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Conserved domains on  [gi|1958760045|ref|XP_038960274|]
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rap guanine nucleotide exchange factor 4 isoform X4 [Rattus norvegicus]

Protein Classification

DEP_Epac and RasGEF domain-containing protein( domain architecture ID 10858397)

protein containing domains DEP_Epac, CAP_ED, REM, and RasGEF

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;
606-847 6.66e-93

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 291.84  E-value: 6.66e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  606 FELMSSKDLAYQMTTYDWELFNCVHELELIYHTFGRHNFK-KTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 684
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKsPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  685 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLE-PPLIPFMP 763
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  764 LLIKDMTFTHEGNKTFI-DNLVNFEKMRMIANTARTVRYYRSQPFNPdaaqaNKNHQDVRSYVRQL-NVIDNQRTLSQMS 841
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLeNGLVNFEKRRQIAEILREIRQLQSQPYNL-----RPNRSDIQSLLQQLlDHLDEEEELYQLS 235


                   ....*.
gi 1958760045  842 HRLEPR 847
Cdd:smart00147 236 LKIEPR 241
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 44-172 3.34e-68

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: 221.83  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  44 AGKILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYL 123
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958760045 124 FYRFLDDEHEDAPLpteeEKKECDEELQDTMLLLSQMGPDAHMRMILRK 172
Cdd:cd04437    81 FYRFSDDECSPAPL----EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 194-305 1.48e-21

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: 90.46  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 194 ALSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAP 269
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAG-EVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958760045 270 RAASIVLREDnCHFLRVDKEDFNRILRDVEANTVRL 305
Cdd:cd00038    80 RSATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 337-443 1.39e-19

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: 84.66  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 337 TVMSGTPEKILEHFLETirlepsLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTEQE---RMDYALNNKR 413
Cdd:pfam00618   1 QVKAGTLEKLVEYLTST------RIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDsywISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958760045 414 RVIRLVLQWAAMYGDLLQEDDVAMAFLEEF 443
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
606-847 6.66e-93

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 291.84  E-value: 6.66e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  606 FELMSSKDLAYQMTTYDWELFNCVHELELIYHTFGRHNFK-KTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 684
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKsPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  685 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLE-PPLIPFMP 763
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  764 LLIKDMTFTHEGNKTFI-DNLVNFEKMRMIANTARTVRYYRSQPFNPdaaqaNKNHQDVRSYVRQL-NVIDNQRTLSQMS 841
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLeNGLVNFEKRRQIAEILREIRQLQSQPYNL-----RPNRSDIQSLLQQLlDHLDEEEELYQLS 235


                   ....*.
gi 1958760045  842 HRLEPR 847
Cdd:smart00147 236 LKIEPR 241
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 606-843 1.48e-85

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: 272.59  E-value: 1.48e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 606 FELMSSKDLAYQMTTYDWELFNCVHELELIYHTFGRHNFKK-TTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 684
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 685 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYR--LTAAKLEPPLIPFM 762
Cdd:cd00155    81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRklLKSVGPNPPCVPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 763 PLLIKDMTFTHEGNKTFID-NLVNFEKMRMIANTARTVRYYRSQPFNPDAaqANKNHQDVRSYVRQlnvIDNQRTLSQMS 841
Cdd:cd00155   161 GVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSNSYELNR--DEDILAFLWKLLEL---ILNEDELYELS 235


                  ..
gi 1958760045 842 HR 843
Cdd:cd00155   236 LE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 613-790 7.90e-73

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 236.33  E-value: 7.90e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 613 DLAYQMTTYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKFIKIAAHC 692
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 693 KEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLEPPLIPFMPLLIKDMTFT 772
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                         170
                  ....*....|....*....
gi 1958760045 773 HEGNKTFI-DNLVNFEKMR 790
Cdd:pfam00617 161 EEGNPDFLeGGLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 44-172 3.34e-68

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: 221.83  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  44 AGKILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYL 123
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958760045 124 FYRFLDDEHEDAPLpteeEKKECDEELQDTMLLLSQMGPDAHMRMILRK 172
Cdd:cd04437    81 FYRFSDDECSPAPL----EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 194-305 1.48e-21

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: 90.46  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 194 ALSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAP 269
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAG-EVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958760045 270 RAASIVLREDnCHFLRVDKEDFNRILRDVEANTVRL 305
Cdd:cd00038    80 RSATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 55-129 3.32e-20

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 85.41  E-value: 3.32e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760045   55 RAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTScVHSRTQAVGMWQVLLEDGVLNHVD--QERHFQDKYLFYRFLD 129
Cdd:smart00049   2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFTT 77
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 337-443 1.39e-19

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: 84.66  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 337 TVMSGTPEKILEHFLETirlepsLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTEQE---RMDYALNNKR 413
Cdd:pfam00618   1 QVKAGTLEKLVEYLTST------RIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDsywISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958760045 414 RVIRLVLQWAAMYGDLLQEDDVAMAFLEEF 443
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 60-127 3.52e-19

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: 82.25  E-value: 3.52e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760045  60 IRDRKYHLKTYRQCCVGTELVDWMIQQTSCVhSRTQAVGMWQVLLEDGVLNHVDQERH-FQDKYLFYRF 127
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLEII-TREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 342-466 5.22e-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: 80.53  E-value: 5.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 342 TPEKILEHFLetirlePSLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTE--QERMDYALNNKRRVIRLV 419
Cdd:cd06224     1 TLEALIEHLT------STFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEynDWDKKKSKPIRLRVLNVL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958760045 420 LQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARMMVAFKEQLAELEK 466
Cdd:cd06224    75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 215-297 2.49e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 74.57  E-value: 2.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 215 HAKGGTVLFNQGEEGTSWYIILKGSVNVVIYG----KGVVCTLHEGDDFGKLALVNDAPRAASIVLREDnCHFLRVDKED 290
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALTD-SELLVIPRED 81


                  ....*..
gi 1958760045 291 FNRILRD 297
Cdd:pfam00027  82 FLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 195-308 3.66e-15

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: 72.43  E-value: 3.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  195 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 270
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAG-EVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958760045  271 AASIVLREdnCHFLRVDKEDFNRILRDVEANTVRLKEH 308
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 195-297 7.21e-12

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: 65.39  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 195 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 270
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKG-EVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1958760045 271 AASIVLREDnCHFLRVDKEDFNRILRD 297
Cdd:COG0664    80 PATAEALED-SELLRIPREDLEELLER 105
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 334-453 2.83e-11

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: 61.58  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  334 QKYTVMSGTPEKILEHFLETIRLepslneATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTeQERMDYALNNKR 413
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDK------ADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESW-VEEKVNPRRVKN 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958760045  414 RVIRLVLQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARM 453
Cdd:smart00229  74 RVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYP 113
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
220-297 5.46e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.19  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 220 TVLFNQGEEGTSWYIILKGSVNVVIY---GKGVVCT-LHEGDDFGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRIL 295
Cdd:PRK11753   29 STLIHAGEKAETLYYIVKGSVAVLIKdeeGKEMILSyLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLI 108


                  ..
gi 1958760045 296 RD 297
Cdd:PRK11753  109 QV 110
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
606-847 6.66e-93

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 291.84  E-value: 6.66e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  606 FELMSSKDLAYQMTTYDWELFNCVHELELIYHTFGRHNFK-KTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 684
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKsPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  685 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLE-PPLIPFMP 763
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  764 LLIKDMTFTHEGNKTFI-DNLVNFEKMRMIANTARTVRYYRSQPFNPdaaqaNKNHQDVRSYVRQL-NVIDNQRTLSQMS 841
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLeNGLVNFEKRRQIAEILREIRQLQSQPYNL-----RPNRSDIQSLLQQLlDHLDEEEELYQLS 235


                   ....*.
gi 1958760045  842 HRLEPR 847
Cdd:smart00147 236 LKIEPR 241
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 606-843 1.48e-85

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: 272.59  E-value: 1.48e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 606 FELMSSKDLAYQMTTYDWELFNCVHELELIYHTFGRHNFKK-TTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 684
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 685 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYR--LTAAKLEPPLIPFM 762
Cdd:cd00155    81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRklLKSVGPNPPCVPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 763 PLLIKDMTFTHEGNKTFID-NLVNFEKMRMIANTARTVRYYRSQPFNPDAaqANKNHQDVRSYVRQlnvIDNQRTLSQMS 841
Cdd:cd00155   161 GVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSNSYELNR--DEDILAFLWKLLEL---ILNEDELYELS 235


                  ..
gi 1958760045 842 HR 843
Cdd:cd00155   236 LE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 613-790 7.90e-73

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 236.33  E-value: 7.90e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 613 DLAYQMTTYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKFIKIAAHC 692
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 693 KEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLEPPLIPFMPLLIKDMTFT 772
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                         170
                  ....*....|....*....
gi 1958760045 773 HEGNKTFI-DNLVNFEKMR 790
Cdd:pfam00617 161 EEGNPDFLeGGLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 44-172 3.34e-68

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: 221.83  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  44 AGKILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYL 123
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958760045 124 FYRFLDDEHEDAPLpteeEKKECDEELQDTMLLLSQMGPDAHMRMILRK 172
Cdd:cd04437    81 FYRFSDDECSPAPL----EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 47-126 8.15e-24

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: 95.87  E-value: 8.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  47 ILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCVhSRTQAVGMWQVLLEDGVLNHVDQERH-FQDKYLFY 125
Cdd:cd04371     2 LVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVSDDKHtFRDSYALY 80


                  .
gi 1958760045 126 R 126
Cdd:cd04371    81 R 81
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 194-305 1.48e-21

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: 90.46  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 194 ALSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAP 269
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAG-EVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958760045 270 RAASIVLREDnCHFLRVDKEDFNRILRDVEANTVRL 305
Cdd:cd00038    80 RSATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 55-129 3.32e-20

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 85.41  E-value: 3.32e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760045   55 RAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTScVHSRTQAVGMWQVLLEDGVLNHVD--QERHFQDKYLFYRFLD 129
Cdd:smart00049   2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFTT 77
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 337-443 1.39e-19

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: 84.66  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 337 TVMSGTPEKILEHFLETirlepsLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTEQE---RMDYALNNKR 413
Cdd:pfam00618   1 QVKAGTLEKLVEYLTST------RIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDsywISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958760045 414 RVIRLVLQWAAMYGDLLQEDDVAMAFLEEF 443
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 60-127 3.52e-19

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: 82.25  E-value: 3.52e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760045  60 IRDRKYHLKTYRQCCVGTELVDWMIQQTSCVhSRTQAVGMWQVLLEDGVLNHVDQERH-FQDKYLFYRF 127
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLEII-TREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 342-466 5.22e-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: 80.53  E-value: 5.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 342 TPEKILEHFLetirlePSLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTE--QERMDYALNNKRRVIRLV 419
Cdd:cd06224     1 TLEALIEHLT------STFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEynDWDKKKSKPIRLRVLNVL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958760045 420 LQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARMMVAFKEQLAELEK 466
Cdd:cd06224    75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 215-297 2.49e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 74.57  E-value: 2.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 215 HAKGGTVLFNQGEEGTSWYIILKGSVNVVIYG----KGVVCTLHEGDDFGKLALVNDAPRAASIVLREDnCHFLRVDKED 290
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALTD-SELLVIPRED 81


                  ....*..
gi 1958760045 291 FNRILRD 297
Cdd:pfam00027  82 FLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 195-308 3.66e-15

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: 72.43  E-value: 3.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  195 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 270
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAG-EVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958760045  271 AASIVLREdnCHFLRVDKEDFNRILRDVEANTVRLKEH 308
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 44-127 1.79e-14

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: 69.15  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  44 AGKILRIAIlsRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTScVHSRTQAVGMWQVLLEDGVLNHV-DQERHFQDKY 122
Cdd:cd04442     1 TGEQLRLRL--HEAKVIKDRRHHLRTYPNCFVGKELIDWLIEHKE-ASDRETAIKIMQKLLDHSIIHHVcDEHKEFKDAK 77


                  ....*
gi 1958760045 123 LFYRF 127
Cdd:cd04442    78 LFYRF 82
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
 59-127 3.01e-14

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: 68.51  E-value: 3.01e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760045  59 MIRDRKYHLKTYRQCCVGTELVDWMIQqTSCVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYRF 127
Cdd:cd04443    16 IVKDRRCGLRTYKGVFCGCDLVSWLIE-VGLAQDRGEAVLYGRRLLQGGVLQHITNEHHFRDENLLYRF 83
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 59-126 8.08e-14

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: 67.47  E-value: 8.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760045  59 MIRDRKYHLKTYRQCCVGTELVDWMIQQTScVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYR 126
Cdd:cd04448    14 EFQDHRYRLRTYTNCILGKELVNWLIRQGK-AATRVQAIAIGQALLDAGWIECVSDDDLFRDEYALYK 80
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 195-297 7.21e-12

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: 65.39  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 195 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 270
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKG-EVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1958760045 271 AASIVLREDnCHFLRVDKEDFNRILRD 297
Cdd:COG0664    80 PATAEALED-SELLRIPREDLEELLER 105
DEP_2_P-Rex cd04440
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex ...
 39-130 1.24e-11

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: 61.48  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  39 EKILRAGKILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCvHSRTQAVGMWQVLLEDGVLNHVDQERHF 118
Cdd:cd04440     3 EDIMSKGVRLYCRLHSLFTPVVKDRDYHLKTYKSVVPASKLVDWLLAQGDC-RTREEAVILGVGLCNNGFMHHVLEKSEF 81

                          90
                  ....*....|..
gi 1958760045 119 QDKYLFYRFLDD 130
Cdd:cd04440    82 KDEPLLFRFYAD 93
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
 52-127 1.82e-11

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: 60.66  E-value: 1.82e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760045  52 ILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTScVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYRF 127
Cdd:cd04439     7 MMCKQGSLIKDRRRKLSTFPKCFLGNEFVSWLLEIGE-ISKPEEGVNLGQALLENGIIHHVSDKHQFKNEQVLYRF 81
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 334-453 2.83e-11

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: 61.58  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045  334 QKYTVMSGTPEKILEHFLETIRLepslneATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQPSQGTeQERMDYALNNKR 413
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDK------ADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESW-VEEKVNPRRVKN 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958760045  414 RVIRLVLQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARM 453
Cdd:smart00229  74 RVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYP 113
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
 63-127 2.27e-09

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


Pssm-ID: 239888  Cd Length: 85  Bit Score: 54.75  E-value: 2.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958760045  63 RKYHLKTYRQCCVGTELVDWMIQQTScVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYRF 127
Cdd:cd04441    22 REEEGVKYERTFVGSEFIDWLLQEGE-AESRREAVQLCRRLLEHGIIQHVSNKHHFFDSNLLYQF 85
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 60-127 4.43e-07

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: 48.43  E-value: 4.43e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760045  60 IRDRKYHLKTYRQCCVGTELVDWMIQQTSCVHSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYRF 127
Cdd:cd04449    16 IFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFYFYYI 83
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
220-297 5.46e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.19  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760045 220 TVLFNQGEEGTSWYIILKGSVNVVIY---GKGVVCT-LHEGDDFGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRIL 295
Cdd:PRK11753   29 STLIHAGEKAETLYYIVKGSVAVLIKdeeGKEMILSyLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLI 108


                  ..
gi 1958760045 296 RD 297
Cdd:PRK11753  109 QV 110
 
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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