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Conserved domains on  [gi|1772790996|ref|NP_001362799|]
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rap guanine nucleotide exchange factor 4 isoform l [Homo sapiens]

Protein Classification

Ras-GEF domain-containing protein( domain architecture ID 10805331)

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
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 206-334 1.57e-70

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: 229.15  E-value: 1.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 206 AGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYL 285
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1772790996 286 FYRFLDDEHEDAPLpteeEKKECDEELQDTMLLLSQMGPDAHMRMILRK 334
Cdd:cd04437    81 FYRFSDDECSPAPL----EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
768-929 1.14e-63

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 215.19  E-value: 1.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  768 FELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFK-KTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 846
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKsPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  847 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLE-PPLIPFMP 925
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160


                   ....
gi 1772790996  926 LLIK 929
Cdd:smart00147 161 VLLK 164
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 43-158 2.37e-22

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: 93.16  E-value: 2.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  43 AFEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNT 121
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGS--VEVYKLDEDGREQIVGFLGPGDLFGElALLGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1772790996 122 PRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLL 158
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 356-467 1.69e-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: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 356 ALSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAP 431
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAG-EVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1772790996 432 RAASIVLREDnCHFLRVDKEDFNRILRDVEANTVRL 467
Cdd:cd00038    80 RSATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 499-605 1.43e-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: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 499 TVMSGTPEKILEHFLETirleatLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEK---MDYALNNKR 575
Cdd:pfam00618   1 QVKAGTLEKLVEYLTST------RIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSywiSKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1772790996 576 RVIRLVLQWAAMYGDLLQEDDVSMAFLEEF 605
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
 
Name Accession Description Interval E-value
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 206-334 1.57e-70

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: 229.15  E-value: 1.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 206 AGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYL 285
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1772790996 286 FYRFLDDEHEDAPLpteeEKKECDEELQDTMLLLSQMGPDAHMRMILRK 334
Cdd:cd04437    81 FYRFSDDECSPAPL----EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
768-929 1.14e-63

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 215.19  E-value: 1.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  768 FELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFK-KTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 846
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKsPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  847 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLE-PPLIPFMP 925
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160


                   ....
gi 1772790996  926 LLIK 929
Cdd:smart00147 161 VLLK 164
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 775-929 3.42e-61

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 205.52  E-value: 3.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 775 DLAYQMTIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKFIKIAAHC 854
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1772790996 855 KEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLEPPLIPFMPLLIK 929
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLT 155
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 768-929 1.78e-60

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: 205.95  E-value: 1.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 768 FELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFKK-TTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 846
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 847 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKL--EPPLIPFM 924
Cdd:cd00155    81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160


                  ....*
gi 1772790996 925 PLLIK 929
Cdd:cd00155   161 GVYLK 165
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 43-158 2.37e-22

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: 93.16  E-value: 2.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  43 AFEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNT 121
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGS--VEVYKLDEDGREQIVGFLGPGDLFGElALLGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1772790996 122 PRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLL 158
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 217-291 1.50e-21

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: 89.27  E-value: 1.50e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1772790996  217 RAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPcVHSRTQAVGMWQVLLEDGVLNHVD--QEHHFQDKYLFYRFLD 291
Cdd:smart00049   2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFTT 77
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 356-467 1.69e-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: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 356 ALSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAP 431
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAG-EVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1772790996 432 RAASIVLREDnCHFLRVDKEDFNRILRDVEANTVRL 467
Cdd:cd00038    80 RSATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 222-289 1.80e-20

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: 86.10  E-value: 1.80e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1772790996 222 IRDRKYHLKTYRQCCVGTELVDWMMQQTPCVhSRTQAVGMWQVLLEDGVLNHVDQEHH-FQDKYLFYRF 289
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLEII-TREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 499-605 1.43e-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: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 499 TVMSGTPEKILEHFLETirleatLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEK---MDYALNNKR 575
Cdd:pfam00618   1 QVKAGTLEKLVEYLTST------RIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSywiSKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1772790996 576 RVIRLVLQWAAMYGDLLQEDDVSMAFLEEF 605
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 504-629 2.29e-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: 81.69  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 504 TPEKILEHFLETirleatLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTE--QEKMDYALNNKRRVIRLV 581
Cdd:cd06224     1 TLEALIEHLTST------FDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEynDWDKKKSKPIRLRVLNVL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1772790996 582 LQWAAMYGDLLQEDDVSMAFLEEFYVSVSDDARMIAALKEQLPELEKI 629
Cdd:cd06224    75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKLLKL 122
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 62-150 1.93e-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: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  62 ENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNTPRHATIVTRESSELLRIEQ 140
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGK--VKVYRTLEDGREQILAVLGPGDFFGElALLGGEPRSATVVALTDSELLVIPR 79

                          90
                  ....*....|
gi 1772790996 141 KDFKALWEKY 150
Cdd:pfam00027  80 EDFLELLERD 89
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 377-459 3.46e-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: 74.57  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 377 HAKGGTVLFNQGEEGTSWYIILKGSVNVVIYG----KGVVCTLHEGDDFGKLALVNDAPRAASIVLREDnCHFLRVDKED 452
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALTD-SELLVIPRED 81


                  ....*..
gi 1772790996 453 FNRILRD 459
Cdd:pfam00027  82 FLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 357-470 4.12e-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: 4.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  357 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 432
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAG-EVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1772790996  433 AASIVLREdnCHFLRVDKEDFNRILRDVEANTVRLKEH 470
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 44-154 1.05e-14

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 71.28  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996   44 FEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSLDVkVSETSSHQDaVTICTLGIGTAFGE-SILDNTP 122
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEV-YKVLEDGEE-QIVGTLGPGDFFGElALLTNSR 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1772790996  123 RHATiVTRESSELLRIEQKDFKALWEKYRQYM 154
Cdd:smart00100  80 RAAS-AAAVALELATLLRIDFRDFLQLLPELP 110
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 44-159 2.58e-14

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: 72.71  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  44 FEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNTP 122
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGL--VKLYRISEDGREQILGFLGPGDFFGElSLLGGEP 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1772790996 123 RHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLA 159
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLR 115
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 496-634 1.65e-12

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: 65.43  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  496 QKYTVMSGTPEKILEHFLETIRLeatlneATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEKMdYALNNKR 575
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDK------ADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKV-NPRRVKN 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1772790996  576 RVIRLVLQWAAMYGDLLQEDDVSMAFLEEFYVSVSDDARMIAALkeqlpELEKIVKQIS 634
Cdd:smart00229  74 RVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVT-----SLLNLLRRLS 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 357-459 7.55e-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: 7.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 357 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 432
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKG-EVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1772790996 433 AASIVLREDnCHFLRVDKEDFNRILRD 459
Cdd:COG0664    80 PATAEALED-SELLRIPREDLEELLER 105
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
382-459 5.71e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.19  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 382 TVLFNQGEEGTSWYIILKGSVNVVIY---GKGVVCT-LHEGDDFGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRIL 457
Cdd:PRK11753   29 STLIHAGEKAETLYYIVKGSVAVLIKdeeGKEMILSyLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLI 108


                  ..
gi 1772790996 458 RD 459
Cdd:PRK11753  109 QV 110
 
Name Accession Description Interval E-value
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 206-334 1.57e-70

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: 229.15  E-value: 1.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 206 AGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYL 285
Cdd:cd04437     1 AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1772790996 286 FYRFLDDEHEDAPLpteeEKKECDEELQDTMLLLSQMGPDAHMRMILRK 334
Cdd:cd04437    81 FYRFSDDECSPAPL----EKREAEEELQEAVTLLSQLGPDALLRMILRK 125
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
768-929 1.14e-63

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 215.19  E-value: 1.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  768 FELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFK-KTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 846
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKsPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  847 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLE-PPLIPFMP 925
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160


                   ....
gi 1772790996  926 LLIK 929
Cdd:smart00147 161 VLLK 164
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 775-929 3.42e-61

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 205.52  E-value: 3.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 775 DLAYQMTIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKFIKIAAHC 854
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1772790996 855 KEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLEPPLIPFMPLLIK 929
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLT 155
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 768-929 1.78e-60

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: 205.95  E-value: 1.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 768 FELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFKK-TTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKK 846
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 847 FIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKL--EPPLIPFM 924
Cdd:cd00155    81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160


                  ....*
gi 1772790996 925 PLLIK 929
Cdd:cd00155   161 GVYLK 165
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 209-288 6.74e-25

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: 98.95  E-value: 6.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 209 ILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPCVhSRTQAVGMWQVLLEDGVLNHV-DQEHHFQDKYLFY 287
Cdd:cd04371     2 LVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVsDDKHTFRDSYALY 80


                  .
gi 1772790996 288 R 288
Cdd:cd04371    81 R 81
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 43-158 2.37e-22

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: 93.16  E-value: 2.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  43 AFEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNT 121
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGS--VEVYKLDEDGREQIVGFLGPGDLFGElALLGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1772790996 122 PRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLL 158
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 217-291 1.50e-21

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: 89.27  E-value: 1.50e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1772790996  217 RAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPcVHSRTQAVGMWQVLLEDGVLNHVD--QEHHFQDKYLFYRFLD 291
Cdd:smart00049   2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNgpNKHTFKDSKALYRFTT 77
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 356-467 1.69e-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: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 356 ALSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAP 431
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAG-EVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1772790996 432 RAASIVLREDnCHFLRVDKEDFNRILRDVEANTVRL 467
Cdd:cd00038    80 RSATVRALTD-SELLVLPRSDFRRLLQEYPELARRL 114
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 222-289 1.80e-20

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: 86.10  E-value: 1.80e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1772790996 222 IRDRKYHLKTYRQCCVGTELVDWMMQQTPCVhSRTQAVGMWQVLLEDGVLNHVDQEHH-FQDKYLFYRF 289
Cdd:pfam00610   4 LKDRRKHLKTYPNCFTGSEAVDWLMDNLEII-TREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 499-605 1.43e-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: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 499 TVMSGTPEKILEHFLETirleatLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEK---MDYALNNKR 575
Cdd:pfam00618   1 QVKAGTLEKLVEYLTST------RIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSywiSKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1772790996 576 RVIRLVLQWAAMYGDLLQEDDVSMAFLEEF 605
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 504-629 2.29e-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: 81.69  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 504 TPEKILEHFLETirleatLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTE--QEKMDYALNNKRRVIRLV 581
Cdd:cd06224     1 TLEALIEHLTST------FDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEynDWDKKKSKPIRLRVLNVL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1772790996 582 LQWAAMYGDLLQEDDVSMAFLEEFYVSVSDDARMIAALKEQLPELEKI 629
Cdd:cd06224    75 RTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKLLKL 122
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 62-150 1.93e-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: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  62 ENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNTPRHATIVTRESSELLRIEQ 140
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGK--VKVYRTLEDGREQILAVLGPGDFFGElALLGGEPRSATVVALTDSELLVIPR 79

                          90
                  ....*....|
gi 1772790996 141 KDFKALWEKY 150
Cdd:pfam00027  80 EDFLELLERD 89
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 377-459 3.46e-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: 74.57  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 377 HAKGGTVLFNQGEEGTSWYIILKGSVNVVIYG----KGVVCTLHEGDDFGKLALVNDAPRAASIVLREDnCHFLRVDKED 452
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALTD-SELLVIPRED 81


                  ....*..
gi 1772790996 453 FNRILRD 459
Cdd:pfam00027  82 FLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 357-470 4.12e-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: 4.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  357 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 432
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAG-EVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1772790996  433 AASIVLREdnCHFLRVDKEDFNRILRDVEANTVRLKEH 470
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
 221-289 4.85e-15

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: 70.82  E-value: 4.85e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1772790996 221 MIRDRKYHLKTYRQCCVGTELVDWMmQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRF 289
Cdd:cd04443    16 IVKDRRCGLRTYKGVFCGCDLVSWL-IEVGLAQDRGEAVLYGRRLLQGGVLQHITNEHHFRDENLLYRF 83
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 44-154 1.05e-14

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 71.28  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996   44 FEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSLDVkVSETSSHQDaVTICTLGIGTAFGE-SILDNTP 122
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEV-YKVLEDGEE-QIVGTLGPGDFFGElALLTNSR 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1772790996  123 RHATiVTRESSELLRIEQKDFKALWEKYRQYM 154
Cdd:smart00100  80 RAAS-AAAVALELATLLRIDFRDFLQLLPELP 110
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 44-159 2.58e-14

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: 72.71  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  44 FEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSldVKVSETSSHQDAVTICTLGIGTAFGE-SILDNTP 122
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGL--VKLYRISEDGREQILGFLGPGDFFGElSLLGGEP 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1772790996 123 RHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLA 159
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLR 115
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
 221-289 6.42e-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: 68.00  E-value: 6.42e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 221 MIRDRKYHLKTYRQCCVGTELVDWMMQQTPcVHSRTQAVGMWQVLLEDGVLNHVDQEH-HFQDKYLFYRF 289
Cdd:cd04442    14 VIKDRRHHLRTYPNCFVGKELIDWLIEHKE-ASDRETAIKIMQKLLDHSIIHHVCDEHkEFKDAKLFYRF 82
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
 214-289 1.11e-12

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: 64.13  E-value: 1.11e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1772790996 214 ILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPcVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRF 289
Cdd:cd04439     7 MMCKQGSLIKDRRRKLSTFPKCFLGNEFVSWLLEIGE-ISKPEEGVNLGQALLENGIIHHVSDKHQFKNEQVLYRF 81
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 496-634 1.65e-12

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: 65.43  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996  496 QKYTVMSGTPEKILEHFLETIRLeatlneATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEKMdYALNNKR 575
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDK------ADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKV-NPRRVKN 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1772790996  576 RVIRLVLQWAAMYGDLLQEDDVSMAFLEEFYVSVSDDARMIAALkeqlpELEKIVKQIS 634
Cdd:smart00229  74 RVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVT-----SLLNLLRRLS 127
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 221-288 2.40e-12

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: 63.23  E-value: 2.40e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1772790996 221 MIRDRKYHLKTYRQCCVGTELVDWMMQQTPcVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYR 288
Cdd:cd04448    14 EFQDHRYRLRTYTNCILGKELVNWLIRQGK-AATRVQAIAIGQALLDAGWIECVSDDDLFRDEYALYK 80
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 357-459 7.55e-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: 7.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 357 LSHLSTTVKRELAGVLIFESHAKGgTVLFNQGEEGTSWYIILKGSVNVVIYGKG----VVCTLHEGDDFGKLALVNDAPR 432
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKG-EVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1772790996 433 AASIVLREDnCHFLRVDKEDFNRILRD 459
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 ...
 221-292 4.36e-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: 60.32  E-value: 4.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1772790996 221 MIRDRKYHLKTYRQCCVGTELVDWMMQQTPCvHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRFLDD 292
Cdd:cd04440    23 VVKDRDYHLKTYKSVVPASKLVDWLLAQGDC-RTREEAVILGVGLCNNGFMHHVLEKSEFKDEPLLFRFYAD 93
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
 207-289 1.06e-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: 58.60  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 207 GKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPcVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLF 286
Cdd:cd04441     4 GQRLYEKLMSTENSILQVREEEGVKYERTFVGSEFIDWLLQEGE-AESRREAVQLCRRLLEHGIIQHVSNKHHFFDSNLL 82


                  ...
gi 1772790996 287 YRF 289
Cdd:cd04441    83 YQF 85
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
 222-289 3.17e-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: 48.81  E-value: 3.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1772790996 222 IRDRKYHLKTYRQCCVGTELVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRF 289
Cdd:cd04449    16 IFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSGRHPFLDGFYFYYI 83
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
382-459 5.71e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.19  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772790996 382 TVLFNQGEEGTSWYIILKGSVNVVIY---GKGVVCT-LHEGDDFGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRIL 457
Cdd:PRK11753   29 STLIHAGEKAETLYYIVKGSVAVLIKdeeGKEMILSyLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLI 108


                  ..
gi 1772790996 458 RD 459
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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