDWLLEHCPFVQCRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYVFY 222
Cdd:cd04449     2 AEIAEAMRDPSGIGIFDRSwhkglpsNCfIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFYFY 81

                  ..
gi 1907087262 223 QF 224
Cdd:cd04449    82 YI 83
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
167-223 5.45e-05

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: 41.66  E-value: 5.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907087262 167 YRRSCVGSELVDWLLEHCPFVQcRSMAIGVWQLLLDMGIMSSVDQHLYFQDNYVFYQ 223
Cdd:cd04448    25 YTNCILGKELVNWLIRQGKAAT-RVQAIAIGQALLDAGWIECVSDDDLFRDEYALYK 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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