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Conserved domains on  [gi|422010879|ref|NP_001258703|]
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ral guanine nucleotide dissociation stimulator isoform 3 [Homo sapiens]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 13898960)

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 ...
 353-615 3.03e-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: 285.69  E-value: 3.03e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 353 LLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKgkEHLAPTIRATVTQFNSVANCVITTCLGnrSTKAPDRAR 432
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILL--CTNPKKRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 433 VVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTSKFa 512
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 513 tlemnpkraqkrpketgiiqgTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSacNNYSIAPDE 592
Cdd:cd00155  156 ---------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELNRDE 212

                        250       260
                 ....*....|....*....|....*
gi 422010879 593 QFGAWFRAVER--LSETESYNLSCE 615
Cdd:cd00155  213 DILAFLWKLLEliLNEDELYELSLE 237
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 769-854 2.15e-47

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: 163.20  E-value: 2.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYD 848
Cdd:cd17209    1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                 ....*.
gi 422010879 849 FVLKKR 854
Cdd:cd17209   81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 95-219 1.46e-37

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: 136.70  E-value: 1.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879    95 KVRTVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGCILPYS-DEDGGPQDQLKNAISSILG 173
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESwVEEKVNPRRVKNRVLNILR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 422010879   174 TWLDQYSEDFCQPP-DFPCLKQLvAYVQLNMPGSDLERRAHLLLAQL 219
Cdd:smart00229  81 TWVENYWEDFEDDPkLISFLLEF-LELVDDEKYPGLVTSLLNLLRRL 126
GGN super family cl37895
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 275-329 3.84e-07

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


The actual alignment was detected with superfamily member pfam15685:

Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 54.00  E-value: 3.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 422010879  275 ELEVAPAPAPELqqapEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPV 329
Cdd:pfam15685 487 ESALAPAPTAPL----PPALAADQAPAPALAAAPAPSPAPAPATADPLPPAPAPI 537
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
222-370 5.75e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 222 SEPIEAEPEALSPVPALKPTPELELAltparapSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAVGLESAPA 301
Cdd:PRK12323 379 AAPVAQPAPAAAAPAAAAPAPAAPPA-------APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010879 302 PALELEPAPEQDPAPSQtleLEPAPAPVPSLQPSwPSPVVAENGLSEEKPHLLVFPPDLVAEQFTLMDA 370
Cdd:PRK12323 452 PAPAAAPAAAARPAAAG---PRPVAAAAAAAPAR-AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 353-615 3.03e-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: 285.69  E-value: 3.03e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 353 LLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKgkEHLAPTIRATVTQFNSVANCVITTCLGnrSTKAPDRAR 432
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILL--CTNPKKRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 433 VVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTSKFa 512
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 513 tlemnpkraqkrpketgiiqgTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSacNNYSIAPDE 592
Cdd:cd00155  156 ---------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELNRDE 212

                        250       260
                 ....*....|....*....|....*
gi 422010879 593 QFGAWFRAVER--LSETESYNLSCE 615
Cdd:cd00155  213 DILAFLWKLLEliLNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
353-620 1.61e-87

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 278.36  E-value: 1.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   353 LLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKEHLapTIRATVTQFNSVANCVITTCLGnrSTKAPDRAR 432
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILK--QTTPKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   433 VVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTskfa 512
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNL---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   513 tlemnpkraqkrpketgiiQGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSAcnNYSIAPDE 592
Cdd:smart00147 153 -------------------PPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLRPNR 211

                          250       260       270
                   ....*....|....*....|....*....|.
gi 422010879   593 Q-FGAWFRAVERL--SETESYNLSCELEPPS 620
Cdd:smart00147 212 SdIQSLLQQLLDHldEEEELYQLSLKIEPRV 242
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 361-567 4.41e-71

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 232.10  E-value: 4.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879  361 VAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKehlAPTIRATVTQFNSVANCVITTCLgnRSTKAPDRARVVEHWIEV 440
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEIL--SEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879  441 ARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTskfatlemnpkr 520
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 422010879  521 aqkrpketgiiqGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRR 567
Cdd:pfam00617 145 ------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 769-854 2.15e-47

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: 163.20  E-value: 2.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYD 848
Cdd:cd17209    1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                 ....*.
gi 422010879 849 FVLKKR 854
Cdd:cd17209   81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 95-219 1.46e-37

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: 136.70  E-value: 1.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879    95 KVRTVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGCILPYS-DEDGGPQDQLKNAISSILG 173
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESwVEEKVNPRRVKNRVLNILR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 422010879   174 TWLDQYSEDFCQPP-DFPCLKQLvAYVQLNMPGSDLERRAHLLLAQL 219
Cdd:smart00229  81 TWVENYWEDFEDDPkLISFLLEF-LELVDDEKYPGLVTSLLNLLRRL 126
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 103-221 1.20e-29

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: 114.05  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 103 TLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRY----GCILPYSDEDGGPQDQLKNAISSILGTWLDQ 178
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYeiapPENLEYNDWDKKKSKPIRLRVLNVLRTWVEN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 422010879 179 YSEDFCqpPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQLEH 221
Cdd:cd06224   81 YPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 98-196 1.16e-26

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: 104.69  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   98 TVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGCILPY-----SDEDGGPQDQLKNAISSIL 172
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLdlssdSYWISKKTLPIRIRVLSVL 80

                          90       100
                  ....*....|....*....|....
gi 422010879  173 GTWLDQYSEDFCQPPdfPCLKQLV 196
Cdd:pfam00618  81 RHWVENYFSDFNDDP--VLLSRLE 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 769-854 5.47e-13

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: 65.40  E-value: 5.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNlEEEEPEDYELLQILSDDRKLKIPENANVFYAMN----ST 844
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFH-LTDDPEEYVLVEVLPDGKERVLPDDENPLQLQKlwprRG 79

                           90
                   ....*....|
gi 422010879   845 ANYDFVLKKR 854
Cdd:smart00314  80 PNLRFVLRKR 89
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 769-854 1.24e-09

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: 55.80  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879  769 DCCIIRVSLDVDN-GNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMN----S 843
Cdd:pfam00788   1 DDGVLKVYTEDGKpGTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLERGGGERRLPDDECPLQIQLqwprD 80

                          90
                  ....*....|.
gi 422010879  844 TANYDFVLKKR 854
Cdd:pfam00788  81 ASDSRFLLRKR 91
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 275-329 3.84e-07

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 54.00  E-value: 3.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 422010879  275 ELEVAPAPAPELqqapEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPV 329
Cdd:pfam15685 487 ESALAPAPTAPL----PPALAADQAPAPALAAAPAPSPAPAPATADPLPPAPAPI 537
PRK04654 PRK04654
sec-independent translocase; Provisional
 273-350 1.98e-04

sec-independent translocase; Provisional


Pssm-ID: 135173 [Multi-domain]  Cd Length: 214  Bit Score: 43.65  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 273 GSELEVAPAPAPELQQAPEPAVGLESAPAPALELEPAPEQDPAPSQ-TLELEPAPAPVPSLQP----SWPSPVVAENGLS 347
Cdd:PRK04654 130 GAEPGAGQAHTPVPAPAPVIAQAQPIAPAPHQTLVPAPHDTIVPAPhAAHLPSAPATPVSVAPvdagTSASPTPSEPTKI 209


                 ...
gi 422010879 348 EEK 350
Cdd:PRK04654 210 QEK 212
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
224-373 2.23e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 224 PIEAEPEALSPVPALKPTPELELALTPARAPSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAvglesAPAPA 303
Cdd:PRK12323 392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAA-----ARPAA 466

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 304 LELEPAPEQDPAPSQTLELEPAPAPVPSLQPSWpspvvaenglSEEKPHLLVFPPDLVAEQFTLMDAELF 373
Cdd:PRK12323 467 AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPW----------EELPPEFASPAPAQPDAAPAGWVAESI 526
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
222-370 5.75e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 222 SEPIEAEPEALSPVPALKPTPELELAltparapSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAVGLESAPA 301
Cdd:PRK12323 379 AAPVAQPAPAAAAPAAAAPAPAAPPA-------APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010879 302 PALELEPAPEQDPAPSQtleLEPAPAPVPSLQPSwPSPVVAENGLSEEKPHLLVFPPDLVAEQFTLMDA 370
Cdd:PRK12323 452 PAPAAAPAAAARPAAAG---PRPVAAAAAAAPAR-AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
COG5373 COG5373
Uncharacterized membrane protein [Function unknown];
274-347 2.54e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444140 [Multi-domain]  Cd Length: 854  Bit Score: 41.52  E-value: 2.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010879 274 SELE---VAPAPAPELQQAPEP-AVGLESAPAPALELEPAPEQDPAPSQTLElepAPAPVPSLQPSWPSPVVAENGLS 347
Cdd:COG5373   31 EELEaelAEAAEAASAPAEPEPeAAAAATAAAPEAAPAPVPEAPAAPPAAAE---APAPAAAAPPAEAEPAAAPAAAS 105
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 353-615 3.03e-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: 285.69  E-value: 3.03e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 353 LLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKgkEHLAPTIRATVTQFNSVANCVITTCLGnrSTKAPDRAR 432
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILL--CTNPKKRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 433 VVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTSKFa 512
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 513 tlemnpkraqkrpketgiiqgTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSacNNYSIAPDE 592
Cdd:cd00155  156 ---------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELNRDE 212

                        250       260
                 ....*....|....*....|....*
gi 422010879 593 QFGAWFRAVER--LSETESYNLSCE 615
Cdd:cd00155  213 DILAFLWKLLEliLNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
353-620 1.61e-87

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 278.36  E-value: 1.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   353 LLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKEHLapTIRATVTQFNSVANCVITTCLGnrSTKAPDRAR 432
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILK--QTTPKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   433 VVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTskfa 512
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNL---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   513 tlemnpkraqkrpketgiiQGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSAcnNYSIAPDE 592
Cdd:smart00147 153 -------------------PPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLRPNR 211

                          250       260       270
                   ....*....|....*....|....*....|.
gi 422010879   593 Q-FGAWFRAVERL--SETESYNLSCELEPPS 620
Cdd:smart00147 212 SdIQSLLQQLLDHldEEEELYQLSLKIEPRV 242
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 361-567 4.41e-71

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 232.10  E-value: 4.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879  361 VAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKehlAPTIRATVTQFNSVANCVITTCLgnRSTKAPDRARVVEHWIEV 440
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEIL--SEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879  441 ARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTskfatlemnpkr 520
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 422010879  521 aqkrpketgiiqGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRR 567
Cdd:pfam00617 145 ------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 769-854 2.15e-47

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: 163.20  E-value: 2.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYD 848
Cdd:cd17209    1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                 ....*.
gi 422010879 849 FVLKKR 854
Cdd:cd17209   81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 95-219 1.46e-37

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: 136.70  E-value: 1.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879    95 KVRTVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGCILPYS-DEDGGPQDQLKNAISSILG 173
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESwVEEKVNPRRVKNRVLNILR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 422010879   174 TWLDQYSEDFCQPP-DFPCLKQLvAYVQLNMPGSDLERRAHLLLAQL 219
Cdd:smart00229  81 TWVENYWEDFEDDPkLISFLLEF-LELVDDEKYPGLVTSLLNLLRRL 126
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 769-854 2.42e-36

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: 131.65  E-value: 2.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYD 848
Cdd:cd17210    2 DTCIIRVSVEDNNGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNFD 81


                 ....*.
gi 422010879 849 FVLKKR 854
Cdd:cd17210   82 FILRKK 87
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 769-854 6.29e-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: 130.77  E-value: 6.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 769 DCCIIRVSLD--VDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTAN 846
Cdd:cd00153    1 DSRIIRVSLEdgSEDGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAN 80


                 ....*...
gi 422010879 847 YDFVLKKR 854
Cdd:cd00153   81 LNFILRKK 88
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 103-221 1.20e-29

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: 114.05  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 103 TLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRY----GCILPYSDEDGGPQDQLKNAISSILGTWLDQ 178
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYeiapPENLEYNDWDKKKSKPIRLRVLNVLRTWVEN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 422010879 179 YSEDFCqpPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQLEH 221
Cdd:cd06224   81 YPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
 772-854 1.53e-29

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: 112.34  E-value: 1.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 772 IIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYDFVL 851
Cdd:cd17212    5 VIRVSIDNDHGNLYRSILLTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANVFYAMSPAAPGDFML 84


                 ...
gi 422010879 852 KKR 854
Cdd:cd17212   85 RRK 87
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 769-854 1.59e-27

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: 106.45  E-value: 1.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNStANYD 848
Cdd:cd17211    2 DCRIIRVRMELHDGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSS-ASLD 80


                 ....*.
gi 422010879 849 FVLKKR 854
Cdd:cd17211   81 FILRPR 86
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 98-196 1.16e-26

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: 104.69  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   98 TVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGCILPY-----SDEDGGPQDQLKNAISSIL 172
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLdlssdSYWISKKTLPIRIRVLSVL 80

                          90       100
                  ....*....|....*....|....
gi 422010879  173 GTWLDQYSEDFCQPPdfPCLKQLV 196
Cdd:pfam00618  81 RHWVENYFSDFNDDP--VLLSRLE 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 769-854 5.47e-13

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: 65.40  E-value: 5.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879   769 DCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNlEEEEPEDYELLQILSDDRKLKIPENANVFYAMN----ST 844
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFH-LTDDPEEYVLVEVLPDGKERVLPDDENPLQLQKlwprRG 79

                           90
                   ....*....|
gi 422010879   845 ANYDFVLKKR 854
Cdd:smart00314  80 PNLRFVLRKR 89
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 769-854 1.24e-09

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: 55.80  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879  769 DCCIIRVSLDVDN-GNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMN----S 843
Cdd:pfam00788   1 DDGVLKVYTEDGKpGTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLERGGGERRLPDDECPLQIQLqwprD 80

                          90
                  ....*....|.
gi 422010879  844 TANYDFVLKKR 854
Cdd:pfam00788  81 ASDSRFLLRKR 91
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 275-329 3.84e-07

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 54.00  E-value: 3.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 422010879  275 ELEVAPAPAPELqqapEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPV 329
Cdd:pfam15685 487 ESALAPAPTAPL----PPALAADQAPAPALAAAPAPSPAPAPATADPLPPAPAPI 537
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 280-332 2.18e-05

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 45.17  E-value: 2.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 422010879  280 PAPAPELQQAPEPAVGLESAPAPALELEPAPEQDPAPsqtlelEPAPAPVPSL 332
Cdd:pfam05887  73 PEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP------EPGAATLKSV 119
PRK04654 PRK04654
sec-independent translocase; Provisional
 273-350 1.98e-04

sec-independent translocase; Provisional


Pssm-ID: 135173 [Multi-domain]  Cd Length: 214  Bit Score: 43.65  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 273 GSELEVAPAPAPELQQAPEPAVGLESAPAPALELEPAPEQDPAPSQ-TLELEPAPAPVPSLQP----SWPSPVVAENGLS 347
Cdd:PRK04654 130 GAEPGAGQAHTPVPAPAPVIAQAQPIAPAPHQTLVPAPHDTIVPAPhAAHLPSAPATPVSVAPvdagTSASPTPSEPTKI 209


                 ...
gi 422010879 348 EEK 350
Cdd:PRK04654 210 QEK 212
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
224-373 2.23e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 224 PIEAEPEALSPVPALKPTPELELALTPARAPSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAvglesAPAPA 303
Cdd:PRK12323 392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAA-----ARPAA 466

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 304 LELEPAPEQDPAPSQTLELEPAPAPVPSLQPSWpspvvaenglSEEKPHLLVFPPDLVAEQFTLMDAELF 373
Cdd:PRK12323 467 AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPW----------EELPPEFASPAPAQPDAAPAGWVAESI 526
PRK11633 PRK11633
cell division protein DedD; Provisional
 273-334 3.92e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 42.68  E-value: 3.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010879 273 GSELEVAPAPAPELQQ----APEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPVPSLQP 334
Cdd:PRK11633  72 AEAVRAGDAAAPSLDPatvaPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKP 137
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
222-370 5.75e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 222 SEPIEAEPEALSPVPALKPTPELELAltparapSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAVGLESAPA 301
Cdd:PRK12323 379 AAPVAQPAPAAAAPAAAAPAPAAPPA-------APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010879 302 PALELEPAPEQDPAPSQtleLEPAPAPVPSLQPSwPSPVVAENGLSEEKPHLLVFPPDLVAEQFTLMDA 370
Cdd:PRK12323 452 PAPAAAPAAAARPAAAG---PRPVAAAAAAAPAR-AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
COG5373 COG5373
Uncharacterized membrane protein [Function unknown];
274-347 2.54e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444140 [Multi-domain]  Cd Length: 854  Bit Score: 41.52  E-value: 2.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010879 274 SELE---VAPAPAPELQQAPEP-AVGLESAPAPALELEPAPEQDPAPSQTLElepAPAPVPSLQPSWPSPVVAENGLS 347
Cdd:COG5373   31 EELEaelAEAAEAASAPAEPEPeAAAAATAAAPEAAPAPVPEAPAAPPAAAE---APAPAAAAPPAEAEPAAAPAAAS 105
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 772-853 2.67e-03

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: 37.68  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 772 IIRVSLDVDNGN-MYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYD-- 848
Cdd:cd17043    1 VLKVYDDDLAPGsAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGte 80


                 ....*..
gi 422010879 849 --FVLKK 853
Cdd:cd17043   81 frFVLKR 87
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 279-351 3.05e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 41.09  E-value: 3.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010879 279 APAPAPELQQApepAVGLESAPAPALELEPAPEQDPAPSQTleLEPAPAPVPSLQPSWPSPVVAENGLSEEKP 351
Cdd:PHA03291 190 LPLSAPRLGPA---DVFVPATPRPTPRTTASPETTPTPSTT--TSPPSTTIPAPSTTIAAPQAGTTPEAEGTP 257
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
 282-334 3.30e-03

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 461548 [Multi-domain]  Cd Length: 140  Bit Score: 38.95  E-value: 3.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 422010879  282 PAPELQQAPEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPVPSLQP 334
Cdd:pfam05104  55 QADESEEEPREFKTPDEAPSAALEPEPVPTPVPAPVEPEPAPPSESPAPSPKE 107
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 279-363 6.26e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.08  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 279 APAPAPELQQAPEPAVGLESAPAPalELEPAPEQDPAPSQTLELEPAPAPVPSLQPSWPSPVVAENGLSEEKPHLLVFPP 358
Cdd:PRK14951 370 AEAAAPAEKKTPARPEAAAPAAAP--VAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL 447


                 ....*
gi 422010879 359 DLVAE 363
Cdd:PRK14951 448 APAPP 452
PHA03378 PHA03378
EBNA-3B; Provisional
 224-335 6.33e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 224 PIEAEPEALSPVPALKPTPELELALTPARAPSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAVGlesAPAPa 303
Cdd:PHA03378 701 PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG---APTP- 776

                         90       100       110
                 ....*....|....*....|....*....|..
gi 422010879 304 lelEPAPEQDPAPSQTLELEPAPAPVPSLQPS 335
Cdd:PHA03378 777 ---QPPPQAPPAPQQRPRGAPTPQPPPQAGPT 805
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 277-340 6.56e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 40.31  E-value: 6.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010879 277 EVAPAPA---PELQQAPEPavglesaPAPALELEPAPEQDPAPSQTLELEPAPA--PVPSLQPSWPSPV 340
Cdd:PRK14954 379 GVAPSPAgspDVKKKAPEP-------DLPQPDRHPGPAKPEAPGARPAELPSPAsaPTPEQQPPVARSA 440
PRK11633 PRK11633
cell division protein DedD; Provisional
 275-351 7.08e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 38.83  E-value: 7.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010879 275 ELEVAPAPAPEL-QQAPEPAV-GLESAPAPALELEPA--------PEQDPAPSQTLELEPAPAPVPSLQPSwPSPVVAEN 344
Cdd:PRK11633  52 EPDMMPAATQALpTQPPEGAAeAVRAGDAAAPSLDPAtvappntpVEPEPAPVEPPKPKPVEKPKPKPKPQ-QKVEAPPA 130


                 ....*..
gi 422010879 345 GLSEEKP 351
Cdd:PRK11633 131 PKPEPKP 137
 
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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