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Conserved domains on  [gi|385719163|ref|NP_001245295|]
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protein diaphanous homolog 3 isoform c [Homo sapiens]

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;
625-997 7.37e-129

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 398.95  E-value: 7.37e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   625 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELkFL 704
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVS-LL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   705 DSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKR 784
Cdd:pfam02181   79 DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   785 LRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKS 864
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   865 ADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASKVSVETLEKNLRQMGRQLQQLEKELETFPPPEDLHDKFVTKMSR 944
Cdd:pfam02181  239 TDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVLKE 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 385719163   945 FVISAKEQYETLSKLHENMEKLYQSIIGYYAIDVKKVSVEDFLTDLNNFRTTF 997
Cdd:pfam02181  319 FLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
294-477 1.41e-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: 211.36  E-value: 1.41e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   294 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 369
Cdd:pfam06367    4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   370 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 449
Cdd:pfam06367   84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                          170       180
                   ....*....|....*....|....*...
gi 385719163   450 IDECVSQIVLHRDGMDPDFTYRKRLDLD 477
Cdd:pfam06367  164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
103-286 7.81e-60

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: 203.32  E-value: 7.81e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   103 PKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTG------SLKRSRQISPQEFIHELKMGS 176
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   177 ADErlvTCLESLRVSLTSNPVSWVESF-GHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSE 255
Cdd:pfam06371   81 ISS---KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGH 157
                          170       180       190
                   ....*....|....*....|....*....|.
gi 385719163   256 ERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 286
Cdd:pfam06371  158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
488-541 1.62e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 385719163  488 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 541
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
625-997 7.37e-129

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 398.95  E-value: 7.37e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   625 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELkFL 704
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVS-LL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   705 DSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKR 784
Cdd:pfam02181   79 DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   785 LRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKS 864
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   865 ADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASKVSVETLEKNLRQMGRQLQQLEKELETFPPPEDLHDKFVTKMSR 944
Cdd:pfam02181  239 TDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVLKE 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 385719163   945 FVISAKEQYETLSKLHENMEKLYQSIIGYYAIDVKKVSVEDFLTDLNNFRTTF 997
Cdd:pfam02181  319 FLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
626-1059 7.76e-110

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: 349.34  E-value: 7.76e-110
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    626 KKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENkyeNVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELKF-- 703
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASQEFki 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    704 LDSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSE-YSNLCEPEQFVVVMSNV 782
Cdd:smart00498   77 LDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    783 KRLRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDT 862
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    863 KSADQKTTLLHFLVEICEEKYpdilnfvddlepldkaskvsvetleknlrqmgrqlqqlekeLETFPPPEDLHDKFVTKM 942
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIEVM 275
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    943 SRFVISAKEQYETLSKLHENMEKLYQSIIGYYAIDVKKVSVEDFLTDLNNFRTTFMQAIKENIKKREAEEKEKRvRIAKE 1022
Cdd:smart00498  276 KPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRK-KLVKE 354
                           410       420       430
                    ....*....|....*....|....*....|....*...
gi 385719163   1023 LAERERL-ERQQKKKRLLEMKTEGDETGVMDNLLEALQ 1059
Cdd:smart00498  355 TTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
294-477 1.41e-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: 211.36  E-value: 1.41e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   294 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 369
Cdd:pfam06367    4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   370 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 449
Cdd:pfam06367   84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                          170       180
                   ....*....|....*....|....*...
gi 385719163   450 IDECVSQIVLHRDGMDPDFTYRKRLDLD 477
Cdd:pfam06367  164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
103-286 7.81e-60

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: 203.32  E-value: 7.81e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   103 PKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTG------SLKRSRQISPQEFIHELKMGS 176
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   177 ADErlvTCLESLRVSLTSNPVSWVESF-GHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSE 255
Cdd:pfam06371   81 ISS---KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGH 157
                          170       180       190
                   ....*....|....*....|....*....|.
gi 385719163   256 ERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 286
Cdd:pfam06371  158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
488-541 1.62e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 385719163  488 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 541
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
625-997 7.37e-129

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 398.95  E-value: 7.37e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   625 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELkFL 704
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVS-LL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   705 DSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKR 784
Cdd:pfam02181   79 DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   785 LRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKS 864
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   865 ADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASKVSVETLEKNLRQMGRQLQQLEKELETFPPPEDLHDKFVTKMSR 944
Cdd:pfam02181  239 TDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFREVLKE 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 385719163   945 FVISAKEQYETLSKLHENMEKLYQSIIGYYAIDVKKVSVEDFLTDLNNFRTTF 997
Cdd:pfam02181  319 FLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
626-1059 7.76e-110

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: 349.34  E-value: 7.76e-110
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    626 KKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENkyeNVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELKF-- 703
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASQEFki 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    704 LDSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSE-YSNLCEPEQFVVVMSNV 782
Cdd:smart00498   77 LDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    783 KRLRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDT 862
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    863 KSADQKTTLLHFLVEICEEKYpdilnfvddlepldkaskvsvetleknlrqmgrqlqqlekeLETFPPPEDLHDKFVTKM 942
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIEVM 275
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163    943 SRFVISAKEQYETLSKLHENMEKLYQSIIGYYAIDVKKVSVEDFLTDLNNFRTTFMQAIKENIKKREAEEKEKRvRIAKE 1022
Cdd:smart00498  276 KPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRK-KLVKE 354
                           410       420       430
                    ....*....|....*....|....*....|....*...
gi 385719163   1023 LAERERL-ERQQKKKRLLEMKTEGDETGVMDNLLEALQ 1059
Cdd:smart00498  355 TTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
294-477 1.41e-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: 211.36  E-value: 1.41e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   294 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 369
Cdd:pfam06367    4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   370 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 449
Cdd:pfam06367   84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                          170       180
                   ....*....|....*....|....*...
gi 385719163   450 IDECVSQIVLHRDGMDPDFTYRKRLDLD 477
Cdd:pfam06367  164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
103-286 7.81e-60

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: 203.32  E-value: 7.81e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   103 PKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTG------SLKRSRQISPQEFIHELKMGS 176
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719163   177 ADErlvTCLESLRVSLTSNPVSWVESF-GHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSE 255
Cdd:pfam06371   81 ISS---KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGH 157
                          170       180       190
                   ....*....|....*....|....*....|.
gi 385719163   256 ERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 286
Cdd:pfam06371  158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
488-541 1.62e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 385719163  488 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 541
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
 
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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