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Conserved domains on  [gi|440214006|gb|AGB93175|]
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diaphanous, isoform E [Drosophila melanogaster]

Protein Classification

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

protein containing domains Drf_GBD, Drf_FH3, and FH2

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
601-976 2.96e-128

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 395.49  E-value: 2.96e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   601 PKKKWDVKNPMKRANWKAIVPAKMSDkAFWVKCQEDKLAQDDFLAELAVKFSSKPVKKEQKDAVDKPTtLTKKNVDLRVL 680
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSS-SKKKPKEVSLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   681 DSKTAQNLAIMLGgSLkHLSYEQIKICLLRCDTDILSSNILQQLIQYLPPPEHLKRLQEIKAKGEPLPPIEQFAATIGEI 760
Cdd:pfam02181   79 DPKRAQNIAILLR-KL-KLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   761 KRLSPRLHNLNFKLTYADMVQDIKPDIVAGTAACEEIRNSKKFSKILELILLLGNYMNSGSKNEAAFGFEISYLTKLSNT 840
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   841 KDADNKQTLLHYLADLVEKKFPDALNFYDDLSHVNKASRVNMDAIQKAMRQMNSAVKNLETDLQNNKVPQCDDDKFSEVM 920
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 440214006   921 GKFAEECRQQVDVLGKMQLQMEKLYKDLSEYYAFDPSKYTMEEFFADIKTFKDAFQ 976
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
246-446 5.45e-62

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: 209.44  E-value: 5.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   246 NGYEKVLRAITTIAATSFKaSERFRPIVDALfaSDQQDPKRDLACHSLIFINTLTNTPTDLNFRLHLRCEIMRMGLYDRL 325
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRE-RGRFQSLVGAL--DSSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   326 DEFTKIveasNNENLQQHFKIFNEIREDDFEEFVQRFDNVTFNMDDATDCFDVLKNLVTDTTSEPYFLSILQHLLYIRDD 405
Cdd:pfam06367   78 DKLREL----ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 440214006   406 FYFRPAYYQLIEECISQIVFHKGYCDPNFENR-NFNIDTSLL 446
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
59-241 5.03e-57

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: 195.23  E-value: 5.03e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    59 IQQLSVAELDAKFLEIIEDMNIPKDKREPLLAKSKEERQKMIMWHLKGKNSLE------RSANSRFEKPIDYVEYLQNGE 132
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   133 HSThkvyQCVESLRVALTSNPISWIKEF-GVAGIGTIEKLLARSKNNASYE----KIEFEAIRCLKAIMNNTWGLNVVLN 207
Cdd:pfam06371   81 ISS----KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEeedlDREYEILKCLKALMNNKFGLDHVLG 156
                          170       180       190
                   ....*....|....*....|....*....|....
gi 440214006   208 pdQHSVVLLLAQSLDPRKPQTMCEALKLLASFCI 241
Cdd:pfam06371  157 --HPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
601-976 2.96e-128

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 395.49  E-value: 2.96e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   601 PKKKWDVKNPMKRANWKAIVPAKMSDkAFWVKCQEDKLAQDDFLAELAVKFSSKPVKKEQKDAVDKPTtLTKKNVDLRVL 680
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSS-SKKKPKEVSLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   681 DSKTAQNLAIMLGgSLkHLSYEQIKICLLRCDTDILSSNILQQLIQYLPPPEHLKRLQEIKAKGEPLPPIEQFAATIGEI 760
Cdd:pfam02181   79 DPKRAQNIAILLR-KL-KLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   761 KRLSPRLHNLNFKLTYADMVQDIKPDIVAGTAACEEIRNSKKFSKILELILLLGNYMNSGSKNEAAFGFEISYLTKLSNT 840
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   841 KDADNKQTLLHYLADLVEKKFPDALNFYDDLSHVNKASRVNMDAIQKAMRQMNSAVKNLETDLQNNKVPQCDDDKFSEVM 920
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 440214006   921 GKFAEECRQQVDVLGKMQLQMEKLYKDLSEYYAFDPSKYTMEEFFADIKTFKDAFQ 976
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
602-1037 4.42e-120

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: 374.76  E-value: 4.42e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    602 KKKWDVKNPMKRANWKAIVPAKMSDKaFWVKCQEDklaQDDFLAELAVKFSSKPVKKEQKDAVDKPTTLTKKNVD--LRV 679
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGT-VWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASqeFKI 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    680 LDSKTAQNLAIMLGGSlkHLSYEQIKICLLRCDTDILSSNILQQLIQYLPPPEHLKRLQEIK-AKGEPLPPIEQFAATIG 758
Cdd:smart00498   77 LDPKRSQNLAILLRKL--HMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKeEDPEELARAEQFLLLIS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    759 EIKRLSPRLHNLNFKLTYADMVQDIKPDIVAGTAACEEIRNSKKFSKILELILLLGNYMNSGSKNEAAFGFEISYLTKLS 838
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    839 NTKDADNKQTLLHYLADLVEKKFpdalnfyddlshvnkasrvnmdaiqkamrqmnsavknletdLQNNKVPQCDDDKFSE 918
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    919 VMGKFAEECRQQVDVLGKMQLQMEKLYKDLSEYYAFDPSKYTMEEFFADIKTFKDAFQAAHNDNVRVREElEKKRRLQEA 998
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEE-EEERRKKLV 352
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 440214006    999 REQSAREQ-QERQQRKKAVVDMDAPQTQEGVMDSLLEALQ 1037
Cdd:smart00498  353 KETTEYEQsSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
246-446 5.45e-62

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: 209.44  E-value: 5.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   246 NGYEKVLRAITTIAATSFKaSERFRPIVDALfaSDQQDPKRDLACHSLIFINTLTNTPTDLNFRLHLRCEIMRMGLYDRL 325
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRE-RGRFQSLVGAL--DSSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   326 DEFTKIveasNNENLQQHFKIFNEIREDDFEEFVQRFDNVTFNMDDATDCFDVLKNLVTDTTSEPYFLSILQHLLYIRDD 405
Cdd:pfam06367   78 DKLREL----ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 440214006   406 FYFRPAYYQLIEECISQIVFHKGYCDPNFENR-NFNIDTSLL 446
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
59-241 5.03e-57

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: 195.23  E-value: 5.03e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    59 IQQLSVAELDAKFLEIIEDMNIPKDKREPLLAKSKEERQKMIMWHLKGKNSLE------RSANSRFEKPIDYVEYLQNGE 132
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   133 HSThkvyQCVESLRVALTSNPISWIKEF-GVAGIGTIEKLLARSKNNASYE----KIEFEAIRCLKAIMNNTWGLNVVLN 207
Cdd:pfam06371   81 ISS----KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEeedlDREYEILKCLKALMNNKFGLDHVLG 156
                          170       180       190
                   ....*....|....*....|....*....|....
gi 440214006   208 pdQHSVVLLLAQSLDPRKPQTMCEALKLLASFCI 241
Cdd:pfam06371  157 --HPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
601-976 2.96e-128

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 395.49  E-value: 2.96e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   601 PKKKWDVKNPMKRANWKAIVPAKMSDkAFWVKCQEDKLAQDDFLAELAVKFSSKPVKKEQKDAVDKPTtLTKKNVDLRVL 680
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSS-SKKKPKEVSLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   681 DSKTAQNLAIMLGgSLkHLSYEQIKICLLRCDTDILSSNILQQLIQYLPPPEHLKRLQEIKAKGEPLPPIEQFAATIGEI 760
Cdd:pfam02181   79 DPKRAQNIAILLR-KL-KLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   761 KRLSPRLHNLNFKLTYADMVQDIKPDIVAGTAACEEIRNSKKFSKILELILLLGNYMNSGSKNEAAFGFEISYLTKLSNT 840
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   841 KDADNKQTLLHYLADLVEKKFPDALNFYDDLSHVNKASRVNMDAIQKAMRQMNSAVKNLETDLQNNKVPQCDDDKFSEVM 920
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 440214006   921 GKFAEECRQQVDVLGKMQLQMEKLYKDLSEYYAFDPSKYTMEEFFADIKTFKDAFQ 976
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
602-1037 4.42e-120

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: 374.76  E-value: 4.42e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    602 KKKWDVKNPMKRANWKAIVPAKMSDKaFWVKCQEDklaQDDFLAELAVKFSSKPVKKEQKDAVDKPTTLTKKNVD--LRV 679
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGT-VWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASqeFKI 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    680 LDSKTAQNLAIMLGGSlkHLSYEQIKICLLRCDTDILSSNILQQLIQYLPPPEHLKRLQEIK-AKGEPLPPIEQFAATIG 758
Cdd:smart00498   77 LDPKRSQNLAILLRKL--HMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKeEDPEELARAEQFLLLIS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    759 EIKRLSPRLHNLNFKLTYADMVQDIKPDIVAGTAACEEIRNSKKFSKILELILLLGNYMNSGSKNEAAFGFEISYLTKLS 838
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    839 NTKDADNKQTLLHYLADLVEKKFpdalnfyddlshvnkasrvnmdaiqkamrqmnsavknletdLQNNKVPQCDDDKFSE 918
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    919 VMGKFAEECRQQVDVLGKMQLQMEKLYKDLSEYYAFDPSKYTMEEFFADIKTFKDAFQAAHNDNVRVREElEKKRRLQEA 998
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEE-EEERRKKLV 352
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 440214006    999 REQSAREQ-QERQQRKKAVVDMDAPQTQEGVMDSLLEALQ 1037
Cdd:smart00498  353 KETTEYEQsSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
246-446 5.45e-62

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: 209.44  E-value: 5.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   246 NGYEKVLRAITTIAATSFKaSERFRPIVDALfaSDQQDPKRDLACHSLIFINTLTNTPTDLNFRLHLRCEIMRMGLYDRL 325
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRE-RGRFQSLVGAL--DSSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   326 DEFTKIveasNNENLQQHFKIFNEIREDDFEEFVQRFDNVTFNMDDATDCFDVLKNLVTDTTSEPYFLSILQHLLYIRDD 405
Cdd:pfam06367   78 DKLREL----ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 440214006   406 FYFRPAYYQLIEECISQIVFHKGYCDPNFENR-NFNIDTSLL 446
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
59-241 5.03e-57

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: 195.23  E-value: 5.03e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006    59 IQQLSVAELDAKFLEIIEDMNIPKDKREPLLAKSKEERQKMIMWHLKGKNSLE------RSANSRFEKPIDYVEYLQNGE 132
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214006   133 HSThkvyQCVESLRVALTSNPISWIKEF-GVAGIGTIEKLLARSKNNASYE----KIEFEAIRCLKAIMNNTWGLNVVLN 207
Cdd:pfam06371   81 ISS----KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEeedlDREYEILKCLKALMNNKFGLDHVLG 156
                          170       180       190
                   ....*....|....*....|....*....|....
gi 440214006   208 pdQHSVVLLLAQSLDPRKPQTMCEALKLLASFCI 241
Cdd:pfam06371  157 --HPSSIDLLVQSLDSERLKTRKLVLELLTALCL 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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