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Conserved domains on  [gi|28574917|ref|NP_788504|]
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Ral guanine nucleotide dissociation stimulator-like, isoform C [Drosophila melanogaster]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 10865542)

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;
274-539 2.67e-64

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 214.42  E-value: 2.67e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    274 HVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRD--SGGSETVVATINQFNAVLFRVVSSILIDRlKPQERALNISRW 351
Cdd:smart00147   3 LLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSkkSPSPLNLEAFIRRFNEVSNWVATEILKQT-TPKDRAELLSKF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    352 IDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTAknpdpgsd 431
Cdd:smart00147  82 IQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNLP-------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    432 hsdrhlqklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKRKEFEVLAQIKLLQgaANTYNLQADA 511
Cdd:smart00147 154 -------------------PCIPFLGVLLKDLTFIDEGNPDFL-ENGLVNFEKRRQIAEILREIRQLQ--SQPYNLRPNR 211
                          250       260       270
                   ....*....|....*....|....*....|...
gi 28574917    512 -----LFDHWFNSMPvfDEREAFELSCRLEPPP 539
Cdd:smart00147 212 sdiqsLLQQLLDHLD--EEEELYQLSLKIEPRV 242
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
678-766 6.77e-36

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: 130.39  E-value: 6.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 678 DFYIIRVTYETDNielDGIVLYKSIMLGNNERTPQVIRNAMLKLGLED-DPDRFTLAQVLP-DKELVMPKNANVYYAVNT 755
Cdd:cd00153   1 DSRIIRVSLEDGS---EDGNLYKSILLTNQDRTPSVIRRALEKHNLEDeDPDDFSLVQILPdDKELVIPDNANVFYAMNS 77
                        90
                ....*....|.
gi 28574917 756 NYNLNFILRPR 766
Cdd:cd00153  78 SANLNFILRKK 88
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
66-198 4.35e-17

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: 77.84  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917  66 TLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYdalHEKHLEELEQAQQNGQVMDPAydphasiheqh 145
Cdd:cd06224   1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERY---EIAPPENLEYNDWDKKKSKPI----------- 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574917 146 KKTLVSALHVWLDGFPEDWHED--NLQQILAFATKRLKRSDLHIKVLNRLERLIK 198
Cdd:cd06224  67 RLRVLNVLRTWVENYPYDFFDDeeLLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
274-539 2.67e-64

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 214.42  E-value: 2.67e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    274 HVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRD--SGGSETVVATINQFNAVLFRVVSSILIDRlKPQERALNISRW 351
Cdd:smart00147   3 LLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSkkSPSPLNLEAFIRRFNEVSNWVATEILKQT-TPKDRAELLSKF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    352 IDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTAknpdpgsd 431
Cdd:smart00147  82 IQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNLP-------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    432 hsdrhlqklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKRKEFEVLAQIKLLQgaANTYNLQADA 511
Cdd:smart00147 154 -------------------PCIPFLGVLLKDLTFIDEGNPDFL-ENGLVNFEKRRQIAEILREIRQLQ--SQPYNLRPNR 211
                          250       260       270
                   ....*....|....*....|....*....|...
gi 28574917    512 -----LFDHWFNSMPvfDEREAFELSCRLEPPP 539
Cdd:smart00147 212 sdiqsLLQQLLDHLD--EEEELYQLSLKIEPRV 242
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
272-534 2.71e-63

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: 211.73  E-value: 2.71e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 272 FPHVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRD--SGGSETVVATINQFNAVLFRVVSSILIDRlKPQERALNIS 349
Cdd:cd00155   1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDknIHLSPNLERFIERFNNLSNWVASEILLCT-NPKKRARLLS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 350 RWIDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKregtAKNPDPg 429
Cdd:cd00155  80 KFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLK----SVGPNP- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 430 sdhsdrhlqklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKRKEFEVLAQIKLLQgaANTYNLQA 509
Cdd:cd00155 155 ---------------------PCVPFLGVYLKDLTFLHEGNPDFL-EGNLVNFEKRRKIAEILREIRQLQ--SNSYELNR 210
                       250       260
                ....*....|....*....|....*..
gi 28574917 510 DALFDHWFNS--MPVFDEREAFELSCR 534
Cdd:cd00155 211 DEDILAFLWKllELILNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
279-486 6.90e-62

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 205.52  E-value: 6.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917   279 HFAEQLTRMDTELFKRLIPHQCLGHTWARRD-SGGSETVVATINQFNAVLFRVVSSILiDRLKPQERALNISRWIDIAQE 357
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDkKENSPNIEAMIARFNKLSNWVASEIL-SEEDLKKRAKVIKKFIKIAEH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917   358 LRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTaknpdpgsdhsdrhl 437
Cdd:pfam00617  80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP--------------- 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 28574917   438 qklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKR 486
Cdd:pfam00617 145 -------------PCIPFLGLYLTDLTFIEEGNPDFL-EGGLINFEKRR 179
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
678-766 6.77e-36

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: 130.39  E-value: 6.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 678 DFYIIRVTYETDNielDGIVLYKSIMLGNNERTPQVIRNAMLKLGLED-DPDRFTLAQVLP-DKELVMPKNANVYYAVNT 755
Cdd:cd00153   1 DSRIIRVSLEDGS---EDGNLYKSILLTNQDRTPSVIRRALEKHNLEDeDPDDFSLVQILPdDKELVIPDNANVFYAMNS 77
                        90
                ....*....|.
gi 28574917 756 NYNLNFILRPR 766
Cdd:cd00153  78 SANLNFILRKK 88
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
66-198 4.35e-17

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: 77.84  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917  66 TLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYdalHEKHLEELEQAQQNGQVMDPAydphasiheqh 145
Cdd:cd06224   1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERY---EIAPPENLEYNDWDKKKSKPI----------- 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574917 146 KKTLVSALHVWLDGFPEDWHED--NLQQILAFATKRLKRSDLHIKVLNRLERLIK 198
Cdd:cd06224  67 RLRVLNVLRTWVENYPYDFFDDeeLLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
62-175 4.48e-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: 71.57  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    62 VKAATLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYDalHEKHLEELEQAQQNGQVMDPAydphasi 141
Cdd:pfam00618   2 VKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYN--IPPPLDLSSDSYWISKKTLPI------- 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 28574917   142 heqhKKTLVSALHVWLDGFPEDWHED--NLQQILAF 175
Cdd:pfam00618  73 ----RIRVLSVLRHWVENYFSDFNDDpvLLSRLEKF 104
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
62-196 2.24e-10

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 58.88  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917     62 VKAATLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRY-DALHEKHLEEleqaqqngqvmdpaydPHAS 140
Cdd:smart00229   5 IKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYnAIPPESWVEE----------------KVNP 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574917    141 IHEQHKktLVSALHVWLDGFPEDWHED-----NLQQILAFATKRlKRSDLHIKVLNRLERL 196
Cdd:smart00229  69 RRVKNR--VLNILRTWVENYWEDFEDDpklisFLLEFLELVDDE-KYPGLVTSLLNLLRRL 126
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
678-754 1.11e-09

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: 55.77  E-value: 1.11e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574917    678 DFYIIRVTYETDNIELdgivlYKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLP-DKELVMPKNANVYYAVN 754
Cdd:smart00314   1 DTFVLRVYVDDLPGGT-----YKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPdGKERVLPDDENPLQLQK 73
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
699-767 2.78e-08

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: 51.95  E-value: 2.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574917   699 YKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLP--DKELVMPKNANVYYAVNTNY----NLNFILRPRK 767
Cdd:pfam00788  18 YKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLErgGGERRLPDDECPLQIQLQWPrdasDSRFLLRKRD 92
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
274-539 2.67e-64

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 214.42  E-value: 2.67e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    274 HVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRD--SGGSETVVATINQFNAVLFRVVSSILIDRlKPQERALNISRW 351
Cdd:smart00147   3 LLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSkkSPSPLNLEAFIRRFNEVSNWVATEILKQT-TPKDRAELLSKF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    352 IDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTAknpdpgsd 431
Cdd:smart00147  82 IQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNLP-------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    432 hsdrhlqklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKRKEFEVLAQIKLLQgaANTYNLQADA 511
Cdd:smart00147 154 -------------------PCIPFLGVLLKDLTFIDEGNPDFL-ENGLVNFEKRRQIAEILREIRQLQ--SQPYNLRPNR 211
                          250       260       270
                   ....*....|....*....|....*....|...
gi 28574917    512 -----LFDHWFNSMPvfDEREAFELSCRLEPPP 539
Cdd:smart00147 212 sdiqsLLQQLLDHLD--EEEELYQLSLKIEPRV 242
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
272-534 2.71e-63

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: 211.73  E-value: 2.71e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 272 FPHVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRD--SGGSETVVATINQFNAVLFRVVSSILIDRlKPQERALNIS 349
Cdd:cd00155   1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDknIHLSPNLERFIERFNNLSNWVASEILLCT-NPKKRARLLS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 350 RWIDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKregtAKNPDPg 429
Cdd:cd00155  80 KFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLK----SVGPNP- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 430 sdhsdrhlqklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKRKEFEVLAQIKLLQgaANTYNLQA 509
Cdd:cd00155 155 ---------------------PCVPFLGVYLKDLTFLHEGNPDFL-EGNLVNFEKRRKIAEILREIRQLQ--SNSYELNR 210
                       250       260
                ....*....|....*....|....*..
gi 28574917 510 DALFDHWFNS--MPVFDEREAFELSCR 534
Cdd:cd00155 211 DEDILAFLWKllELILNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
279-486 6.90e-62

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 205.52  E-value: 6.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917   279 HFAEQLTRMDTELFKRLIPHQCLGHTWARRD-SGGSETVVATINQFNAVLFRVVSSILiDRLKPQERALNISRWIDIAQE 357
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDkKENSPNIEAMIARFNKLSNWVASEIL-SEEDLKKRAKVIKKFIKIAEH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917   358 LRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTaknpdpgsdhsdrhl 437
Cdd:pfam00617  80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP--------------- 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 28574917   438 qklilnlgtqtshGTIPYLGTFLTDLTMIHTANPDYLtENKLINFDKKR 486
Cdd:pfam00617 145 -------------PCIPFLGLYLTDLTFIEEGNPDFL-EGGLINFEKRR 179
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
678-766 6.77e-36

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: 130.39  E-value: 6.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 678 DFYIIRVTYETDNielDGIVLYKSIMLGNNERTPQVIRNAMLKLGLED-DPDRFTLAQVLP-DKELVMPKNANVYYAVNT 755
Cdd:cd00153   1 DSRIIRVSLEDGS---EDGNLYKSILLTNQDRTPSVIRRALEKHNLEDeDPDDFSLVQILPdDKELVIPDNANVFYAMNS 77
                        90
                ....*....|.
gi 28574917 756 NYNLNFILRPR 766
Cdd:cd00153  78 SANLNFILRKK 88
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
678-766 6.72e-22

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: 90.43  E-value: 6.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 678 DFYIIRVTYETDNIELdgivlYKSIMLGNNERTPQVIRNAMLKLGLEDDP-DRFTLAQVLP-DKELVMPKNANVYYAVNT 755
Cdd:cd17210   2 DTCIIRVSVEDNNGNM-----YKSIMLTSQDKTPAVIQRAMSKHNLESDPaEDYELVQVISeDRELVIPDNANVFYAMNS 76
                        90
                ....*....|.
gi 28574917 756 NYNLNFILRPR 766
Cdd:cd17210  77 SVNFDFILRKK 87
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
678-766 3.31e-18

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: 80.00  E-value: 3.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 678 DFYIIRVTYETDNIELdgivlYKSIMLGNNERTPQVIRNAMLKLGLEDD-PDRFTLAQVLP-DKELVMPKNANVYYAVNT 755
Cdd:cd17209   1 DCCIIRVSLDVDNGNM-----YKSILVTSQDKTPVVIRKAMAKHNLDEEePEDYELLQILSeDRELKIPDNANVFYAMNS 75
                        90
                ....*....|.
gi 28574917 756 NYNLNFILRPR 766
Cdd:cd17209  76 TANYDFVLKKR 86
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
66-198 4.35e-17

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: 77.84  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917  66 TLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYdalHEKHLEELEQAQQNGQVMDPAydphasiheqh 145
Cdd:cd06224   1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERY---EIAPPENLEYNDWDKKKSKPI----------- 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574917 146 KKTLVSALHVWLDGFPEDWHED--NLQQILAFATKRLKRSDLHIKVLNRLERLIK 198
Cdd:cd06224  67 RLRVLNVLRTWVENYPYDFFDDeeLLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
62-175 4.48e-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: 71.57  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917    62 VKAATLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYDalHEKHLEELEQAQQNGQVMDPAydphasi 141
Cdd:pfam00618   2 VKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYN--IPPPLDLSSDSYWISKKTLPI------- 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 28574917   142 heqhKKTLVSALHVWLDGFPEDWHED--NLQQILAF 175
Cdd:pfam00618  73 ----RIRVLSVLRHWVENYFSDFNDDpvLLSRLEKF 104
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
681-766 3.48e-13

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: 65.73  E-value: 3.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 681 IIRVTYETDNIELdgivlYKSIMLGNNERTPQVIRNAMLKLGLEDD-PDRFTLAQVLP-DKELVMPKNANVYYAVNTNYN 758
Cdd:cd17212   5 VIRVSIDNDHGNL-----YRSILLTSQDKAPSVVQRALQKHNVPQPwARDYQLFQVLPgDRELLIPDNANVFYAMSPAAP 79

                ....*...
gi 28574917 759 LNFILRPR 766
Cdd:cd17212  80 GDFMLRRK 87
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
677-766 8.39e-13

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: 64.46  E-value: 8.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917 677 PDFYIIRVtyetdNIELDGIVLYKSIMLGNNERTPQVIRNAMLKLGLE-DDPDRFTLAQVLP-DKELVMPKNANVYYAVN 754
Cdd:cd17211   1 SDCRIIRV-----RMELHDGSVYKSILVTSQDKTPAVISRALEKHNQSsQAASPYELVQLLPeGKELTIPPTANVFYAMS 75
                        90
                ....*....|..
gi 28574917 755 TNyNLNFILRPR 766
Cdd:cd17211  76 SA-SLDFILRPR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
62-196 2.24e-10

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 58.88  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574917     62 VKAATLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRY-DALHEKHLEEleqaqqngqvmdpaydPHAS 140
Cdd:smart00229   5 IKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYnAIPPESWVEE----------------KVNP 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574917    141 IHEQHKktLVSALHVWLDGFPEDWHED-----NLQQILAFATKRlKRSDLHIKVLNRLERL 196
Cdd:smart00229  69 RRVKNR--VLNILRTWVENYWEDFEDDpklisFLLEFLELVDDE-KYPGLVTSLLNLLRRL 126
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
678-754 1.11e-09

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: 55.77  E-value: 1.11e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574917    678 DFYIIRVTYETDNIELdgivlYKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLP-DKELVMPKNANVYYAVN 754
Cdd:smart00314   1 DTFVLRVYVDDLPGGT-----YKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPdGKERVLPDDENPLQLQK 73
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
699-767 2.78e-08

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: 51.95  E-value: 2.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574917   699 YKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLP--DKELVMPKNANVYYAVNTNY----NLNFILRPRK 767
Cdd:pfam00788  18 YKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLErgGGERRLPDDECPLQIQLQWPrdasDSRFLLRKRD 92
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
699-752 2.54e-04

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: 40.38  E-value: 2.54e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28574917 699 YKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLP--DKELVMPKNANVYYA 752
Cdd:cd17043  15 YKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEkqETERVLHDDECPLLI 70
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
693-742 4.05e-04

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) 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. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 39.90  E-value: 4.05e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28574917 693 LDGIVLYKSIMLGNNERTPQVIRNAMLKLGLED-DPDRFTLAQVLPDKELV 742
Cdd:cd01783  10 LKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDeDPEDFRLVEVLMDKGVV 60
 
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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