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Conserved domains on  [gi|1338810926|ref|XP_023647716|]
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ral guanine nucleotide dissociation stimulator-like 3 isoform X1 [Paramormyrops kingsleyae]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 10457322)

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 cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 266-536 2.73e-76

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: 246.40  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 266 FMDFPVRDVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENLAPTIRATVAQFNIVTNRVMTSLLcspvgvvsptipLA 345
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEIL------------LC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 346 SSPTQRARIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVV 425
Cdd:cd00155    69 TNPKKRARLLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 426 edesqsaedpSGPHQSPkicpppmsaasgVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRRREFEILSEIRQLQgTCS 505
Cdd:cd00155   149 ----------SVGPNPP------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQ-SNS 205

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1338810926 506 lYSLPPHAQIAARLQDCEL--LSDQTSYELSQE 536
Cdd:cd00155   206 -YELNRDEDILAFLWKLLEliLNEDELYELSLE 237
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 668-754 2.36e-42

Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with activated Ras and may function as effectors for other Ras family. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes and is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. The RalGDS family includes RalGDS, RGL, RGL2/Rlf and RGL3. All family members have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal RA domain. The RA domain mediates the GTP-dependent interaction with Ras and Ras-related proteins.


:

Pssm-ID: 340449  Cd Length: 88  Bit Score: 148.49  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVECGNN-GNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMSTSAN 746
Cdd:cd00153     1 DSRIIRVSLEDGSEdGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAN 80


                  ....*...
gi 1338810926 747 YDFILRRR 754
Cdd:cd00153    81 LNFILRKK 88
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 112-196 3.43e-15

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: 71.95  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 112 RLKATTLDRLVAELLDPSC-QEPNYNHIFLCTYRAFTSTSTLVELLFQR------DDVLSELYPDCQNSS-----MLPLI 179
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRImLDDSFLSTFLLTYRSFTTPAELLELLIERynipppLDLSSDSYWISKKTLpirirVLSVL 80

                          90
                  ....*....|....*..
gi 1338810926 180 QTWLDEYSEDFWDPPQC 196
Cdd:pfam00618  81 RHWVENYFSDFNDDPVL 97
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 266-536 2.73e-76

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: 246.40  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 266 FMDFPVRDVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENLAPTIRATVAQFNIVTNRVMTSLLcspvgvvsptipLA 345
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEIL------------LC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 346 SSPTQRARIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVV 425
Cdd:cd00155    69 TNPKKRARLLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 426 edesqsaedpSGPHQSPkicpppmsaasgVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRRREFEILSEIRQLQgTCS 505
Cdd:cd00155   149 ----------SVGPNPP------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQ-SNS 205

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1338810926 506 lYSLPPHAQIAARLQDCEL--LSDQTSYELSQE 536
Cdd:cd00155   206 -YELNRDEDILAFLWKLLEliLNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
266-541 4.29e-74

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 240.61  E-value: 4.29e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  266 FMDFPVRDVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENLAPTIRATVAQFNIVTNRVMTSLLcspvgvvsptipLA 345
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEIL------------KQ 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  346 SSPTQRARIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVv 425
Cdd:smart00147  69 TTPKDRAELLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREAL- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  426 edesqsaedpsgphqspKICPPPmsaasGVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRRREFEILSEIRQLQGtcS 505
Cdd:smart00147 148 -----------------SSCNLP-----PCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQS--Q 203

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1338810926  506 LYSLPPHAQIAARL--QDCELL-SDQTSYELSQELEPPV 541
Cdd:smart00147 204 PYNLRPNRSDIQSLlqQLLDHLdEEEELYQLSLKIEPRV 242
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 273-488 1.44e-65

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 215.53  E-value: 1.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 273 DVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENlAPTIRATVAQFNIVTNRVMTSLLCSPvgvvsptiplasSPTQRA 352
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN-SPNIEAMIARFNKLSNWVASEILSEE------------DLKKRA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 353 RIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVvedesqsa 432
Cdd:pfam00617  68 KVIKKFIKIAEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREAL-------- 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1338810926 433 edpsgphqspkicpppMSAASGVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRR 488
Cdd:pfam00617 140 ----------------SSASPPCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 668-754 2.36e-42

Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with activated Ras and may function as effectors for other Ras family. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes and is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. The RalGDS family includes RalGDS, RGL, RGL2/Rlf and RGL3. All family members have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal RA domain. The RA domain mediates the GTP-dependent interaction with Ras and Ras-related proteins.


Pssm-ID: 340449  Cd Length: 88  Bit Score: 148.49  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVECGNN-GNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMSTSAN 746
Cdd:cd00153     1 DSRIIRVSLEDGSEdGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAN 80


                  ....*...
gi 1338810926 747 YDFILRRR 754
Cdd:cd00153    81 LNFILRKK 88
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 668-754 2.72e-16

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


Pssm-ID: 214612  Cd Length: 90  Bit Score: 74.64  E-value: 2.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  668 DSCIVRVSVEcGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGvDIHNFTLSQVLPEDKELCIPDKANVFYAMST---- 743
Cdd:smart00314   1 DTFVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTD-DPEEYVLVEVLPDGKERVLPDDENPLQLQKLwprr 78

                           90
                   ....*....|.
gi 1338810926  744 SANYDFILRRR 754
Cdd:smart00314  79 GPNLRFVLRKR 89
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 112-196 3.43e-15

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: 71.95  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 112 RLKATTLDRLVAELLDPSC-QEPNYNHIFLCTYRAFTSTSTLVELLFQR------DDVLSELYPDCQNSS-----MLPLI 179
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRImLDDSFLSTFLLTYRSFTTPAELLELLIERynipppLDLSSDSYWISKKTLpirirVLSVL 80

                          90
                  ....*....|....*..
gi 1338810926 180 QTWLDEYSEDFWDPPQC 196
Cdd:pfam00618  81 RHWVENYFSDFNDDPVL 97
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 668-754 1.54e-13

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 66.97  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVECGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGvDIHNFTLSQVL-PEDKELCIPDKANVFYAMST--- 743
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLED-DPRDYVLVEVLeRGGGERRLPDDECPLQIQLQwpr 79

                          90
                  ....*....|..
gi 1338810926 744 -SANYDFILRRR 754
Cdd:pfam00788  80 dASDSRFLLRKR 91
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 117-196 6.19e-13

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: 65.90  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 117 TLDRLVAELLDP-SCQEPNYNHIFLCTYRAFTSTSTLVELLFQR---DDVLSELYPDCQNSSMLP-------LIQTWLDE 185
Cdd:cd06224     1 TLEALIEHLTSTfDMPDPSFVSTFLLTYRSFTTPTELLEKLIERyeiAPPENLEYNDWDKKKSKPirlrvlnVLRTWVEN 80

                          90
                  ....*....|.
gi 1338810926 186 YSEDFWDPPQC 196
Cdd:cd06224    81 YPYDFFDDEEL 91
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 109-227 1.32e-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: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  109 KLRRLKATTLDRLVAELLDP-SCQEPNYNHIFLCTYRAFTSTSTLVELLFQR-------DDVLSELYPDCQNSSMLPLIQ 180
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAfDKADPSFVETFLLTYRSFITTQELLQLLLYRynaippeSWVEEKVNPRRVKNRVLNILR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1338810926  181 TWLDEYSEDFWDPPqCPALRLLS-AHLFQRPCFRRLAKRADTLLRKFQ 227
Cdd:smart00229  81 TWVENYWEDFEDDP-KLISFLLEfLELVDDEKYPGLVTSLLNLLRRLS 127
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 266-536 2.73e-76

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: 246.40  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 266 FMDFPVRDVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENLAPTIRATVAQFNIVTNRVMTSLLcspvgvvsptipLA 345
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEIL------------LC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 346 SSPTQRARIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVV 425
Cdd:cd00155    69 TNPKKRARLLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 426 edesqsaedpSGPHQSPkicpppmsaasgVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRRREFEILSEIRQLQgTCS 505
Cdd:cd00155   149 ----------SVGPNPP------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQ-SNS 205

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1338810926 506 lYSLPPHAQIAARLQDCEL--LSDQTSYELSQE 536
Cdd:cd00155   206 -YELNRDEDILAFLWKLLEliLNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
266-541 4.29e-74

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 240.61  E-value: 4.29e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  266 FMDFPVRDVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENLAPTIRATVAQFNIVTNRVMTSLLcspvgvvsptipLA 345
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPLNLEAFIRRFNEVSNWVATEIL------------KQ 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  346 SSPTQRARIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVv 425
Cdd:smart00147  69 TTPKDRAELLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREAL- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  426 edesqsaedpsgphqspKICPPPmsaasGVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRRREFEILSEIRQLQGtcS 505
Cdd:smart00147 148 -----------------SSCNLP-----PCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQS--Q 203

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1338810926  506 LYSLPPHAQIAARL--QDCELL-SDQTSYELSQELEPPV 541
Cdd:smart00147 204 PYNLRPNRSDIQSLlqQLLDHLdEEEELYQLSLKIEPRV 242
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 273-488 1.44e-65

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 215.53  E-value: 1.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 273 DVAEELTRLDAELFEKVVPFQCLGCVWSQRDKKENlAPTIRATVAQFNIVTNRVMTSLLCSPvgvvsptiplasSPTQRA 352
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN-SPNIEAMIARFNKLSNWVASEILSEE------------DLKKRA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 353 RIIEKWISVAQECRQLKNFSSLRAILSALQSNAIYRLKKTWAAVSREYIANFENLCETFTDENGVLTSREIVvedesqsa 432
Cdd:pfam00617  68 KVIKKFIKIAEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREAL-------- 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1338810926 433 edpsgphqspkicpppMSAASGVIPYLGTYLTILTMLDTALPDTVEGGLINFEKRR 488
Cdd:pfam00617 140 ----------------SSASPPCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 668-754 2.36e-42

Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with activated Ras and may function as effectors for other Ras family. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes and is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. The RalGDS family includes RalGDS, RGL, RGL2/Rlf and RGL3. All family members have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal RA domain. The RA domain mediates the GTP-dependent interaction with Ras and Ras-related proteins.


Pssm-ID: 340449  Cd Length: 88  Bit Score: 148.49  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVECGNN-GNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMSTSAN 746
Cdd:cd00153     1 DSRIIRVSLEDGSEdGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAN 80


                  ....*...
gi 1338810926 747 YDFILRRR 754
Cdd:cd00153    81 LNFILRKK 88
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 668-754 2.33e-39

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 (RalGDS-like 1) and similar proteins; RalGDS-like 1 (RGL) is a Ral-specific guanine nucleotide exchange factor that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL has been identified as a possible effector protein of Ras. It also regulates c-fos promoter and the GDP/GTP exchange of Ral. Members in this family have similar structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340730  Cd Length: 87  Bit Score: 140.12  E-value: 2.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVEcGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMSTSANY 747
Cdd:cd17210     2 DTCIIRVSVE-DNNGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNF 80


                  ....*..
gi 1338810926 748 DFILRRR 754
Cdd:cd17210    81 DFILRKK 87
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 668-754 1.16e-33

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) and similar proteins; RalGDS, also termed Ral guanine nucleotide exchange factor (RalGEF), is a guanine exchange factor (GEF) for the Ral family of small GTPases. It is the prototype of RalGDS family proteins that are involved in Ras and Ral signaling pathways as downstream effector proteins. RalGDS stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. Moreover, RalGDS functions as a novel interacting partner for Rab7-interacting lysosomal protein (RILP), a key regulator for late endosomal/lysosomal trafficking. RILP suppresses invasion of breast cancer cells by inhibiting the GEF activity for RalA of RalGDS. RalGDS also plays a vital role in the regulation of Ral-dependent Weibel-Palade bodies (WPB) exocytosis from endothelial cells. In addition, RalGDS couples growth factor signaling to Akt activation by promoting PDK1-induced Akt phosphorylation. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340729  Cd Length: 86  Bit Score: 123.91  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVECgNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMSTSANY 747
Cdd:cd17209     1 DCCIIRVSLDV-DNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANY 79


                  ....*..
gi 1338810926 748 DFILRRR 754
Cdd:cd17209    80 DFVLKKR 86
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
 671-754 3.10e-31

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 (RalGDS-like 3) and similar proteins; RalGDS-like 3 (RGL3), also termed Ras pathway modulator (RPM), interacts in a GTP- and effector loop-dependent manner with Rit and Ras. As a novel potential effector of both p21 Ras and M-Ras, RGL3 negatively regulates Elk-1-dependent gene induction downstream of p21 Ras or mitogen activated protein/extracellular signal regulated kinase Kinase 1 (MEKK1). It also functions as a potential binding partner for Rap-family small G-proteins and profilin II. RGL3 belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340732  Cd Length: 87  Bit Score: 116.96  E-value: 3.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 671 IVRVSVEcGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMSTSANYDFI 750
Cdd:cd17212     5 VIRVSID-NDHGNLYRSILLTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANVFYAMSPAAPGDFM 83


                  ....
gi 1338810926 751 LRRR 754
Cdd:cd17212    84 LRRK 87
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 667-754 5.47e-29

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) and similar proteins; RalGDS-like 2 (RGL2), also termed RalGDS-like factor (RLF), or Ras-associated protein RAB2L, is a novel Ras and Rap 1A-associating protein that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL2 exhibits guanine nucleotide exchange activity towards the small GTPase Ral. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of RGL2 is phosphorylated by protein kinase A and the phosphorylation affects the ability of RGL2 to bind both Ras and Rap1.


Pssm-ID: 340731  Cd Length: 86  Bit Score: 110.68  E-value: 5.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 667 ADSCIVRVSVECGNnGNVYKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQVLPEDKELCIPDKANVFYAMStSAN 746
Cdd:cd17211     1 SDCRIIRVRMELHD-GSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMS-SAS 78


                  ....*...
gi 1338810926 747 YDFILRRR 754
Cdd:cd17211    79 LDFILRPR 86
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 668-754 2.72e-16

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


Pssm-ID: 214612  Cd Length: 90  Bit Score: 74.64  E-value: 2.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  668 DSCIVRVSVEcGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGvDIHNFTLSQVLPEDKELCIPDKANVFYAMST---- 743
Cdd:smart00314   1 DTFVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTD-DPEEYVLVEVLPDGKERVLPDDENPLQLQKLwprr 78

                           90
                   ....*....|.
gi 1338810926  744 SANYDFILRRR 754
Cdd:smart00314  79 GPNLRFVLRKR 89
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 112-196 3.43e-15

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: 71.95  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 112 RLKATTLDRLVAELLDPSC-QEPNYNHIFLCTYRAFTSTSTLVELLFQR------DDVLSELYPDCQNSS-----MLPLI 179
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRImLDDSFLSTFLLTYRSFTTPAELLELLIERynipppLDLSSDSYWISKKTLpirirVLSVL 80

                          90
                  ....*....|....*..
gi 1338810926 180 QTWLDEYSEDFWDPPQC 196
Cdd:pfam00618  81 RHWVENYFSDFNDDPVL 97
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 668-754 1.54e-13

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 66.97  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 668 DSCIVRVSVECGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGvDIHNFTLSQVL-PEDKELCIPDKANVFYAMST--- 743
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLED-DPRDYVLVEVLeRGGGERRLPDDECPLQIQLQwpr 79

                          90
                  ....*....|..
gi 1338810926 744 -SANYDFILRRR 754
Cdd:pfam00788  80 dASDSRFLLRKR 91
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 117-196 6.19e-13

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: 65.90  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 117 TLDRLVAELLDP-SCQEPNYNHIFLCTYRAFTSTSTLVELLFQR---DDVLSELYPDCQNSSMLP-------LIQTWLDE 185
Cdd:cd06224     1 TLEALIEHLTSTfDMPDPSFVSTFLLTYRSFTTPTELLEKLIERyeiAPPENLEYNDWDKKKSKPirlrvlnVLRTWVEN 80

                          90
                  ....*....|.
gi 1338810926 186 YSEDFWDPPQC 196
Cdd:cd06224    81 YPYDFFDDEEL 91
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 109-227 1.32e-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: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926  109 KLRRLKATTLDRLVAELLDP-SCQEPNYNHIFLCTYRAFTSTSTLVELLFQR-------DDVLSELYPDCQNSSMLPLIQ 180
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAfDKADPSFVETFLLTYRSFITTQELLQLLLYRynaippeSWVEEKVNPRRVKNRVLNILR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1338810926  181 TWLDEYSEDFWDPPqCPALRLLS-AHLFQRPCFRRLAKRADTLLRKFQ 227
Cdd:smart00229  81 TWVENYWEDFEDDP-KLISFLLEfLELVDDEKYPGLVTSLLNLLRRLS 127
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 671-753 1.54e-09

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 55.40  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338810926 671 IVRVSVECGNNGNVYKSILLTSQDKTAQVIQRALEKHNLEGvDIHNFTLSQVLP-EDKELCIPDKANVFYAMSTSANYD- 748
Cdd:cd17043     1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEE-DPEDYSLYEVSEkQETERVLHDDECPLLIQLEWGPQGt 79


                  ....*...
gi 1338810926 749 ---FILRR 753
Cdd:cd17043    80 efrFVLKR 87
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 685-722 1.76e-04

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 41.49  E-value: 1.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1338810926 685 YKSILLTSQDKTAQVIQRALEKHNLEGVDIHNFTLSQV 722
Cdd:cd01781    17 YKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQV 54
 
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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