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Conserved domains on  [gi|385719171|ref|NP_001245299|]
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protein diaphanous homolog 3 isoform g [Homo sapiens]

Protein Classification

Drf_FH3 and FH2 domain-containing protein( domain architecture ID 10533854)

Drf_FH3 and FH2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
373-649 7.25e-100

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 311.13  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  373 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELkFL 452
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVS-LL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  453 DSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKR 532
Cdd:pfam02181  79 DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  533 LRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKS 612
Cdd:pfam02181 159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKS 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 385719171  613 ADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASK 649
Cdd:pfam02181 239 TDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAK 275
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
42-225 1.96e-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: 209.05  E-value: 1.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   42 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 117
Cdd:pfam06367   4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  118 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 197
Cdd:pfam06367  84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                         170       180
                  ....*....|....*....|....*...
gi 385719171  198 IDECVSQIVLHRDGMDPDFTYRKRLDLD 225
Cdd:pfam06367 164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
236-289 8.53e-04

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: 8.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 385719171 236 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 289
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
1-34 3.05e-03

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: 39.22  E-value: 3.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 385719171    1 MSEERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 34
Cdd:pfam06371 155 LGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
373-649 7.25e-100

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 311.13  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  373 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELkFL 452
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVS-LL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  453 DSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKR 532
Cdd:pfam02181  79 DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  533 LRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKS 612
Cdd:pfam02181 159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKS 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 385719171  613 ADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASK 649
Cdd:pfam02181 239 TDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAK 275
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
374-656 1.07e-85

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: 275.00  E-value: 1.07e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   374 KKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENkyeNVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELKF-- 451
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASQEFki 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   452 LDSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSE-YSNLCEPEQFVVVMSNV 530
Cdd:smart00498  77 LDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   531 KRLRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDT 610
Cdd:smart00498 157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDV 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 385719171   611 KSADQKTTLLHFLVEICEEKYpdILNFVDDLEPLDKASKGLCLFKK 656
Cdd:smart00498 237 KSADNKTTLLHFLVKIIRKKY--LGGLSDPENLDDKFIEVMKPFLK 280
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
42-225 1.96e-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: 209.05  E-value: 1.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   42 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 117
Cdd:pfam06367   4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  118 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 197
Cdd:pfam06367  84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                         170       180
                  ....*....|....*....|....*...
gi 385719171  198 IDECVSQIVLHRDGMDPDFTYRKRLDLD 225
Cdd:pfam06367 164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
236-289 8.53e-04

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: 8.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 385719171 236 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 289
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
1-34 3.05e-03

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: 39.22  E-value: 3.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 385719171    1 MSEERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 34
Cdd:pfam06371 155 LGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
373-649 7.25e-100

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 311.13  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  373 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELkFL 452
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVS-LL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  453 DSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKR 532
Cdd:pfam02181  79 DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  533 LRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKS 612
Cdd:pfam02181 159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKS 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 385719171  613 ADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASK 649
Cdd:pfam02181 239 TDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAK 275
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
374-656 1.07e-85

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: 275.00  E-value: 1.07e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   374 KKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENkyeNVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELKF-- 451
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKSILKKKASQEFki 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   452 LDSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSE-YSNLCEPEQFVVVMSNV 530
Cdd:smart00498  77 LDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   531 KRLRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDT 610
Cdd:smart00498 157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDV 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 385719171   611 KSADQKTTLLHFLVEICEEKYpdILNFVDDLEPLDKASKGLCLFKK 656
Cdd:smart00498 237 KSADNKTTLLHFLVKIIRKKY--LGGLSDPENLDDKFIEVMKPFLK 280
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
42-225 1.96e-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: 209.05  E-value: 1.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171   42 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 117
Cdd:pfam06367   4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719171  118 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 197
Cdd:pfam06367  84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                         170       180
                  ....*....|....*....|....*...
gi 385719171  198 IDECVSQIVLHRDGMDPDFTYRKRLDLD 225
Cdd:pfam06367 164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
236-289 8.53e-04

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: 8.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 385719171 236 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 289
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
1-34 3.05e-03

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: 39.22  E-value: 3.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 385719171    1 MSEERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 34
Cdd:pfam06371 155 LGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 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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