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Conserved domains on  [gi|1827392984|ref|NP_001366301|]
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disheveled-associated activator of morphogenesis 2 isoform 3 [Mus musculus]

Protein Classification

formin homology family protein( domain architecture ID 10273102)

formin homology family protein is a cytoskeletal remodeling protein that may be involved a diverse array of cellular functions including the regulation of actin dynamics as well as the stability and organization of microtubules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
595-968 3.07e-132

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 405.12  E-value: 3.07e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  595 KKRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQVFRILDLEDFEKMFSAYQRHQKELGStEDIYITSRKVKELSVID 674
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  675 GRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDH 754
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  755 YQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIGNFMNKGQ-RGGAYGFRVASLNKIADTKS 833
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  834 SiDRNISLLHYLIMILEKHFPDILNMPSELKHLSEAAKVNLAELEKEVSILRRGLRAVEVELEYQRhQARDPNDKFVPVM 913
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1827392984  914 SDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFLQAF 968
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
231-435 1.55e-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: 210.98  E-value: 1.55e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  231 GGHKKVLQAMLHYQAYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 310
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  311 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKHTEAYPCLLSVLHHCLQMpYKR 390
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1827392984  391 NGGYFQQWQLLDRILQQIVLQDErgvDPDLAPLENFNVKNIVNML 435
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRT---KPDPKFDERKNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
41-228 7.55e-49

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


The actual alignment was detected with superfamily member pfam06371:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 171.73  E-value: 7.55e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   41 PIPNPEELNVRFAELVDELDLTDKNREAVFALPPEKKWQIYCSKR----KEQEDPNKL-----ATSWPEYYIDRINAMAA 111
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  112 MQnlyetedeetdkrnQVVEDLKTALRTQPMRFVTRFIDLEGLTCLLNFLRGMDHTTCESR----IHTSLIGCIKALMNN 187
Cdd:pfam06371   82 SS--------------KQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1827392984  188 SQGRAHVLAQPEAISIIAQSLRTENSKTKVAVLEILGAVCL 228
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
595-968 3.07e-132

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 405.12  E-value: 3.07e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  595 KKRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQVFRILDLEDFEKMFSAYQRHQKELGStEDIYITSRKVKELSVID 674
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  675 GRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDH 754
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  755 YQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIGNFMNKGQ-RGGAYGFRVASLNKIADTKS 833
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  834 SiDRNISLLHYLIMILEKHFPDILNMPSELKHLSEAAKVNLAELEKEVSILRRGLRAVEVELEYQRhQARDPNDKFVPVM 913
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1827392984  914 SDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFLQAF 968
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
596-1030 9.21e-76

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: 254.97  E-value: 9.21e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   596 KRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQvfrILDLEDFEKMFSAYQRHQKELGSTED--IYITSRKVKELSVI 673
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTKSASKDVSEkkSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   674 DGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHE-IERMARADRFLYEMSRI 752
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   753 DHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIGNFMNKG-QRGGAYGFRVASLNKIADT 831
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   832 KSSiDRNISLLHYLIMILEKHFpdilnmpselkhlseaakvnlaelekevsilRRGLRAVEveleyqrhqarDPNDKFVP 911
Cdd:smart00498  237 KSA-DNKTTLLHFLVKIIRKKY-------------------------------LGGLSDPE-----------NLDDKFIE 273
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   912 VMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFLQAFLEARQDLEAMRRRKEEDERRARM 991
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVK 353
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 1827392984   992 EFMLKEQrEKERWQRQRKVLAGGA-LEESGEFDDLVSALR 1030
Cdd:smart00498  354 ETTEYEQ-SSSRQKERNPSMDFEVeRDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
231-435 1.55e-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: 210.98  E-value: 1.55e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  231 GGHKKVLQAMLHYQAYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 310
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  311 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKHTEAYPCLLSVLHHCLQMpYKR 390
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1827392984  391 NGGYFQQWQLLDRILQQIVLQDErgvDPDLAPLENFNVKNIVNML 435
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRT---KPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
41-228 7.55e-49

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: 171.73  E-value: 7.55e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   41 PIPNPEELNVRFAELVDELDLTDKNREAVFALPPEKKWQIYCSKR----KEQEDPNKL-----ATSWPEYYIDRINAMAA 111
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  112 MQnlyetedeetdkrnQVVEDLKTALRTQPMRFVTRFIDLEGLTCLLNFLRGMDHTTCESR----IHTSLIGCIKALMNN 187
Cdd:pfam06371   82 SS--------------KQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1827392984  188 SQGRAHVLAQPEAISIIAQSLRTENSKTKVAVLEILGAVCL 228
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
595-968 3.07e-132

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 405.12  E-value: 3.07e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  595 KKRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQVFRILDLEDFEKMFSAYQRHQKELGStEDIYITSRKVKELSVID 674
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  675 GRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDH 754
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  755 YQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIGNFMNKGQ-RGGAYGFRVASLNKIADTKS 833
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  834 SiDRNISLLHYLIMILEKHFPDILNMPSELKHLSEAAKVNLAELEKEVSILRRGLRAVEVELEYQRhQARDPNDKFVPVM 913
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1827392984  914 SDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFLQAF 968
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
596-1030 9.21e-76

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: 254.97  E-value: 9.21e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   596 KRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQvfrILDLEDFEKMFSAYQRHQKELGSTED--IYITSRKVKELSVI 673
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTKSASKDVSEkkSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   674 DGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHE-IERMARADRFLYEMSRI 752
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   753 DHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIGNFMNKG-QRGGAYGFRVASLNKIADT 831
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   832 KSSiDRNISLLHYLIMILEKHFpdilnmpselkhlseaakvnlaelekevsilRRGLRAVEveleyqrhqarDPNDKFVP 911
Cdd:smart00498  237 KSA-DNKTTLLHFLVKIIRKKY-------------------------------LGGLSDPE-----------NLDDKFIE 273
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   912 VMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFLQAFLEARQDLEAMRRRKEEDERRARM 991
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVK 353
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 1827392984   992 EFMLKEQrEKERWQRQRKVLAGGA-LEESGEFDDLVSALR 1030
Cdd:smart00498  354 ETTEYEQ-SSSRQKERNPSMDFEVeRDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
231-435 1.55e-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: 210.98  E-value: 1.55e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  231 GGHKKVLQAMLHYQAYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 310
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  311 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKHTEAYPCLLSVLHHCLQMpYKR 390
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1827392984  391 NGGYFQQWQLLDRILQQIVLQDErgvDPDLAPLENFNVKNIVNML 435
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRT---KPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
41-228 7.55e-49

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: 171.73  E-value: 7.55e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984   41 PIPNPEELNVRFAELVDELDLTDKNREAVFALPPEKKWQIYCSKR----KEQEDPNKL-----ATSWPEYYIDRINAMAA 111
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827392984  112 MQnlyetedeetdkrnQVVEDLKTALRTQPMRFVTRFIDLEGLTCLLNFLRGMDHTTCESR----IHTSLIGCIKALMNN 187
Cdd:pfam06371   82 SS--------------KQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1827392984  188 SQGRAHVLAQPEAISIIAQSLRTENSKTKVAVLEILGAVCL 228
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 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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