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Conserved domains on  [gi|189491671|ref|NP_766081|]
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protein diaphanous homolog 2 [Mus musculus]

Protein Classification

Drf_FH3 and FH2 domain-containing protein( domain architecture ID 10533905)

protein containing domains Drf_GBD, Drf_FH3, and FH2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
629-1003 3.05e-125

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 387.78  E-value: 3.05e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   629 QKKLYKPDIPMKRINWSKIEPKELSEnCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNteaAEENRSGPPKKKVKELR 708
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKN---KKSEDKSSSKKKPKEVS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   709 ILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTV 788
Cdd:pfam02181   77 LLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   789 KMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDT 868
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   869 KSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKM 948
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 189491671   949 MSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLF 1003
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
295-483 2.73e-66

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


:

Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 221.38  E-value: 2.73e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   295 DKLLGGITAAAELN-NRERFSPIVEGLENNEALH--LQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEI 371
Cdd:pfam06367    4 EKVLEATLNFKEVCrERGRFQSLVGALDSSENDNveYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   372 ENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKI 451
Cdd:pfam06367   84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                          170       180       190
                   ....*....|....*....|....*....|..
gi 189491671   452 IEECVSQIVLHCSGMDPDFKYRQRIDFDFTHL 483
Cdd:pfam06367  164 LEELVSQIVLHRTKPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
102-287 1.40e-64

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 216.41  E-value: 1.40e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   102 LILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSGGL---KNSKHEFTLSSQEYVHELRSGIS 178
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEGGgskSDSESNETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   179 DEKllnCLESLRVSLTSHPVSWVNNF-GYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDE 257
Cdd:pfam06371   82 SSK---QLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHP 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 189491671   258 RSLLLLARAIDPKQQNMMTEIVKILSAICI 287
Cdd:pfam06371  159 SSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
629-1003 3.05e-125

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 387.78  E-value: 3.05e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   629 QKKLYKPDIPMKRINWSKIEPKELSEnCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNteaAEENRSGPPKKKVKELR 708
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKN---KKSEDKSSSKKKPKEVS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   709 ILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTV 788
Cdd:pfam02181   77 LLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   789 KMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDT 868
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   869 KSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKM 948
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 189491671   949 MSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLF 1003
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
630-1065 1.09e-124

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 387.09  E-value: 1.09e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    630 KKLYKPDIPMKRINWSKIEPKELSEnCVWLKLKEEkyeNADLFAKLALTFPSQMKGQRNTEAAEENRSGPPKKKVKELRI 709
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASQEFKI 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    710 LDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSE-YDDLCEPEQFGVVMSTV 788
Cdd:smart00498   77 LDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    789 KMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDT 868
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    869 KSADQKSTLLHFLAEICDEKYrdilkfpdelehvesagkvsaqilksnlvameqsilhleknIKNFPPAESHHDKFVEKM 948
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIEVM 275
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    949 MSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLFLEALKENHKRKEmEEKSRRAKLAKE 1028
Cdd:smart00498  276 KPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLVKE 354
                           410       420       430
                    ....*....|....*....|....*....|....*...
gi 189491671   1029 KAEQEKL-ERQKKKKQLIDINKEGDETGVMDNLLEALQ 1065
Cdd:smart00498  355 TTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
295-483 2.73e-66

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 221.38  E-value: 2.73e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   295 DKLLGGITAAAELN-NRERFSPIVEGLENNEALH--LQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEI 371
Cdd:pfam06367    4 EKVLEATLNFKEVCrERGRFQSLVGALDSSENDNveYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   372 ENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKI 451
Cdd:pfam06367   84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                          170       180       190
                   ....*....|....*....|....*....|..
gi 189491671   452 IEECVSQIVLHCSGMDPDFKYRQRIDFDFTHL 483
Cdd:pfam06367  164 LEELVSQIVLHRTKPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
102-287 1.40e-64

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 216.41  E-value: 1.40e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   102 LILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSGGL---KNSKHEFTLSSQEYVHELRSGIS 178
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEGGgskSDSESNETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   179 DEKllnCLESLRVSLTSHPVSWVNNF-GYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDE 257
Cdd:pfam06371   82 SSK---QLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHP 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 189491671   258 RSLLLLARAIDPKQQNMMTEIVKILSAICI 287
Cdd:pfam06371  159 SSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
629-1003 3.05e-125

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 387.78  E-value: 3.05e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   629 QKKLYKPDIPMKRINWSKIEPKELSEnCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNteaAEENRSGPPKKKVKELR 708
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKN---KKSEDKSSSKKKPKEVS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   709 ILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTV 788
Cdd:pfam02181   77 LLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   789 KMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDT 868
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   869 KSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKM 948
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 189491671   949 MSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLF 1003
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
630-1065 1.09e-124

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 387.09  E-value: 1.09e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    630 KKLYKPDIPMKRINWSKIEPKELSEnCVWLKLKEEkyeNADLFAKLALTFPSQMKGQRNTEAAEENRSGPPKKKVKELRI 709
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASQEFKI 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    710 LDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSE-YDDLCEPEQFGVVMSTV 788
Cdd:smart00498   77 LDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    789 KMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDT 868
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    869 KSADQKSTLLHFLAEICDEKYrdilkfpdelehvesagkvsaqilksnlvameqsilhleknIKNFPPAESHHDKFVEKM 948
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIEVM 275
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671    949 MSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLFLEALKENHKRKEmEEKSRRAKLAKE 1028
Cdd:smart00498  276 KPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLVKE 354
                           410       420       430
                    ....*....|....*....|....*....|....*...
gi 189491671   1029 KAEQEKL-ERQKKKKQLIDINKEGDETGVMDNLLEALQ 1065
Cdd:smart00498  355 TTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
295-483 2.73e-66

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 221.38  E-value: 2.73e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   295 DKLLGGITAAAELN-NRERFSPIVEGLENNEALH--LQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEI 371
Cdd:pfam06367    4 EKVLEATLNFKEVCrERGRFQSLVGALDSSENDNveYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   372 ENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKI 451
Cdd:pfam06367   84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                          170       180       190
                   ....*....|....*....|....*....|..
gi 189491671   452 IEECVSQIVLHCSGMDPDFKYRQRIDFDFTHL 483
Cdd:pfam06367  164 LEELVSQIVLHRTKPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
102-287 1.40e-64

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 216.41  E-value: 1.40e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   102 LILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSGGL---KNSKHEFTLSSQEYVHELRSGIS 178
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEGGgskSDSESNETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491671   179 DEKllnCLESLRVSLTSHPVSWVNNF-GYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDE 257
Cdd:pfam06371   82 SSK---QLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHP 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 189491671   258 RSLLLLARAIDPKQQNMMTEIVKILSAICI 287
Cdd:pfam06371  159 SSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
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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