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Conserved domains on  [gi|1907112246|ref|XP_036015273|]
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rap guanine nucleotide exchange factor 3 isoform X11 [Mus musculus]

Protein Classification

Ras-GEF domain-containing protein( domain architecture ID 10858397)

Ras guanine nucleotide exchange factor (Ras-GEF) domain-containing protein activates Ras-like small GTPases by mediating the replacement of GDP with GTP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
622-890 8.87e-82

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 263.34  E-value: 8.87e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  622 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 701
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKID---PSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  702 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL-SPPVIP 780
Cdd:smart00147  78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  781 FMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRShSTAPLSPLRsrvSHIHEDSQGSRIstcseqslst 859
Cdd:smart00147 158 FLGVLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQS-QPYNLRPNR---SDIQSLLQQLLD---------- 223

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112246  860 rspastwayvqqlkVIDNQRELSRLSRELEP 890
Cdd:smart00147 224 --------------HLDEEEELYQLSLKIEP 240
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 58-184 4.41e-54

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: 183.31  E-value: 4.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  58 AGKLLHRHLLATYPTLIRDRKYHLRLYRHCCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHgspVKHDWTFQD 137
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH---VDQELHFQD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907112246 138 RDaQFYRFPGPEPEPTGTQ--DVEEELVEAMALLSQRGPDALLTVALRK 184
Cdd:cd04437    78 KY-QFYRFSDDECSPAPLEkrEAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 348-457 1.32e-18

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: 81.97  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 348 TVMSGTPEKILELLLEAMRpdssahDPTETFLSDFLLTHSVFMPSTQLFTALLHHFHVEPADPAGGSEQEHSTYICNKRQ 427
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907112246 428 QILRLVGRWVALYSPMLHSDPVATSFLQKL 457
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 208-317 6.67e-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: 80.06  E-value: 6.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 208 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 283
Cdd:cd00038     3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907112246 284 ATIILREnNCHFLRVDKQDFNRIIKDVEAKTMRL 317
Cdd:cd00038    82 ATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
622-890 8.87e-82

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 263.34  E-value: 8.87e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  622 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 701
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKID---PSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  702 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL-SPPVIP 780
Cdd:smart00147  78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  781 FMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRShSTAPLSPLRsrvSHIHEDSQGSRIstcseqslst 859
Cdd:smart00147 158 FLGVLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQS-QPYNLRPNR---SDIQSLLQQLLD---------- 223

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112246  860 rspastwayvqqlkVIDNQRELSRLSRELEP 890
Cdd:smart00147 224 --------------HLDEEEELYQLSLKIEP 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 622-857 2.49e-80

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: 259.11  E-value: 2.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 622 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 701
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIE---PFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 702 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL--SPPVI 779
Cdd:cd00155    78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 780 PFMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRS--HSTAPLSPLRSRVSHIHEDSQgsRISTCSEQS 856
Cdd:cd00155   158 PFLGVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELS 235


                  .
gi 1907112246 857 L 857
Cdd:cd00155   236 L 236
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 629-810 6.13e-67

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 220.93  E-value: 6.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 629 DLAGQLTDHDWNLFNRIHqvqEVELIHYVLGpQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQLLRKFIKL 708
Cdd:pfam00617   1 ELARQLTLIEFELFRKIK---PRELLGSAWS-KKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 709 AAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKLSPPVIPFMPLLLKD 788
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTD 156

                         170       180
                  ....*....|....*....|...
gi 1907112246 789 VTFIHEGNHTLVEN-LINFEKMR 810
Cdd:pfam00617 157 LTFIEEGNPDFLEGgLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 58-184 4.41e-54

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: 183.31  E-value: 4.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  58 AGKLLHRHLLATYPTLIRDRKYHLRLYRHCCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHgspVKHDWTFQD 137
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH---VDQELHFQD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907112246 138 RDaQFYRFPGPEPEPTGTQ--DVEEELVEAMALLSQRGPDALLTVALRK 184
Cdd:cd04437    78 KY-QFYRFSDDECSPAPLEkrEAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 348-457 1.32e-18

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: 81.97  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 348 TVMSGTPEKILELLLEAMRpdssahDPTETFLSDFLLTHSVFMPSTQLFTALLHHFHVEPADPAGGSEQEHSTYICNKRQ 427
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907112246 428 QILRLVGRWVALYSPMLHSDPVATSFLQKL 457
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 353-474 1.48e-18

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: 82.46  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 353 TPEKILELLLEAMRPDSSahdpteTFLSDFLLTHSVFMPSTQLFTALLHHFHVEPaDPAGGSEQEHSTYICNKRQQILRL 432
Cdd:cd06224     1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907112246 433 VGRWVALYSPMLHSDPVATSFLQKLSDLVSRDARLSNLLREQ 474
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 208-317 6.67e-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: 80.06  E-value: 6.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 208 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 283
Cdd:cd00038     3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907112246 284 ATIILREnNCHFLRVDKQDFNRIIKDVEAKTMRL 317
Cdd:cd00038    82 ATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 69-147 1.41e-17

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: 78.09  E-value: 1.41e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112246   69 TYPTLIRDRKYHLRLYRHCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPvKHDWTFQDrDAQFYRFPG 147
Cdd:smart00049   2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNG-PNKHTFKD-SKALYRFTT 77
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 229-309 1.39e-16

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: 75.34  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 229 KAGTVLFSQGDKGTSWYIIWKGSVNVVTHG----KGLVTTLHEGDDFGQLALVNDAPRAATIILREnNCHFLRVDKQDFN 304
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALT-DSELLVIPREDFL 83


                  ....*
gi 1907112246 305 RIIKD 309
Cdd:pfam00027  84 ELLER 88
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 345-472 1.40e-15

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: 73.91  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  345 NRYTVMSGTPEKILELLLEAMrpdssaHDPTETFLSDFLLTHSVFMPSTQLFTALLHHFhvEPADPAGGSEQEHSTYICN 424
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAF------DKADPSFVETFLLTYRSFITTQELLQLLLYRY--NAIPPESWVEEKVNPRRVK 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907112246  425 KRqqILRLVGRWVALYSPMLHSDPVATSFLQKLSDLVSRDA------RLSNLLR 472
Cdd:smart00229  73 NR--VLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKypglvtSLLNLLR 124
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 208-320 1.85e-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: 1.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  208 AHLSNSVKRELAAVLlfEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 282
Cdd:smart00100   3 KNLDAEELRELADAL--EPVRyPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907112246  283 AATIILREnnCHFLRVDKQDFNRIIKDVEAKTMRLEEH 320
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 74-145 6.71e-13

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: 64.53  E-value: 6.71e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112246  74 IRDRKYHLRLYRHCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPVKHdwTFQDrDAQFYRF 145
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKHG--LFKD-SYYFYRF 71
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 208-309 1.47e-08

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: 55.76  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 208 AHLSNSVKRELAAvlLFEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 282
Cdd:COG0664     2 AGLSDEELEALLA--HLELRTlKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1907112246 283 AATIILREnNCHFLRVDKQDFNRIIKD 309
Cdd:COG0664    80 PATAEALE-DSELLRIPREDLEELLER 105
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
622-890 8.87e-82

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 263.34  E-value: 8.87e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  622 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 701
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKID---PSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  702 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL-SPPVIP 780
Cdd:smart00147  78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  781 FMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRShSTAPLSPLRsrvSHIHEDSQGSRIstcseqslst 859
Cdd:smart00147 158 FLGVLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQS-QPYNLRPNR---SDIQSLLQQLLD---------- 223

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112246  860 rspastwayvqqlkVIDNQRELSRLSRELEP 890
Cdd:smart00147 224 --------------HLDEEEELYQLSLKIEP 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 622-857 2.49e-80

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: 259.11  E-value: 2.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 622 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 701
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIE---PFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 702 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL--SPPVI 779
Cdd:cd00155    78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 780 PFMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRS--HSTAPLSPLRSRVSHIHEDSQgsRISTCSEQS 856
Cdd:cd00155   158 PFLGVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELS 235


                  .
gi 1907112246 857 L 857
Cdd:cd00155   236 L 236
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 629-810 6.13e-67

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 220.93  E-value: 6.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 629 DLAGQLTDHDWNLFNRIHqvqEVELIHYVLGpQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQLLRKFIKL 708
Cdd:pfam00617   1 ELARQLTLIEFELFRKIK---PRELLGSAWS-KKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 709 AAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKLSPPVIPFMPLLLKD 788
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTD 156

                         170       180
                  ....*....|....*....|...
gi 1907112246 789 VTFIHEGNHTLVEN-LINFEKMR 810
Cdd:pfam00617 157 LTFIEEGNPDFLEGgLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 58-184 4.41e-54

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: 183.31  E-value: 4.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  58 AGKLLHRHLLATYPTLIRDRKYHLRLYRHCCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHgspVKHDWTFQD 137
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH---VDQELHFQD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907112246 138 RDaQFYRFPGPEPEPTGTQ--DVEEELVEAMALLSQRGPDALLTVALRK 184
Cdd:cd04437    78 KY-QFYRFSDDECSPAPLEkrEAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 348-457 1.32e-18

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: 81.97  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 348 TVMSGTPEKILELLLEAMRpdssahDPTETFLSDFLLTHSVFMPSTQLFTALLHHFHVEPADPAGGSEQEHSTYICNKRQ 427
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907112246 428 QILRLVGRWVALYSPMLHSDPVATSFLQKL 457
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 353-474 1.48e-18

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: 82.46  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 353 TPEKILELLLEAMRPDSSahdpteTFLSDFLLTHSVFMPSTQLFTALLHHFHVEPaDPAGGSEQEHSTYICNKRQQILRL 432
Cdd:cd06224     1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907112246 433 VGRWVALYSPMLHSDPVATSFLQKLSDLVSRDARLSNLLREQ 474
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 208-317 6.67e-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: 80.06  E-value: 6.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 208 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 283
Cdd:cd00038     3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907112246 284 ATIILREnNCHFLRVDKQDFNRIIKDVEAKTMRL 317
Cdd:cd00038    82 ATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 69-147 1.41e-17

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: 78.09  E-value: 1.41e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112246   69 TYPTLIRDRKYHLRLYRHCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPvKHDWTFQDrDAQFYRFPG 147
Cdd:smart00049   2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNG-PNKHTFKD-SKALYRFTT 77
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 229-309 1.39e-16

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: 75.34  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 229 KAGTVLFSQGDKGTSWYIIWKGSVNVVTHG----KGLVTTLHEGDDFGQLALVNDAPRAATIILREnNCHFLRVDKQDFN 304
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALT-DSELLVIPREDFL 83


                  ....*
gi 1907112246 305 RIIKD 309
Cdd:pfam00027  84 ELLER 88
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 61-144 4.07e-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: 4.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  61 LLHRHLLATYPTLIRDRKYHLRLYRHCCSGRELVDGILALGLGVhSRSQAVGICQVLLDEGALCHGSPVKHdwTFQDrDA 140
Cdd:cd04371     2 LVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVSDDKH--TFRD-SY 77


                  ....
gi 1907112246 141 QFYR 144
Cdd:cd04371    78 ALYR 81
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 345-472 1.40e-15

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: 73.91  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  345 NRYTVMSGTPEKILELLLEAMrpdssaHDPTETFLSDFLLTHSVFMPSTQLFTALLHHFhvEPADPAGGSEQEHSTYICN 424
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAF------DKADPSFVETFLLTYRSFITTQELLQLLLYRY--NAIPPESWVEEKVNPRRVK 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907112246  425 KRqqILRLVGRWVALYSPMLHSDPVATSFLQKLSDLVSRDA------RLSNLLR 472
Cdd:smart00229  73 NR--VLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKypglvtSLLNLLR 124
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 208-320 1.85e-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: 1.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  208 AHLSNSVKRELAAVLlfEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 282
Cdd:smart00100   3 KNLDAEELRELADAL--EPVRyPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907112246  283 AATIILREnnCHFLRVDKQDFNRIIKDVEAKTMRLEEH 320
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 74-145 6.71e-13

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: 64.53  E-value: 6.71e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112246  74 IRDRKYHLRLYRHCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPVKHdwTFQDrDAQFYRF 145
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKHG--LFKD-SYYFYRF 71
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 208-309 1.47e-08

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: 55.76  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246 208 AHLSNSVKRELAAvlLFEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 282
Cdd:COG0664     2 AGLSDEELEALLA--HLELRTlKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1907112246 283 AATIILREnNCHFLRVDKQDFNRIIKD 309
Cdd:COG0664    80 PATAEALE-DSELLRIPREDLEELLER 105
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 73-142 8.20e-07

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) PIKfyve-like proteins. PIKfyve contains N-terminal Fyve finger and DEP domains, a central chaperonin-like domain and a C-terminal PIPK (phosphatidylinositol phosphate kinase) domain. PIKfyve-like proteins are important phosphatidylinositol (3)-monophosphate (PtdIns(3)P)-5-kinases, producing PtdIns(3,5)P2, which plays a major role in multivesicular body (MVB) sorting and control of retrograde traffic from the vacuole back to the endosome and/or Golgi. PIKfyve itself has been shown to be play a role in regulating early-endosome-to-trans-Golgi network (TGN) retrograde trafficking.


Pssm-ID: 239895  Cd Length: 81  Bit Score: 47.44  E-value: 8.20e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  73 LIRDRKYHLRLYRHCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALchgSPVKHDWTFQDRDAQF 142
Cdd:cd04448    14 EFQDHRYRLRTYTNCILGKELVNWLIRQGK-AATRVQAIAIGQALLDAGWI---ECVSDDDLFRDEYALY 79
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 73-145 3.85e-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: 39.88  E-value: 3.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907112246  73 LIRDRKYHLRLYRHCCSGRELVDGILAlglgvHS----RSQAVGICQVLLDEGALCHGSpvkhDWTFQDRDAQ-FYRF 145
Cdd:cd04442    14 VIKDRRHHLRTYPNCFVGKELIDWLIE-----HKeasdRETAIKIMQKLLDHSIIHHVC----DEHKEFKDAKlFYRF 82
DEP_DEPDC4 cd04446
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC4-like proteins. DEPDC4 is a ...
 74-144 6.12e-04

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: 39.65  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  74 IRDRKYHLRLYRHCCSGRELVDGILA-------LGLGVHSRSQAVGICQVLLDE------GALCHGSpvKHDWTFQDRDA 140
Cdd:cd04446    14 VKKRRHNLKSYHDCFLGSEAVDVVLAhlmqnkyFGDVDVPRAKAVRLCQALMDCrvfeavGTKVFKK--KKRAVFEDSSS 91


                  ....
gi 1907112246 141 QFYR 144
Cdd:cd04446    92 SLYR 95
DEP_2_P-Rex cd04440
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex ...
 53-145 1.92e-03

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


Pssm-ID: 239887  Cd Length: 93  Bit Score: 38.37  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  53 EHVHKAGKLLHRHLLATYPTLIRDRKYHLRLYRHCCSGRELVDGILALGlGVHSRSQAVGICQVLLDEGALCHGSPVKHd 132
Cdd:cd04440     3 EDIMSKGVRLYCRLHSLFTPVVKDRDYHLKTYKSVVPASKLVDWLLAQG-DCRTREEAVILGVGLCNNGFMHHVLEKSE- 80

                          90
                  ....*....|...
gi 1907112246 133 wtFQDrDAQFYRF 145
Cdd:cd04440    81 --FKD-EPLLFRF 90
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
 73-145 5.78e-03

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: 36.54  E-value: 5.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907112246  73 LIRDRKYHLRLYRHCCSGRELVDGILALGLGVhSRSQAVGICQVLLDEGALCHgspVKHDWTFQDrDAQFYRF 145
Cdd:cd04443    16 IVKDRRCGLRTYKGVFCGCDLVSWLIEVGLAQ-DRGEAVLYGRRLLQGGVLQH---ITNEHHFRD-ENLLYRF 83
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
 59-145 9.40e-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: 36.01  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112246  59 GKLLHrHLLATYPTLIRDRKYHLRLYRHCCSGRELVDGILALGlGVHSRSQAVGICQVLLDEGALCHGSPvKHDWTfqdR 138
Cdd:cd04439     1 GEKLY-KMMCKQGSLIKDRRRKLSTFPKCFLGNEFVSWLLEIG-EISKPEEGVNLGQALLENGIIHHVSD-KHQFK---N 74


                  ....*..
gi 1907112246 139 DAQFYRF 145
Cdd:cd04439    75 EQVLYRF 81
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 73-127 9.53e-03

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: 36.10  E-value: 9.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907112246  73 LIRDRKYHLRLYRHCCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHGS 127
Cdd:cd04449    15 GIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVS 69
 
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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