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Conserved domains on  [gi|767908797|ref|XP_011507643|]
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ral guanine nucleotide dissociation stimulator-like 1 isoform X2 [Homo sapiens]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 13898967)

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 ...
 263-532 4.77e-90

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: 281.06  E-value: 4.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 263 FTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKEnkHLAPTIRATISQFNTLTKCVVSTILGGKELKtqQRAK 342
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNI--HLSPNLERFIERFNNLSNWVASEILLCTNPK--KRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 343 IIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTSKFa 422
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 423 nldssvkenqkrtqrrlqlqkdmgvmqgTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSacNS 502
Cdd:cd00155  156 ----------------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NS 205

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767908797 503 YCMTPDQKFIQWFQ--RQQLLTEEESYALSCE 532
Cdd:cd00155  206 YELNRDEDILAFLWklLELILNEDELYELSLE 237
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 619-683 4.34e-39

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


The actual alignment was detected with superfamily member cd17210:

Pssm-ID: 475130  Cd Length: 87  Bit Score: 138.97  E-value: 4.34e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767908797 619 LTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKK 683
Cdd:cd17210   23 LTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNFDFILRKK 87
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 100-231 3.09e-32

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: 121.29  E-value: 3.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   100 KIRTIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCeedgsQSSSESKMVIRNAI 179
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESW-----VEEKVNPRRVKNRV 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767908797   180 ASILRAWLDQCAEDFREPPH-FPCLQKLLDYLTRmMPGSDPERRAQNLLEQFQ 231
Cdd:smart00229  76 LNILRTWVENYWEDFEDDPKlISFLLEFLELVDD-EKYPGLVTSLLNLLRRLS 127
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 263-532 4.77e-90

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: 281.06  E-value: 4.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 263 FTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKEnkHLAPTIRATISQFNTLTKCVVSTILGGKELKtqQRAK 342
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNI--HLSPNLERFIERFNNLSNWVASEILLCTNPK--KRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 343 IIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTSKFa 422
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 423 nldssvkenqkrtqrrlqlqkdmgvmqgTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSacNS 502
Cdd:cd00155  156 ----------------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NS 205

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767908797 503 YCMTPDQKFIQWFQ--RQQLLTEEESYALSCE 532
Cdd:cd00155  206 YELNRDEDILAFLWklLELILNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
263-534 8.46e-88

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 275.66  E-value: 8.46e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   263 FTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKENKHLapTIRATISQFNTLTKCVVSTILGGKELKtqQRAK 342
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTTPK--DRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   343 IIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEgtskfa 422
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   423 nldssvkenqkrtqrrlqlqkdmgVMQGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSAcnS 502
Cdd:smart00147 151 ------------------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--P 204

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 767908797   503 YCMTPDQKFIQWFQRQ---QLLTEEESYALSCEIE 534
Cdd:smart00147 205 YNLRPNRSDIQSLLQQlldHLDEEEELYQLSLKIE 239
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 271-484 1.33e-72

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 233.25  E-value: 1.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797  271 VAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKENkhlAPTIRATISQFNTLTKCVVSTILggKELKTQQRAKIIEKWINI 350
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEIL--SEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797  351 AHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTskfanldssvke 430
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767908797  431 nqkrtqrrlqlqkdmgvmqGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRR 484
Cdd:pfam00617 145 -------------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 619-683 4.34e-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: 138.97  E-value: 4.34e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767908797 619 LTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKK 683
Cdd:cd17210   23 LTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNFDFILRKK 87
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 100-231 3.09e-32

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: 121.29  E-value: 3.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   100 KIRTIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCeedgsQSSSESKMVIRNAI 179
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESW-----VEEKVNPRRVKNRV 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767908797   180 ASILRAWLDQCAEDFREPPH-FPCLQKLLDYLTRmMPGSDPERRAQNLLEQFQ 231
Cdd:smart00229  76 LNILRTWVENYWEDFEDDPKlISFLLEFLELVDD-EKYPGLVTSLLNLLRRLS 127
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 108-232 2.14e-27

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: 107.11  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 108 TLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNltSPNCEEDGSQSSSESKMVIRNAIASILRAWL 187
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEI--APPENLEYNDWDKKKSKPIRLRVLNVLRTWV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767908797 188 DQCAEDFRepPHFPCLQKLLDYLTRMMPGSDPERRAQNLLEQFQK 232
Cdd:cd06224   79 ENYPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 103-208 2.42e-25

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: 100.84  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797  103 TIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCEEDgSQSSSESKMVIRNAIASI 182
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSD-SYWISKKTLPIRIRVLSV 79

                          90       100
                  ....*....|....*....|....*.
gi 767908797  183 LRAWLDQCAEDFREPPHfpCLQKLLD 208
Cdd:pfam00618  80 LRHWVENYFSDFNDDPV--LLSRLEK 103
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 606-684 1.73e-14

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: 69.25  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   606 ITPMDTPDEPQK--KLTSQDKTPAVIQRAMLKHNLDSDPaEEYELVQVISEDKELVIPDSANVFYAMN----SQVNFDFI 679
Cdd:smart00314   7 VYVDDLPGGTYKtlRVSSRTTARDVIQQLLEKFHLTDDP-EEYVLVEVLPDGKERVLPDDENPLQLQKlwprRGPNLRFV 85


                   ....*
gi 767908797   680 LRKKN 684
Cdd:smart00314  86 LRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 618-684 1.01e-07

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: 50.02  E-value: 1.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767908797  618 KLTSQDKTPAVIQRAMLKHNLDSDPaEEYELVQVI-SEDKELVIPDSANVFYAMN----SQVNFDFILRKKN 684
Cdd:pfam00788  22 LVSSSTTAEEVIEALLEKFGLEDDP-RDYVLVEVLeRGGGERRLPDDECPLQIQLqwprDASDSRFLLRKRD 92
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 263-532 4.77e-90

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: 281.06  E-value: 4.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 263 FTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKEnkHLAPTIRATISQFNTLTKCVVSTILGGKELKtqQRAK 342
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNI--HLSPNLERFIERFNNLSNWVASEILLCTNPK--KRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 343 IIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTSKFa 422
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 423 nldssvkenqkrtqrrlqlqkdmgvmqgTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSacNS 502
Cdd:cd00155  156 ----------------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NS 205

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767908797 503 YCMTPDQKFIQWFQ--RQQLLTEEESYALSCE 532
Cdd:cd00155  206 YELNRDEDILAFLWklLELILNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
263-534 8.46e-88

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 275.66  E-value: 8.46e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   263 FTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKENKHLapTIRATISQFNTLTKCVVSTILGGKELKtqQRAK 342
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTTPK--DRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   343 IIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEgtskfa 422
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   423 nldssvkenqkrtqrrlqlqkdmgVMQGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSAcnS 502
Cdd:smart00147 151 ------------------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--P 204

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 767908797   503 YCMTPDQKFIQWFQRQ---QLLTEEESYALSCEIE 534
Cdd:smart00147 205 YNLRPNRSDIQSLLQQlldHLDEEEELYQLSLKIE 239
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 271-484 1.33e-72

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 233.25  E-value: 1.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797  271 VAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKENkhlAPTIRATISQFNTLTKCVVSTILggKELKTQQRAKIIEKWINI 350
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEIL--SEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797  351 AHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTskfanldssvke 430
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767908797  431 nqkrtqrrlqlqkdmgvmqGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRR 484
Cdd:pfam00617 145 -------------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 619-683 4.34e-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: 138.97  E-value: 4.34e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767908797 619 LTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKK 683
Cdd:cd17210   23 LTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNFDFILRKK 87
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 100-231 3.09e-32

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: 121.29  E-value: 3.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   100 KIRTIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCeedgsQSSSESKMVIRNAI 179
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESW-----VEEKVNPRRVKNRV 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767908797   180 ASILRAWLDQCAEDFREPPH-FPCLQKLLDYLTRmMPGSDPERRAQNLLEQFQ 231
Cdd:smart00229  76 LNILRTWVENYWEDFEDDPKlISFLLEFLELVDD-EKYPGLVTSLLNLLRRLS 127
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 618-683 9.38e-31

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: 115.36  E-value: 9.38e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767908797 618 KLTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKK 683
Cdd:cd00153   23 LLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSANLNFILRKK 88
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 619-683 1.63e-30

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: 115.05  E-value: 1.63e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767908797 619 LTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKK 683
Cdd:cd17209   22 VTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYDFVLKKR 86
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 108-232 2.14e-27

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: 107.11  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 108 TLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNltSPNCEEDGSQSSSESKMVIRNAIASILRAWL 187
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEI--APPENLEYNDWDKKKSKPIRLRVLNVLRTWV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767908797 188 DQCAEDFRepPHFPCLQKLLDYLTRMMPGSDPERRAQNLLEQFQK 232
Cdd:cd06224   79 ENYPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 103-208 2.42e-25

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: 100.84  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797  103 TIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCEEDgSQSSSESKMVIRNAIASI 182
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSD-SYWISKKTLPIRIRVLSV 79

                          90       100
                  ....*....|....*....|....*.
gi 767908797  183 LRAWLDQCAEDFREPPHfpCLQKLLD 208
Cdd:pfam00618  80 LRHWVENYFSDFNDDPV--LLSRLEK 103
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
 619-683 9.92e-24

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: 95.39  E-value: 9.92e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767908797 619 LTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKK 683
Cdd:cd17212   23 LTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANVFYAMSPAAPGDFMLRRK 87
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 619-683 3.45e-23

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: 94.12  E-value: 3.45e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767908797 619 LTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQvNFDFILRKK 683
Cdd:cd17211   23 VTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSSA-SLDFILRPR 86
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 606-684 1.73e-14

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: 69.25  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797   606 ITPMDTPDEPQK--KLTSQDKTPAVIQRAMLKHNLDSDPaEEYELVQVISEDKELVIPDSANVFYAMN----SQVNFDFI 679
Cdd:smart00314   7 VYVDDLPGGTYKtlRVSSRTTARDVIQQLLEKFHLTDDP-EEYVLVEVLPDGKERVLPDDENPLQLQKlwprRGPNLRFV 85


                   ....*
gi 767908797   680 LRKKN 684
Cdd:smart00314  86 LRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 607-682 7.32e-08

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: 50.39  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908797 607 TPMDTPDEPQKKL--TSQDKTPAVIQRAMLKHNLDSDPaEEYELVQVI-SEDKELVIPDSANVFYAMNSQVN----FDFI 679
Cdd:cd17043    6 DDDLAPGSAYKSIlvSSTTTAREVVQLLLEKYGLEEDP-EDYSLYEVSeKQETERVLHDDECPLLIQLEWGPqgteFRFV 84


                 ...
gi 767908797 680 LRK 682
Cdd:cd17043   85 LKR 87
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 618-684 1.01e-07

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: 50.02  E-value: 1.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767908797  618 KLTSQDKTPAVIQRAMLKHNLDSDPaEEYELVQVI-SEDKELVIPDSANVFYAMN----SQVNFDFILRKKN 684
Cdd:pfam00788  22 LVSSSTTAEEVIEALLEKFGLEDDP-RDYVLVEVLeRGGGERRLPDDECPLQIQLqwprDASDSRFLLRKRD 92
 
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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