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Conserved domains on  [gi|569001968|ref|XP_006525149|]
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disheveled-associated activator of morphogenesis 2 isoform X1 [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;
595-996 1.55e-128

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 396.26  E-value: 1.55e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   595 KKRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQVFRILDLEDFEKMFSAYqrhqacmqegpqrergnvrdggaasrp 674
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   675 lpAVEKELGSTEDIYITSRKVKELSVIDGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDI 754
Cdd:pfam02181   54 --AKTKKNKKSEDKSSSKKKPKEVSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEEL 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   755 DLLEEHKHEIERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIG 834
Cdd:pfam02181  131 KKLKEYKGDPSELGRAEQFLLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   835 NFMNKGQ-RGGAYGFRVASLNKIADTKSSiDRNISLLHYLIMILEKHFPDILNMPSELKHLSEAAKVNLAELEKEVSILR 913
Cdd:pfam02181  211 NYMNDGTrRGQAKGFKLSSLLKLSDTKST-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   914 RGLRAVEVELEYQRhQARDPNDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFL 993
Cdd:pfam02181  290 RGLKKLERELELSA-LDEHPDDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFL 368

                   ...
gi 569001968   994 QAF 996
Cdd:pfam02181  369 KEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
231-435 4.38e-63

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: 212.52  E-value: 4.38e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   231 GGHKKVLQAMLHYQAYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 310
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   311 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKHTEAYPCLLSVLHHCLQMpYKR 390
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 569001968   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 3.24e-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: 172.89  E-value: 3.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    41 PIPNPEELNVRFAELVDELDLTDKNREAVFALPPEKKWQIYCSKR----KEQEDPNKL-----ATSWPEYYIDRINAMAA 111
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   112 MQnlyetedeetdkrnQVVEDLKTALRTQPMRFVTRFIDLEGLTCLLNFLRGMDHTTCESR----IHTSLIGCIKALMNN 187
Cdd:pfam06371   82 SS--------------KQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 569001968   188 SQGRAHVLAQPEAISIIAQSLRTENSKTKVAVLEILGAVCL 228
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
595-996 1.55e-128

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 396.26  E-value: 1.55e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   595 KKRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQVFRILDLEDFEKMFSAYqrhqacmqegpqrergnvrdggaasrp 674
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   675 lpAVEKELGSTEDIYITSRKVKELSVIDGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDI 754
Cdd:pfam02181   54 --AKTKKNKKSEDKSSSKKKPKEVSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEEL 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   755 DLLEEHKHEIERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIG 834
Cdd:pfam02181  131 KKLKEYKGDPSELGRAEQFLLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   835 NFMNKGQ-RGGAYGFRVASLNKIADTKSSiDRNISLLHYLIMILEKHFPDILNMPSELKHLSEAAKVNLAELEKEVSILR 913
Cdd:pfam02181  211 NYMNDGTrRGQAKGFKLSSLLKLSDTKST-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   914 RGLRAVEVELEYQRhQARDPNDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFL 993
Cdd:pfam02181  290 RGLKKLERELELSA-LDEHPDDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFL 368

                   ...
gi 569001968   994 QAF 996
Cdd:pfam02181  369 KEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
596-1058 4.34e-73

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: 248.03  E-value: 4.34e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    596 KRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQvfrILDLEDFEKMFSAYQRHQacmqegpqrergnvrdggaasrpL 675
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTK-----------------------S 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    676 PAVEKELGSTediYITSRKVKELSVIDGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDID 755
Cdd:smart00498   55 ASKDVSEKKS---ILKKKASQEFKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELK 130
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    756 LLEEHKHE-IERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIG 834
Cdd:smart00498  131 KLREYKEEdPEELARAEQFLLLISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIG 210
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    835 NFMNKG-QRGGAYGFRVASLNKIADTKSSiDRNISLLHYLIMILEKHFpdilnmpselkhlseaakvnlaelekevsilR 913
Cdd:smart00498  211 NYMNGGsRRGQAYGFKLSSLLKLSDVKSA-DNKTTLLHFLVKIIRKKY-------------------------------L 258
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    914 RGLRAVEveleyqrhqarDPNDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFL 993
Cdd:smart00498  259 GGLSDPE-----------NLDDKFIEVMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFL 327
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569001968    994 QAFLEARQDLEAMRRRKEEDERRARMEFMLKEQrEKERWQRQRKVLAGGA-LEESGEFDDLVSALR 1058
Cdd:smart00498  328 KEFSKAAEENIKKEEEEEERRKKLVKETTEYEQ-SSSRQKERNPSMDFEVeRDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
231-435 4.38e-63

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: 212.52  E-value: 4.38e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   231 GGHKKVLQAMLHYQAYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 310
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   311 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKHTEAYPCLLSVLHHCLQMpYKR 390
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 569001968   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 3.24e-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: 172.89  E-value: 3.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    41 PIPNPEELNVRFAELVDELDLTDKNREAVFALPPEKKWQIYCSKR----KEQEDPNKL-----ATSWPEYYIDRINAMAA 111
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   112 MQnlyetedeetdkrnQVVEDLKTALRTQPMRFVTRFIDLEGLTCLLNFLRGMDHTTCESR----IHTSLIGCIKALMNN 187
Cdd:pfam06371   82 SS--------------KQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 569001968   188 SQGRAHVLAQPEAISIIAQSLRTENSKTKVAVLEILGAVCL 228
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
595-996 1.55e-128

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 396.26  E-value: 1.55e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   595 KKRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQVFRILDLEDFEKMFSAYqrhqacmqegpqrergnvrdggaasrp 674
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   675 lpAVEKELGSTEDIYITSRKVKELSVIDGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDI 754
Cdd:pfam02181   54 --AKTKKNKKSEDKSSSKKKPKEVSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEEL 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   755 DLLEEHKHEIERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIG 834
Cdd:pfam02181  131 KKLKEYKGDPSELGRAEQFLLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   835 NFMNKGQ-RGGAYGFRVASLNKIADTKSSiDRNISLLHYLIMILEKHFPDILNMPSELKHLSEAAKVNLAELEKEVSILR 913
Cdd:pfam02181  211 NYMNDGTrRGQAKGFKLSSLLKLSDTKST-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   914 RGLRAVEVELEYQRhQARDPNDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFL 993
Cdd:pfam02181  290 RGLKKLERELELSA-LDEHPDDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFL 368

                   ...
gi 569001968   994 QAF 996
Cdd:pfam02181  369 KEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
596-1058 4.34e-73

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: 248.03  E-value: 4.34e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    596 KRIPQPSHPLKSFNWVKLNEERVSGTVWNEIDDSQvfrILDLEDFEKMFSAYQRHQacmqegpqrergnvrdggaasrpL 675
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTK-----------------------S 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    676 PAVEKELGSTediYITSRKVKELSVIDGRRAQNCIILLSKLKLSNDEIRQAILRMDEqEDLAKDMLEQLLKFIPEKSDID 755
Cdd:smart00498   55 ASKDVSEKKS---ILKKKASQEFKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELK 130
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    756 LLEEHKHE-IERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELTLSQRLKQMLEVVLAIG 834
Cdd:smart00498  131 KLREYKEEdPEELARAEQFLLLISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIG 210
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    835 NFMNKG-QRGGAYGFRVASLNKIADTKSSiDRNISLLHYLIMILEKHFpdilnmpselkhlseaakvnlaelekevsilR 913
Cdd:smart00498  211 NYMNGGsRRGQAYGFKLSSLLKLSDVKSA-DNKTTLLHFLVKIIRKKY-------------------------------L 258
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    914 RGLRAVEveleyqrhqarDPNDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALTHFGEQESKMQPDEFFGIFDTFL 993
Cdd:smart00498  259 GGLSDPE-----------NLDDKFIEVMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFL 327
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569001968    994 QAFLEARQDLEAMRRRKEEDERRARMEFMLKEQrEKERWQRQRKVLAGGA-LEESGEFDDLVSALR 1058
Cdd:smart00498  328 KEFSKAAEENIKKEEEEEERRKKLVKETTEYEQ-SSSRQKERNPSMDFEVeRDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
231-435 4.38e-63

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: 212.52  E-value: 4.38e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   231 GGHKKVLQAMLHYQAYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 310
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   311 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKHTEAYPCLLSVLHHCLQMpYKR 390
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 569001968   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 3.24e-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: 172.89  E-value: 3.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968    41 PIPNPEELNVRFAELVDELDLTDKNREAVFALPPEKKWQIYCSKR----KEQEDPNKL-----ATSWPEYYIDRINAMAA 111
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKDDSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001968   112 MQnlyetedeetdkrnQVVEDLKTALRTQPMRFVTRFIDLEGLTCLLNFLRGMDHTTCESR----IHTSLIGCIKALMNN 187
Cdd:pfam06371   82 SS--------------KQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 569001968   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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