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Conserved domains on  [gi|442622530|ref|NP_001260736|]
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exchange protein directly activated by cAMP, isoform F [Drosophila melanogaster]

Protein Classification

Ras-GEF domain-containing protein( domain architecture ID 12868393)

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;
695-931 2.32e-76

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 249.47  E-value: 2.32e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   695 LSTKELAYHITLFEWDLFWAVHEYELLYHTFGRHHF-GKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIK 773
Cdd:smart00147   4 LDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKkSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSKFIQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   774 LAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKL-QPPLIPFMPLLL 852
Cdd:smart00147  84 VAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLGVLL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   853 KDMTFAHEGNKTSL-DGLVNFEKMHMMAQTMRTIRFCRSRSlglePPSPKSEGEVRSYI-SSFRVIDNQRVLTAMSQKVE 930
Cdd:smart00147 164 KDLTFIDEGNPDFLeNGLVNFEKRRQIAEILREIRQLQSQP----YNLRPNRSDIQSLLqQLLDHLDEEEELYQLSLKIE 239


                   .
gi 442622530   931 P 931
Cdd:smart00147 240 P 240
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 128-259 7.57e-58

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: 194.10  E-value: 7.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 128 MGWALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCF 207
Cdd:cd04437    1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442622530 208 LYRFRIDEEGGTAAagvpqaeDLGAANEHIREALSALFQRGPDATLRMILRK 259
Cdd:cd04437   81 FYRFSDDECSPAPL-------EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 281-392 1.08e-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: 91.23  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 281 ALSHLSTSIKRELSSIFvFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAP 356
Cdd:cd00038    1 LFSGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442622530 357 RAATIVLKEnNCHLLRVDKEHFNRILRDVEANTLRL 392
Cdd:cd00038   80 RSATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 418-523 2.08e-14

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: 70.03  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  418 TVMSGTPAKMLEHLLETRLGQSvggmDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDR--EYIINFKKRV 495
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLD----DSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWisKKTLPIRIRV 76

                          90       100
                  ....*....|....*....|....*...
gi 442622530  496 IQFMQKWVMAVRHAAFEEPSVCDFIEDL 523
Cdd:pfam00618  77 LSVLRHWVENYFSDFNDDPVLLSRLEKF 104
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 23-75 6.94e-07

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: 48.86  E-value: 6.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442622530  23 VTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELM 75
Cdd:cd00038   58 QIVGFLGPGDLFGElALLGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELA 111
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 581-651 2.27e-03

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member smart00314:

Pssm-ID: 475130  Cd Length: 90  Bit Score: 38.05  E-value: 2.27e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622530   581 SKTVIRpdddiIFRVYCADHTYCTLRFPMHTTA-ELIKACAAdKLQLNRGPEDLVLVEVKSNGERSVFKDND 651
Cdd:smart00314   1 DTFVLR-----VYVDDLPGGTYKTLRVSSRTTArDVIQQLLE-KFHLTDDPEEYVLVEVLPDGKERVLPDDE 66
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
695-931 2.32e-76

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 249.47  E-value: 2.32e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   695 LSTKELAYHITLFEWDLFWAVHEYELLYHTFGRHHF-GKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIK 773
Cdd:smart00147   4 LDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKkSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSKFIQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   774 LAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKL-QPPLIPFMPLLL 852
Cdd:smart00147  84 VAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLGVLL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   853 KDMTFAHEGNKTSL-DGLVNFEKMHMMAQTMRTIRFCRSRSlglePPSPKSEGEVRSYI-SSFRVIDNQRVLTAMSQKVE 930
Cdd:smart00147 164 KDLTFIDEGNPDFLeNGLVNFEKRRQIAEILREIRQLQSQP----YNLRPNRSDIQSLLqQLLDHLDEEEELYQLSLKIE 239


                   .
gi 442622530   931 P 931
Cdd:smart00147 240 P 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 695-928 1.05e-69

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: 231.37  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 695 LSTKELAYHITLFEWDLFWAVHEYELLYHTFG-RHHFGKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIK 773
Cdd:cd00155    4 LDPKELAEQLTLLDFELFRKIEPFELLGSLWSkKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSKFIQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 774 LAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKL--QPPLIPFMPLL 851
Cdd:cd00155   84 VAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFLGVY 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622530 852 LKDMTFAHEGNKTSLD-GLVNFEKMHMMAQTMRTIRFCRSRSLGLEPPSpksegEVRSYISSFR-VIDNQRVLTAMSQK 928
Cdd:cd00155  164 LKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSNSYELNRDE-----DILAFLWKLLeLILNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 699-876 1.07e-67

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 223.62  E-value: 1.07e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  699 ELAYHITLFEWDLFWAVHEYELLYHTFGRHHFGKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIKLAAYC 778
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  779 KEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKLQPPLIPFMPLLLKDMTFA 858
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                         170
                  ....*....|....*....
gi 442622530  859 HEGNKTSL-DGLVNFEKMH 876
Cdd:pfam00617 161 EEGNPDFLeGGLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 128-259 7.57e-58

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: 194.10  E-value: 7.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 128 MGWALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCF 207
Cdd:cd04437    1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442622530 208 LYRFRIDEEGGTAAagvpqaeDLGAANEHIREALSALFQRGPDATLRMILRK 259
Cdd:cd04437   81 FYRFSDDECSPAPL-------EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 281-392 1.08e-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: 91.23  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 281 ALSHLSTSIKRELSSIFvFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAP 356
Cdd:cd00038    1 LFSGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442622530 357 RAATIVLKEnNCHLLRVDKEHFNRILRDVEANTLRL 392
Cdd:cd00038   80 RSATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 144-212 9.36e-18

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: 78.48  E-value: 9.36e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622530   144 LKDRKVSGKLIRKCAPGTELVDWLVNLSPIvHTRAQAAGMWQALLEEGVLAHVN--KEQPFKDKCFLYRFR 212
Cdd:smart00049   7 LRDRKYFLKTYPNCFTGSELVDWLMDNLEI-IDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFT 76
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 302-384 1.47e-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: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  302 HAQAGTILFNQGDEGRSWYILLKGSVDVVIHG----KGTVATLKTGDDFGKLALINDAPRAATIVLKEnNCHLLRVDKEH 377
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALT-DSELLVIPRED 81


                  ....*..
gi 442622530  378 FNRILRD 384
Cdd:pfam00027  82 FLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 282-395 1.33e-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: 73.97  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   282 LSHLSTSIKRELSSIFvFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAPR 357
Cdd:smart00100   2 FKNLDAEELRELADAL-EPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 442622530   358 AATIVLKEnnCHLLRVDKEHFNRILRDVEANTLRLQEH 395
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 144-211 1.27e-14

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 459867  Cd Length: 71  Bit Score: 69.54  E-value: 1.27e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622530  144 LKDRKVSGKLIRKCAPGTELVDWLVNLSPIVhTRAQAAGMWQALLEEGVLAHVNKE-QPFKDKCFLYRF 211
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLEII-TREEAVELGQLLLDQGLIHHVGDKhGLFKDSYYFYRF 71
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 418-523 2.08e-14

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: 70.03  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  418 TVMSGTPAKMLEHLLETRLGQSvggmDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDR--EYIINFKKRV 495
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLD----DSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWisKKTLPIRIRV 76

                          90       100
                  ....*....|....*....|....*...
gi 442622530  496 IQFMQKWVMAVRHAAFEEPSVCDFIEDL 523
Cdd:pfam00618  77 LSVLRHWVENYFSDFNDDPVLLSRLEKF 104
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 282-414 4.89e-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: 66.16  E-value: 4.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 282 LSHLSTSIKRELSSIFVfEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAPR 357
Cdd:COG0664    1 FAGLSDEELEALLAHLE-LRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442622530 358 AATIVLKEnNCHLLRVDKEHFNRILRDVEANTLRLQEH-GKDVLVLERVAKQRGQHSA 414
Cdd:COG0664   80 PATAEALE-DSELLRIPREDLEELLERNPELARALLRLlARRLRQLQERLVSLAFLSA 136
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 423-544 2.84e-11

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: 61.66  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 423 TPAKMLEHLLETRLGQSvggmDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTP-EDREYIINFKKRVIQFMQK 501
Cdd:cd06224    1 TLEALIEHLTSTFDMPD----PSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEYNdWDKKKSKPIRLRVLNVLRT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442622530 502 WVMAVRHAAFEEPSVCDFIEDLAAEVEADPDLNEETSIVHNVL 544
Cdd:cd06224   77 WVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKL 119
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 416-540 8.72e-10

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: 57.34  E-value: 8.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   416 KYTVMSGTPAKMLEHLLETRlgqsvGGMDP-FLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDREYIInfKKR 494
Cdd:smart00229   2 GGLIKGGTLEALIEHLTEAF-----DKADPsFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKVNPRRV--KNR 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 442622530   495 VIQFMQKWVMAVRHAAFEEPSVCDFIEDLAAEVEADPDLNEETSIV 540
Cdd:smart00229  75 VLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVTSLL 120
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 23-75 6.94e-07

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: 48.86  E-value: 6.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442622530  23 VTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELM 75
Cdd:cd00038   58 QIVGFLGPGDLFGElALLGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELA 111
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 11-71 2.55e-05

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: 43.75  E-value: 2.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622530   11 VEQSTRHYAKSAVTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKN 71
Cdd:pfam00027  28 VKVYRTLEDGREQILAVLGPGDFFGElALLGGEPRSATVVALTDSELLVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 23-79 6.88e-04

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: 41.90  E-value: 6.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442622530  23 VTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELMNDIF 79
Cdd:COG0664   57 QILGFLGPGDFFGElSLLGGEPSPATAEALEDSELLRIPREDLEELLERNPELARALL 114
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 305-376 7.07e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 42.96  E-value: 7.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622530  305 AGTILFNQGDEGRSWYILLKGSVDVVIHGKG---TVATLKTGDDFGKLALIN-DAPRAATIVLKENNChLLRVDKE 376
Cdd:TIGR03896 168 AGTILIHEGGTVDALYILLYGEASLSISPDGpgrEVGSSRRGEILGETPFLNgSLPGTATVKAIENSV-LLAIDKQ 242
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 581-651 2.27e-03

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 38.05  E-value: 2.27e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622530   581 SKTVIRpdddiIFRVYCADHTYCTLRFPMHTTA-ELIKACAAdKLQLNRGPEDLVLVEVKSNGERSVFKDND 651
Cdd:smart00314   1 DTFVLR-----VYVDDLPGGTYKTLRVSSRTTArDVIQQLLE-KFHLTDDPEEYVLVEVLPDGKERVLPDDE 66
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
 592-642 5.38e-03

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 37.30  E-value: 5.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442622530 592 IFRVY----CADHTYCTLRFPMHTTAELIKACAADKLQLNrGPEDLVLVEVKSNG 642
Cdd:cd01779    1 MVRVYpgalSPETEFLSVEATKQTTASEVIECLVAKLRLD-KAECYELAEVCGSG 54
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
299-384 6.93e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 299 FEAHAQ-----AGTILFNQGDEGRSWYILLKGSVDVVI----HGKGTVATLKTGDDFGKLAL-INDAPRAATIVLKeNNC 368
Cdd:PRK11753  16 FLSHCHihkypAKSTLIHAGEKAETLYYIVKGSVAVLIkdeeGKEMILSYLNQGDFIGELGLfEEGQERSAWVRAK-TAC 94

                         90
                 ....*....|....*.
gi 442622530 369 HLLRVDKEHFNRILRD 384
Cdd:PRK11753  95 EVAEISYKKFRQLIQV 110
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
695-931 2.32e-76

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 249.47  E-value: 2.32e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   695 LSTKELAYHITLFEWDLFWAVHEYELLYHTFGRHHF-GKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIK 773
Cdd:smart00147   4 LDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKkSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSKFIQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   774 LAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKL-QPPLIPFMPLLL 852
Cdd:smart00147  84 VAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLGVLL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   853 KDMTFAHEGNKTSL-DGLVNFEKMHMMAQTMRTIRFCRSRSlglePPSPKSEGEVRSYI-SSFRVIDNQRVLTAMSQKVE 930
Cdd:smart00147 164 KDLTFIDEGNPDFLeNGLVNFEKRRQIAEILREIRQLQSQP----YNLRPNRSDIQSLLqQLLDHLDEEEELYQLSLKIE 239


                   .
gi 442622530   931 P 931
Cdd:smart00147 240 P 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 695-928 1.05e-69

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: 231.37  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 695 LSTKELAYHITLFEWDLFWAVHEYELLYHTFG-RHHFGKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIK 773
Cdd:cd00155    4 LDPKELAEQLTLLDFELFRKIEPFELLGSLWSkKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSKFIQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 774 LAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKL--QPPLIPFMPLL 851
Cdd:cd00155   84 VAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFLGVY 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622530 852 LKDMTFAHEGNKTSLD-GLVNFEKMHMMAQTMRTIRFCRSRSLGLEPPSpksegEVRSYISSFR-VIDNQRVLTAMSQK 928
Cdd:cd00155  164 LKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSNSYELNRDE-----DILAFLWKLLeLILNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 699-876 1.07e-67

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 223.62  E-value: 1.07e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  699 ELAYHITLFEWDLFWAVHEYELLYHTFGRHHFGKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIKLAAYC 778
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  779 KEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKLQPPLIPFMPLLLKDMTFA 858
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                         170
                  ....*....|....*....
gi 442622530  859 HEGNKTSL-DGLVNFEKMH 876
Cdd:pfam00617 161 EEGNPDFLeGGLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 128-259 7.57e-58

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: 194.10  E-value: 7.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 128 MGWALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCF 207
Cdd:cd04437    1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442622530 208 LYRFRIDEEGGTAAagvpqaeDLGAANEHIREALSALFQRGPDATLRMILRK 259
Cdd:cd04437   81 FYRFSDDECSPAPL-------EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 281-392 1.08e-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: 91.23  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 281 ALSHLSTSIKRELSSIFvFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAP 356
Cdd:cd00038    1 LFSGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442622530 357 RAATIVLKEnNCHLLRVDKEHFNRILRDVEANTLRL 392
Cdd:cd00038   80 RSATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 131-210 6.82e-18

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: 78.92  E-value: 6.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 131 ALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIVhTRAQAAGMWQALLEEGVLAHV-NKEQPFKDKCFLY 209
Cdd:cd04371    2 LVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVsDDKHTFRDSYALY 80


                 .
gi 442622530 210 R 210
Cdd:cd04371   81 R 81
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 144-212 9.36e-18

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: 78.48  E-value: 9.36e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622530   144 LKDRKVSGKLIRKCAPGTELVDWLVNLSPIvHTRAQAAGMWQALLEEGVLAHVN--KEQPFKDKCFLYRFR 212
Cdd:smart00049   7 LRDRKYFLKTYPNCFTGSELVDWLMDNLEI-IDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFT 76
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 302-384 1.47e-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: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  302 HAQAGTILFNQGDEGRSWYILLKGSVDVVIHG----KGTVATLKTGDDFGKLALINDAPRAATIVLKEnNCHLLRVDKEH 377
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALT-DSELLVIPRED 81


                  ....*..
gi 442622530  378 FNRILRD 384
Cdd:pfam00027  82 FLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 282-395 1.33e-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: 73.97  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   282 LSHLSTSIKRELSSIFvFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAPR 357
Cdd:smart00100   2 FKNLDAEELRELADAL-EPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 442622530   358 AATIVLKEnnCHLLRVDKEHFNRILRDVEANTLRLQEH 395
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 144-211 1.27e-14

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 459867  Cd Length: 71  Bit Score: 69.54  E-value: 1.27e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622530  144 LKDRKVSGKLIRKCAPGTELVDWLVNLSPIVhTRAQAAGMWQALLEEGVLAHVNKE-QPFKDKCFLYRF 211
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLEII-TREEAVELGQLLLDQGLIHHVGDKhGLFKDSYYFYRF 71
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 418-523 2.08e-14

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: 70.03  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530  418 TVMSGTPAKMLEHLLETRLGQSvggmDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDR--EYIINFKKRV 495
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLD----DSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWisKKTLPIRIRV 76

                          90       100
                  ....*....|....*....|....*...
gi 442622530  496 IQFMQKWVMAVRHAAFEEPSVCDFIEDL 523
Cdd:pfam00618  77 LSVLRHWVENYFSDFNDDPVLLSRLEKF 104
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 282-414 4.89e-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: 66.16  E-value: 4.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 282 LSHLSTSIKRELSSIFVfEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKG----TVATLKTGDDFGKLALINDAPR 357
Cdd:COG0664    1 FAGLSDEELEALLAHLE-LRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442622530 358 AATIVLKEnNCHLLRVDKEHFNRILRDVEANTLRLQEH-GKDVLVLERVAKQRGQHSA 414
Cdd:COG0664   80 PATAEALE-DSELLRIPREDLEELLERNPELARALLRLlARRLRQLQERLVSLAFLSA 136
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 423-544 2.84e-11

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: 61.66  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 423 TPAKMLEHLLETRLGQSvggmDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTP-EDREYIINFKKRVIQFMQK 501
Cdd:cd06224    1 TLEALIEHLTSTFDMPD----PSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEYNdWDKKKSKPIRLRVLNVLRT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442622530 502 WVMAVRHAAFEEPSVCDFIEDLAAEVEADPDLNEETSIVHNVL 544
Cdd:cd06224   77 WVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKL 119
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
 136-211 3.34e-10

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: 57.19  E-value: 3.34e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622530 136 LVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIvHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYRF 211
Cdd:cd04439    7 MMCKQGSLIKDRRRKLSTFPKCFLGNEFVSWLLEIGEI-SKPEEGVNLGQALLENGIIHHVSDKHQFKNEQVLYRF 81
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
 129-211 6.28e-10

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: 56.67  E-value: 6.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 129 GWALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPiVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFL 208
Cdd:cd04441    4 GQRLYEKLMSTENSILQVREEEGVKYERTFVGSEFIDWLLQEGE-AESRREAVQLCRRLLEHGIIQHVSNKHHFFDSNLL 82


                 ...
gi 442622530 209 YRF 211
Cdd:cd04441   83 YQF 85
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 416-540 8.72e-10

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: 57.34  E-value: 8.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530   416 KYTVMSGTPAKMLEHLLETRlgqsvGGMDP-FLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDREYIInfKKR 494
Cdd:smart00229   2 GGLIKGGTLEALIEHLTEAF-----DKADPsFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKVNPRRV--KNR 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 442622530   495 VIQFMQKWVMAVRHAAFEEPSVCDFIEDLAAEVEADPDLNEETSIV 540
Cdd:smart00229  75 VLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVTSLL 120
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
 145-211 2.77e-08

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: 51.95  E-value: 2.77e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622530 145 KDRKVSGKLIRKCAPGTELVDWL--VNLSPivhTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYRF 211
Cdd:cd04443   18 KDRRCGLRTYKGVFCGCDLVSWLieVGLAQ---DRGEAVLYGRRLLQGGVLQHITNEHHFRDENLLYRF 83
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 23-75 6.94e-07

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: 48.86  E-value: 6.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442622530  23 VTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELM 75
Cdd:cd00038   58 QIVGFLGPGDLFGElALLGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELA 111
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 140-211 5.19e-06

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: 45.27  E-value: 5.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622530 140 NSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPiVHTRAQAAGMWQALLEEGVLAHVNKE-QPFKDKCFLYRF 211
Cdd:cd04442   11 EAKVIKDRRHHLRTYPNCFVGKELIDWLIEHKE-ASDRETAIKIMQKLLDHSIIHHVCDEhKEFKDAKLFYRF 82
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 157-210 5.54e-06

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: 45.13  E-value: 5.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442622530 157 CAPGTELVDWLVNlSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYR 210
Cdd:cd04448   28 CILGKELVNWLIR-QGKAATRVQAIAIGQALLDAGWIECVSDDDLFRDEYALYK 80
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 11-71 2.55e-05

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: 43.75  E-value: 2.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622530   11 VEQSTRHYAKSAVTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKN 71
Cdd:pfam00027  28 VKVYRTLEDGREQILAVLGPGDFFGElALLGGEPRSATVVALTDSELLVIPREDFLELLERD 89
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 157-211 6.99e-05

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in human also known as KIAA0645, is a DEP domain containing protein of unknown function.


Pssm-ID: 239896  Cd Length: 83  Bit Score: 42.26  E-value: 6.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442622530 157 CAPGTELVDWLVNLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYRF 211
Cdd:cd04449   29 CFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFYFYYI 83
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 23-79 6.88e-04

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: 41.90  E-value: 6.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442622530  23 VTLCNLGVGATFGE-SVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELMNDIF 79
Cdd:COG0664   57 QILGFLGPGDFFGElSLLGGEPSPATAEALEDSELLRIPREDLEELLERNPELARALL 114
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 305-376 7.07e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 42.96  E-value: 7.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622530  305 AGTILFNQGDEGRSWYILLKGSVDVVIHGKG---TVATLKTGDDFGKLALIN-DAPRAATIVLKENNChLLRVDKE 376
Cdd:TIGR03896 168 AGTILIHEGGTVDALYILLYGEASLSISPDGpgrEVGSSRRGEILGETPFLNgSLPGTATVKAIENSV-LLAIDKQ 242
DEP_2_P-Rex cd04440
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex ...
 144-214 7.20e-04

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: 39.52  E-value: 7.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622530 144 LKDRKVSGKLIRKCAPGTELVDWLVnLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYRFRID 214
Cdd:cd04440   24 VKDRDYHLKTYKSVVPASKLVDWLL-AQGDCRTREEAVILGVGLCNNGFMHHVLEKSEFKDEPLLFRFYAD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 581-651 2.27e-03

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 38.05  E-value: 2.27e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622530   581 SKTVIRpdddiIFRVYCADHTYCTLRFPMHTTA-ELIKACAAdKLQLNRGPEDLVLVEVKSNGERSVFKDND 651
Cdd:smart00314   1 DTFVLR-----VYVDDLPGGTYKTLRVSSRTTArDVIQQLLE-KFHLTDDPEEYVLVEVLPDGKERVLPDDE 66
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
 592-642 5.38e-03

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 37.30  E-value: 5.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442622530 592 IFRVY----CADHTYCTLRFPMHTTAELIKACAADKLQLNrGPEDLVLVEVKSNG 642
Cdd:cd01779    1 MVRVYpgalSPETEFLSVEATKQTTASEVIECLVAKLRLD-KAECYELAEVCGSG 54
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
299-384 6.93e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622530 299 FEAHAQ-----AGTILFNQGDEGRSWYILLKGSVDVVI----HGKGTVATLKTGDDFGKLAL-INDAPRAATIVLKeNNC 368
Cdd:PRK11753  16 FLSHCHihkypAKSTLIHAGEKAETLYYIVKGSVAVLIkdeeGKEMILSYLNQGDFIGELGLfEEGQERSAWVRAK-TAC 94

                         90
                 ....*....|....*.
gi 442622530 369 HLLRVDKEHFNRILRD 384
Cdd:PRK11753  95 EVAEISYKKFRQLIQV 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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