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Conserved domains on  [gi|1907112255|ref|XP_036015274|]
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rap guanine nucleotide exchange factor 3 isoform X13 [Mus musculus]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 10911790)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
571-839 5.76e-83

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 265.65  E-value: 5.76e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  571 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 650
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKID---PSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  651 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL-SPPVIP 729
Cdd:smart00147  78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  730 FMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRShSTAPLSPLRsrvSHIHEDSQGSRIstcseqslst 808
Cdd:smart00147 158 FLGVLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQS-QPYNLRPNR---SDIQSLLQQLLD---------- 223

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112255  809 rspastwayvqqlkVIDNQRELSRLSRELEP 839
Cdd:smart00147 224 --------------HLDEEEELYQLSLKIEP 240
DEP super family cl02442
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 36-133 7.36e-39

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.


The actual alignment was detected with superfamily member cd04437:

Pssm-ID: 470580  Cd Length: 125  Bit Score: 140.17  E-value: 7.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  36 CCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHgspVKHDWTFQDRDaQFYRFPGPEPEPTGTQ--DVEEELVE 113
Cdd:cd04437    30 CCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH---VDQELHFQDKY-QFYRFSDDECSPAPLEkrEAEEELQE 105

                          90       100
                  ....*....|....*....|
gi 1907112255 114 AMALLSQRGPDALLTVALRK 133
Cdd:cd04437   106 AVTLLSQLGPDALLRMILRK 125
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 302-423 5.80e-19

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: 83.23  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 302 TPEKILELLLEAMRPDSSahdpteTFLSDFLLTHSVFMPSTQLFTALLHHFHVEPaDPAGGSEQEHSTYICNKRQQILRL 381
Cdd:cd06224     1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907112255 382 VGRWVALYSPMLHSDPVATSFLQKLSDLVSRDARLSNLLREQ 423
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 157-266 3.24e-18

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.83  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 157 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 232
Cdd:cd00038     3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907112255 233 ATIILREnNCHFLRVDKQDFNRIIKDVEAKTMRL 266
Cdd:cd00038    82 ATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
571-839 5.76e-83

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 265.65  E-value: 5.76e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  571 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 650
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKID---PSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  651 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL-SPPVIP 729
Cdd:smart00147  78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  730 FMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRShSTAPLSPLRsrvSHIHEDSQGSRIstcseqslst 808
Cdd:smart00147 158 FLGVLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQS-QPYNLRPNR---SDIQSLLQQLLD---------- 223

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112255  809 rspastwayvqqlkVIDNQRELSRLSRELEP 839
Cdd:smart00147 224 --------------HLDEEEELYQLSLKIEP 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 571-806 1.73e-81

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: 261.42  E-value: 1.73e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 571 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 650
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIE---PFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 651 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL--SPPVI 728
Cdd:cd00155    78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 729 PFMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRS--HSTAPLSPLRSRVSHIHEDSQgsRISTCSEQS 805
Cdd:cd00155   158 PFLGVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELS 235


                  .
gi 1907112255 806 L 806
Cdd:cd00155   236 L 236
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 578-759 9.70e-68

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 222.47  E-value: 9.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 578 DLAGQLTDHDWNLFNRIHqvqEVELIHYVLGpQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQLLRKFIKL 657
Cdd:pfam00617   1 ELARQLTLIEFELFRKIK---PRELLGSAWS-KKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 658 AAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKLSPPVIPFMPLLLKD 737
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTD 156

                         170       180
                  ....*....|....*....|...
gi 1907112255 738 VTFIHEGNHTLVEN-LINFEKMR 759
Cdd:pfam00617 157 LTFIEEGNPDFLEGgLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 36-133 7.36e-39

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: 140.17  E-value: 7.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  36 CCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHgspVKHDWTFQDRDaQFYRFPGPEPEPTGTQ--DVEEELVE 113
Cdd:cd04437    30 CCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH---VDQELHFQDKY-QFYRFSDDECSPAPLEkrEAEEELQE 105

                          90       100
                  ....*....|....*....|
gi 1907112255 114 AMALLSQRGPDALLTVALRK 133
Cdd:cd04437   106 AVTLLSQLGPDALLRMILRK 125
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 302-423 5.80e-19

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: 83.23  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 302 TPEKILELLLEAMRPDSSahdpteTFLSDFLLTHSVFMPSTQLFTALLHHFHVEPaDPAGGSEQEHSTYICNKRQQILRL 381
Cdd:cd06224     1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907112255 382 VGRWVALYSPMLHSDPVATSFLQKLSDLVSRDARLSNLLREQ 423
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKL 115
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 297-406 6.30e-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: 82.74  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 297 TVMSGTPEKILELLLEAMRpdssahDPTETFLSDFLLTHSVFMPSTQLFTALLHHFHVEPADPAGGSEQEHSTYICNKRQ 376
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907112255 377 QILRLVGRWVALYSPMLHSDPVATSFLQKL 406
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 157-266 3.24e-18

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.83  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 157 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 232
Cdd:cd00038     3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907112255 233 ATIILREnNCHFLRVDKQDFNRIIKDVEAKTMRL 266
Cdd:cd00038    82 ATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 178-258 1.30e-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: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 178 KAGTVLFSQGDKGTSWYIIWKGSVNVVTHG----KGLVTTLHEGDDFGQLALVNDAPRAATIILREnNCHFLRVDKQDFN 253
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALT-DSELLVIPREDFL 83


                  ....*
gi 1907112255 254 RIIKD 258
Cdd:pfam00027  84 ELLER 88
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 294-421 5.40e-16

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: 75.06  E-value: 5.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  294 NRYTVMSGTPEKILELLLEAMrpdssaHDPTETFLSDFLLTHSVFMPSTQLFTALLHHFhvEPADPAGGSEQEHSTYICN 373
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAF------DKADPSFVETFLLTYRSFITTQELLQLLLYRY--NAIPPESWVEEKVNPRRVK 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907112255  374 KRqqILRLVGRWVALYSPMLHSDPVATSFLQKLSDLVSRDA------RLSNLLR 421
Cdd:smart00229  73 NR--VLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKypglvtSLLNLLR 124
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 157-269 1.12e-14

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 70.89  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  157 AHLSNSVKRELAAVLlfEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 231
Cdd:smart00100   3 KNLDAEELRELADAL--EPVRyPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907112255  232 AATIILREnnCHFLRVDKQDFNRIIKDVEAKTMRLEEH 269
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 35-96 7.83e-12

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: 61.53  E-value: 7.83e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112255   35 HCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPvKHDWTFQDrDAQFYRFPG 96
Cdd:smart00049  19 NCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNG-PNKHTFKD-SKALYRFTT 77
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 157-258 6.30e-09

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 56.92  E-value: 6.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 157 AHLSNSVKRELAAvlLFEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 231
Cdd:COG0664     2 AGLSDEELEALLA--HLELRTlKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1907112255 232 AATIILREnNCHFLRVDKQDFNRIIKD 258
Cdd:COG0664    80 PATAEALE-DSELLRIPREDLEELLER 105
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 35-94 9.42e-07

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: 46.81  E-value: 9.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  35 HCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPVKHdwTFQDrDAQFYRF 94
Cdd:pfam00610  16 NCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKHG--LFKD-SYYFYRF 71
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
571-839 5.76e-83

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 265.65  E-value: 5.76e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  571 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 650
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKID---PSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEILKQTTPKDRAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  651 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL-SPPVIP 729
Cdd:smart00147  78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  730 FMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRShSTAPLSPLRsrvSHIHEDSQGSRIstcseqslst 808
Cdd:smart00147 158 FLGVLLKDLTFIDEGNPDFLEnGLVNFEKRRQIAEILREIRQLQS-QPYNLRPNR---SDIQSLLQQLLD---------- 223

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112255  809 rspastwayvqqlkVIDNQRELSRLSRELEP 839
Cdd:smart00147 224 --------------HLDEEEELYQLSLKIEP 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 571-806 1.73e-81

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: 261.42  E-value: 1.73e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 571 LDLVSAKDLAGQLTDHDWNLFNRIHqvqEVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQL 650
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIE---PFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 651 LRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKL--SPPVI 728
Cdd:cd00155    78 LSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 729 PFMPLLLKDVTFIHEGNHTLVE-NLINFEKMRMMARAVRMLHHCRS--HSTAPLSPLRSRVSHIHEDSQgsRISTCSEQS 805
Cdd:cd00155   158 PFLGVYLKDLTFLHEGNPDFLEgNLVNFEKRRKIAEILREIRQLQSnsYELNRDEDILAFLWKLLELIL--NEDELYELS 235


                  .
gi 1907112255 806 L 806
Cdd:cd00155   236 L 236
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 578-759 9.70e-68

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 222.47  E-value: 9.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 578 DLAGQLTDHDWNLFNRIHqvqEVELIHYVLGpQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGSRAQLLRKFIKL 657
Cdd:pfam00617   1 ELARQLTLIEFELFRKIK---PRELLGSAWS-KKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 658 AAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALTKLSPPVIPFMPLLLKD 737
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTD 156

                         170       180
                  ....*....|....*....|...
gi 1907112255 738 VTFIHEGNHTLVEN-LINFEKMR 759
Cdd:pfam00617 157 LTFIEEGNPDFLEGgLINFEKRR 179
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
 36-133 7.36e-39

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: 140.17  E-value: 7.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  36 CCSGRELVDGILALGLGVHSRSQAVGICQVLLDEGALCHgspVKHDWTFQDRDaQFYRFPGPEPEPTGTQ--DVEEELVE 113
Cdd:cd04437    30 CCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLH---VDQELHFQDKY-QFYRFSDDECSPAPLEkrEAEEELQE 105

                          90       100
                  ....*....|....*....|
gi 1907112255 114 AMALLSQRGPDALLTVALRK 133
Cdd:cd04437   106 AVTLLSQLGPDALLRMILRK 125
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 302-423 5.80e-19

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: 83.23  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 302 TPEKILELLLEAMRPDSSahdpteTFLSDFLLTHSVFMPSTQLFTALLHHFHVEPaDPAGGSEQEHSTYICNKRQQILRL 381
Cdd:cd06224     1 TLEALIEHLTSTFDMPDP------SFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907112255 382 VGRWVALYSPMLHSDPVATSFLQKLSDLVSRDARLSNLLREQ 423
Cdd:cd06224    74 LRTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKL 115
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 297-406 6.30e-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: 82.74  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 297 TVMSGTPEKILELLLEAMRpdssahDPTETFLSDFLLTHSVFMPSTQLFTALLHHFHVEPADPAGGSEQEHSTYICNKRQ 376
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRI------MLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSDSYWISKKTLPIRI 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907112255 377 QILRLVGRWVALYSPMLHSDPVATSFLQKL 406
Cdd:pfam00618  75 RVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 157-266 3.24e-18

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.83  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 157 AHLSNSVKRELAAVLlFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPRA 232
Cdd:cd00038     3 SGLDDEELEELADAL-EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPRS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907112255 233 ATIILREnNCHFLRVDKQDFNRIIKDVEAKTMRL 266
Cdd:cd00038    82 ATVRALT-DSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 178-258 1.30e-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: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 178 KAGTVLFSQGDKGTSWYIIWKGSVNVVTHG----KGLVTTLHEGDDFGQLALVNDAPRAATIILREnNCHFLRVDKQDFN 253
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgrEQILAVLGPGDFFGELALLGGEPRSATVVALT-DSELLVIPREDFL 83


                  ....*
gi 1907112255 254 RIIKD 258
Cdd:pfam00027  84 ELLER 88
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 294-421 5.40e-16

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: 75.06  E-value: 5.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  294 NRYTVMSGTPEKILELLLEAMrpdssaHDPTETFLSDFLLTHSVFMPSTQLFTALLHHFhvEPADPAGGSEQEHSTYICN 373
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAF------DKADPSFVETFLLTYRSFITTQELLQLLLYRY--NAIPPESWVEEKVNPRRVK 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907112255  374 KRqqILRLVGRWVALYSPMLHSDPVATSFLQKLSDLVSRDA------RLSNLLR 421
Cdd:smart00229  73 NR--VLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKypglvtSLLNLLR 124
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 157-269 1.12e-14

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 70.89  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  157 AHLSNSVKRELAAVLlfEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 231
Cdd:smart00100   3 KNLDAEELRELADAL--EPVRyPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907112255  232 AATIILREnnCHFLRVDKQDFNRIIKDVEAKTMRLEEH 269
Cdd:smart00100  81 AASAAAVA--LELATLLRIDFRDFLQLLPELPQLLLEL 116
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
 35-96 7.83e-12

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: 61.53  E-value: 7.83e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112255   35 HCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPvKHDWTFQDrDAQFYRFPG 96
Cdd:smart00049  19 NCFTGSELVDWLMDNLE-IIDREEAVHLGQLLLDEGLIHHVNG-PNKHTFKD-SKALYRFTT 77
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
 35-93 3.21e-09

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: 54.27  E-value: 3.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112255  35 HCCSGRELVDGILALGLGVhSRSQAVGICQVLLDEGALCHGSPVKHdwTFQDrDAQFYR 93
Cdd:cd04371    27 NCFTGSELVDWLLDNLEAI-TREEAVELGQALLKHGLIHHVSDDKH--TFRD-SYALYR 81
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 157-258 6.30e-09

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 56.92  E-value: 6.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255 157 AHLSNSVKRELAAvlLFEPHS-KAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKG----LVTTLHEGDDFGQLALVNDAPR 231
Cdd:COG0664     2 AGLSDEELEALLA--HLELRTlKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....*..
gi 1907112255 232 AATIILREnNCHFLRVDKQDFNRIIKD 258
Cdd:COG0664    80 PATAEALE-DSELLRIPREDLEELLER 105
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
 35-94 9.42e-07

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: 46.81  E-value: 9.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112255  35 HCCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALCHGSPVKHdwTFQDrDAQFYRF 94
Cdd:pfam00610  16 NCFTGSEAVDWLMDNLE-IITREEAVELGQLLLDQGLIHHVGDKHG--LFKD-SYYFYRF 71
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
 36-91 9.08e-03

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: 35.88  E-value: 9.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907112255  36 CCSGRELVDGILALGLgVHSRSQAVGICQVLLDEGALchgSPVKHDWTFQDRDAQF 91
Cdd:cd04448    28 CILGKELVNWLIRQGK-AATRVQAIAIGQALLDAGWI---ECVSDDDLFRDEYALY 79
 
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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