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Conserved domains on  [gi|767972825|ref|XP_011536057|]
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rap guanine nucleotide exchange factor 3 isoform X2 [Homo sapiens]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 10138341)

Ras guanine nucleotide exchange factor (Ras-GEF) domain-containing protein activates Ras-like small GTPases by mediating the replacement of GDP with GTP| RasGEF domain-containing protein may function as a guanine nucleotide exchange factor for Ras-like small GTPases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 631-863 1.71e-78

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


:

Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 254.48  E-value: 1.71e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 631 LDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRK 710
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 711 FIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKL--SPPVIPFM 788
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767972825 789 PLLLKDMTFIHEGNHTLVE-NLINFEKMRMMARAARMLHHCRS--HNPVPLSPLRSRVSHLHEDSQvaRISTCSEQSL 863
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELSL 236
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 58-196 5.49e-56

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: 188.71  E-value: 5.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  58 AGRQLHRHLLATCPNLIRDRKYHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHasissppprlgl 137
Cdd:cd04437    1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767972825 138 cppVKHDWAFQDRDaQFYRFPGPEPE--PVRTHEMEEELAEAVALLSQRGPDALLTVALRK 196
Cdd:cd04437   69 ---VDQELHFQDKY-QFYRFSDDECSpaPLEKREAEEELQEAVTLLSQLGPDALLRMILRK 125
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 365-484 9.08e-22

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: 91.32  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 365 TPEKILELLLEAMGPDSSahdpteTFLSDFLLTHRVFMPSAQLCAALLHHFHVEP--AGGSEQERSTYVCNKRQQILRLV 442
Cdd:cd06224    1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAPpeNLEYNDWDKKKSKPIRLRVLNVL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767972825 443 SQWVALYGSMLHTDPVATSFLQKLSDLVGRDTRLSNLLREQW 484
Cdd:cd06224   75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLL 116
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 220-329 1.07e-18

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 82.37  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 220 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 295
Cdd:cd00038    3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767972825 296 ATIILREDnCHFLRVDKQDFNRIIKDVEAKTMRL 329
Cdd:cd00038   82 ATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 631-863 1.71e-78

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 254.48  E-value: 1.71e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 631 LDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRK 710
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 711 FIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKL--SPPVIPFM 788
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767972825 789 PLLLKDMTFIHEGNHTLVE-NLINFEKMRMMARAARMLHHCRS--HNPVPLSPLRSRVSHLHEDSQvaRISTCSEQSL 863
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELSL 236
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
631-896 3.69e-77

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 251.01  E-value: 3.69e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   631 LDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRK 710
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   711 FIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKL-SPPVIPFMP 789
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   790 LLLKDMTFIHEGNHTLVE-NLINFEKMRMMARAARMLHHCRSHNPvplsplrsRVSHLHEDSQVaristcseqslstrsp 868
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQSQPY--------NLRPNRSDIQS---------------- 216

                          250       260
                   ....*....|....*....|....*....
gi 767972825   869 astwaYVQQLK-VIDNQRELSRLSRELEP 896
Cdd:smart00147 217 -----LLQQLLdHLDEEEELYQLSLKIEP 240
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 638-814 1.52e-67

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


Pssm-ID: 459872  Cd Length: 179  Bit Score: 222.47  E-value: 1.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  638 DLAGQLTDHDWSLFNSIHQVELIHYVLGpQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRKFIKLAAH 717
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWS-KKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  718 LKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTF 797
Cdd:pfam00617  80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTF 159

                         170
                  ....*....|....*...
gi 767972825  798 IHEGNHTLVEN-LINFEK 814
Cdd:pfam00617 160 IEEGNPDFLEGgLINFEK 177
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 58-196 5.49e-56

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: 188.71  E-value: 5.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  58 AGRQLHRHLLATCPNLIRDRKYHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHasissppprlgl 137
Cdd:cd04437    1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767972825 138 cppVKHDWAFQDRDaQFYRFPGPEPE--PVRTHEMEEELAEAVALLSQRGPDALLTVALRK 196
Cdd:cd04437   69 ---VDQELHFQDKY-QFYRFSDDECSpaPLEKREAEEELQEAVTLLSQLGPDALLRMILRK 125
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 365-484 9.08e-22

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: 91.32  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 365 TPEKILELLLEAMGPDSSahdpteTFLSDFLLTHRVFMPSAQLCAALLHHFHVEP--AGGSEQERSTYVCNKRQQILRLV 442
Cdd:cd06224    1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAPpeNLEYNDWDKKKSKPIRLRVLNVL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767972825 443 SQWVALYGSMLHTDPVATSFLQKLSDLVGRDTRLSNLLREQW 484
Cdd:cd06224   75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLL 116
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 360-466 2.02e-21

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: 89.67  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  360 TVMSGTPEKILELLLEAMGpdssahDPTETFLSDFLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQE---RSTYVCNKRQ 436
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDsywISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 767972825  437 QILRLVSQWVALYGSMLHTDPVATSFLQKL 466
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 357-481 5.95e-20

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: 86.62  E-value: 5.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   357 NRYTVMSGTPEKILELLLEAMgpdssaHDPTETFLSDFLLTHRVFMPSAQLCAALLHHFHVEPaGGSEQERSTYVCNKRQ 436
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAF------DKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIP-PESWVEEKVNPRRVKN 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767972825   437 QILRLVSQWVALYGSMLHTDPVATSFLQKLSDLVGRD------TRLSNLLR 481
Cdd:smart00229  74 RVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEkypglvTSLLNLLR 124
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 220-329 1.07e-18

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 82.37  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 220 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 295
Cdd:cd00038    3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767972825 296 ATIILREDnCHFLRVDKQDFNRIIKDVEAKTMRL 329
Cdd:cd00038   82 ATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 241-321 3.03e-17

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 77.26  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  241 KAGTVLFSQGDKGTSWYIIWKGSVNVVTHG----KGLVTTLHEGDDFGQLALVNDAPRAATIILREDnCHFLRVDKQDFN 316
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALTD-SELLVIPREDFL 83


                  ....*
gi 767972825  317 RIIKD 321
Cdd:pfam00027  84 ELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 220-332 2.12e-14

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 70.51  E-value: 2.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   220 AHLSNSVKRELAAVLlfEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 294
Cdd:smart00100   3 KNLDAEELRELADAL--EPVRyPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767972825   295 AATIILREdnCHFLRVDKQDFNRIIKDVEAKTMRLEEH 332
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 74-159 1.49e-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: 66.54  E-value: 1.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825    74 IRDRKYHLRLYRQCCSGRELVDGILALGLgVHSRSQVVGICQVLLDEGALCHASissppprlglcppVKHDWAFQDrDAQ 153
Cdd:smart00049   7 LRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVN-------------GPNKHTFKD-SKA 71


                   ....*.
gi 767972825   154 FYRFPG 159
Cdd:smart00049  72 LYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 74-157 2.44e-10

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: 57.21  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   74 IRDRKYHLRLYRQCCSGRELVDGILALGLgVHSRSQVVGICQVLLDEGALCHASissppprlglcppvKHDWAFQDrDAQ 153
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVG--------------DKHGLFKD-SYY 67


                  ....
gi 767972825  154 FYRF 157
Cdd:pfam00610  68 FYRF 71
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 220-321 2.84e-09

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 58.07  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 220 AHLSNSVKRELAAvlLFEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 294
Cdd:COG0664    2 AGLSDEELEALLA--HLELRTlKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....*..
gi 767972825 295 AATIILREDnCHFLRVDKQDFNRIIKD 321
Cdd:COG0664   80 PATAEALED-SELLRIPREDLEELLER 105
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 631-863 1.71e-78

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 254.48  E-value: 1.71e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 631 LDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRK 710
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 711 FIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKL--SPPVIPFM 788
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767972825 789 PLLLKDMTFIHEGNHTLVE-NLINFEKMRMMARAARMLHHCRS--HNPVPLSPLRSRVSHLHEDSQvaRISTCSEQSL 863
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELSL 236
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
631-896 3.69e-77

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 251.01  E-value: 3.69e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   631 LDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRK 710
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   711 FIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKL-SPPVIPFMP 789
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   790 LLLKDMTFIHEGNHTLVE-NLINFEKMRMMARAARMLHHCRSHNPvplsplrsRVSHLHEDSQVaristcseqslstrsp 868
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQSQPY--------NLRPNRSDIQS---------------- 216

                          250       260
                   ....*....|....*....|....*....
gi 767972825   869 astwaYVQQLK-VIDNQRELSRLSRELEP 896
Cdd:smart00147 217 -----LLQQLLdHLDEEEELYQLSLKIEP 240
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 638-814 1.52e-67

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


Pssm-ID: 459872  Cd Length: 179  Bit Score: 222.47  E-value: 1.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  638 DLAGQLTDHDWSLFNSIHQVELIHYVLGpQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRKFIKLAAH 717
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWS-KKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  718 LKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTF 797
Cdd:pfam00617  80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTF 159

                         170
                  ....*....|....*...
gi 767972825  798 IHEGNHTLVEN-LINFEK 814
Cdd:pfam00617 160 IEEGNPDFLEGgLINFEK 177
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 58-196 5.49e-56

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: 188.71  E-value: 5.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  58 AGRQLHRHLLATCPNLIRDRKYHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHasissppprlgl 137
Cdd:cd04437    1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767972825 138 cppVKHDWAFQDRDaQFYRFPGPEPE--PVRTHEMEEELAEAVALLSQRGPDALLTVALRK 196
Cdd:cd04437   69 ---VDQELHFQDKY-QFYRFSDDECSpaPLEKREAEEELQEAVTLLSQLGPDALLRMILRK 125
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 365-484 9.08e-22

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: 91.32  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 365 TPEKILELLLEAMGPDSSahdpteTFLSDFLLTHRVFMPSAQLCAALLHHFHVEP--AGGSEQERSTYVCNKRQQILRLV 442
Cdd:cd06224    1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAPpeNLEYNDWDKKKSKPIRLRVLNVL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767972825 443 SQWVALYGSMLHTDPVATSFLQKLSDLVGRDTRLSNLLREQW 484
Cdd:cd06224   75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLL 116
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 360-466 2.02e-21

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: 89.67  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  360 TVMSGTPEKILELLLEAMGpdssahDPTETFLSDFLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQE---RSTYVCNKRQ 436
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDsywISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 767972825  437 QILRLVSQWVALYGSMLHTDPVATSFLQKL 466
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 357-481 5.95e-20

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: 86.62  E-value: 5.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   357 NRYTVMSGTPEKILELLLEAMgpdssaHDPTETFLSDFLLTHRVFMPSAQLCAALLHHFHVEPaGGSEQERSTYVCNKRQ 436
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAF------DKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIP-PESWVEEKVNPRRVKN 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767972825   437 QILRLVSQWVALYGSMLHTDPVATSFLQKLSDLVGRD------TRLSNLLR 481
Cdd:smart00229  74 RVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEkypglvTSLLNLLR 124
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 220-329 1.07e-18

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 82.37  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 220 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 295
Cdd:cd00038    3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767972825 296 ATIILREDnCHFLRVDKQDFNRIIKDVEAKTMRL 329
Cdd:cd00038   82 ATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 241-321 3.03e-17

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 77.26  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  241 KAGTVLFSQGDKGTSWYIIWKGSVNVVTHG----KGLVTTLHEGDDFGQLALVNDAPRAATIILREDnCHFLRVDKQDFN 316
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALTD-SELLVIPREDFL 83


                  ....*
gi 767972825  317 RIIKD 321
Cdd:pfam00027  84 ELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 220-332 2.12e-14

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 70.51  E-value: 2.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   220 AHLSNSVKRELAAVLlfEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 294
Cdd:smart00100   3 KNLDAEELRELADAL--EPVRyPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767972825   295 AATIILREdnCHFLRVDKQDFNRIIKDVEAKTMRLEEH 332
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 74-159 1.49e-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: 66.54  E-value: 1.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825    74 IRDRKYHLRLYRQCCSGRELVDGILALGLgVHSRSQVVGICQVLLDEGALCHASissppprlglcppVKHDWAFQDrDAQ 153
Cdd:smart00049   7 LRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVN-------------GPNKHTFKD-SKA 71


                   ....*.
gi 767972825   154 FYRFPG 159
Cdd:smart00049  72 LYRFTT 77
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 61-156 1.24e-12

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: 63.90  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  61 QLHRHLLATCPNL-IRDRKYHLRLYRQCCSGRELVDGILALGLGVhSRSQVVGICQVLLDEGALCHASissppprlglcp 139
Cdd:cd04371    1 DLVRIMLDSDSGVpIKDRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVS------------ 67

                         90
                 ....*....|....*..
gi 767972825 140 pvKHDWAFQDrDAQFYR 156
Cdd:cd04371   68 --DDKHTFRD-SYALYR 81
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 74-157 2.44e-10

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: 57.21  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825   74 IRDRKYHLRLYRQCCSGRELVDGILALGLgVHSRSQVVGICQVLLDEGALCHASissppprlglcppvKHDWAFQDrDAQ 153
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVG--------------DKHGLFKD-SYY 67


                  ....
gi 767972825  154 FYRF 157
Cdd:pfam00610  68 FYRF 71
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 220-321 2.84e-09

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 58.07  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825 220 AHLSNSVKRELAAvlLFEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 294
Cdd:COG0664    2 AGLSDEELEALLA--HLELRTlKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....*..
gi 767972825 295 AATIILREDnCHFLRVDKQDFNRIIKD 321
Cdd:COG0664   80 PATAEALED-SELLRIPREDLEELLER 105
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 73-154 1.19e-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: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767972825  73 LIRDRKYHLRLYRQCCSGRELVDGILALGLgVHSRSQVVGICQVLLDEGALchasissppprlglcPPVKHDWAFQDRDA 152
Cdd:cd04448   14 EFQDHRYRLRTYTNCILGKELVNWLIRQGK-AATRVQAIAIGQALLDAGWI---------------ECVSDDDLFRDEYA 77


                 ..
gi 767972825 153 QF 154
Cdd:cd04448   78 LY 79
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 58-125 2.22e-03

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: 37.95  E-value: 2.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767972825  58 AGRQLHRHLLATcpNLIRDRKYHLRLYRQCCSGRELVDGILAlglgvHS----RSQVVGICQVLLDEGALCH 125
Cdd:cd04442    1 TGEQLRLRLHEA--KVIKDRRHHLRTYPNCFVGKELIDWLIE-----HKeasdRETAIKIMQKLLDHSIIHH 65
DEP_DEPDC4 cd04446
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC4-like proteins. DEPDC4 is a ...
 74-119 4.88e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC4-like proteins. DEPDC4 is a DEP domain containing protein of unknown function.


Pssm-ID: 239893  Cd Length: 95  Bit Score: 37.34  E-value: 4.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767972825  74 IRDRKYHLRLYRQCCSGRELVDGILA-------LGLGVHSRSQVVGICQVLLD 119
Cdd:cd04446   14 VKKRRHNLKSYHDCFLGSEAVDVVLAhlmqnkyFGDVDVPRAKAVRLCQALMD 66
 
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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