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Conserved domains on  [gi|767978152|ref|XP_011533567|]
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protein diaphanous homolog 3 isoform X6 [Homo sapiens]

Protein Classification

Drf_GBD and Drf_FH3 domain-containing protein( domain architecture ID 10533866)

protein containing domains Drf_GBD, Drf_FH3, CwlO1, and FH2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
305-488 1.39e-65

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: 215.22  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  305 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 380
Cdd:pfam06367   4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  381 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 460
Cdd:pfam06367  84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                         170       180
                  ....*....|....*....|....*...
gi 767978152  461 IDECVSQIVLHRDGMDPDFTYRKRLDLD 488
Cdd:pfam06367 164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
114-297 2.17e-62

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: 206.40  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  114 PKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTG------SLKRSRQISPQEFIHELKMGS 187
Cdd:pfam06371   1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  188 ADErlvTCLESLRVSLTSNPVSWVESF-GHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSE 266
Cdd:pfam06371  81 ISS---KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGH 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767978152  267 ERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 297
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
FH2 super family cl19758
Formin Homology 2 Domain;
636-691 3.99e-07

Formin Homology 2 Domain;


The actual alignment was detected with superfamily member pfam02181:

Pssm-ID: 418645  Cd Length: 372  Bit Score: 52.66  E-value: 3.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767978152  636 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQK 691
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAK 55
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
499-552 8.88e-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: 8.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767978152 499 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 552
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
 
Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
305-488 1.39e-65

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: 215.22  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  305 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 380
Cdd:pfam06367   4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  381 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 460
Cdd:pfam06367  84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                         170       180
                  ....*....|....*....|....*...
gi 767978152  461 IDECVSQIVLHRDGMDPDFTYRKRLDLD 488
Cdd:pfam06367 164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
114-297 2.17e-62

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: 206.40  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  114 PKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTG------SLKRSRQISPQEFIHELKMGS 187
Cdd:pfam06371   1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  188 ADErlvTCLESLRVSLTSNPVSWVESF-GHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSE 266
Cdd:pfam06371  81 ISS---KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGH 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767978152  267 ERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 297
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
FH2 pfam02181
Formin Homology 2 Domain;
636-691 3.99e-07

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 52.66  E-value: 3.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767978152  636 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQK 691
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAK 55
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
637-704 6.14e-06

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: 49.27  E-value: 6.14e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767978152   637 KKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENkyeNVDLLCKLENTFCCQQKVDDISRGNTKSGE 704
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKS 64
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
499-552 8.88e-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: 8.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767978152 499 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 552
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
 
Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
305-488 1.39e-65

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: 215.22  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  305 EEVLEALTSAGEE-KKIDRFFCIVEGLRHN---SVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCI 380
Cdd:pfam06367   4 EKVLEATLNFKEVcRERGRFQSLVGALDSSendNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKLREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  381 KNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKL 460
Cdd:pfam06367  84 ENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSYWKL 163
                         170       180
                  ....*....|....*....|....*...
gi 767978152  461 IDECVSQIVLHRDGMDPDFTYRKRLDLD 488
Cdd:pfam06367 164 LEELVSQIVLHRTKPDPKFDERKNLEID 191
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
114-297 2.17e-62

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: 206.40  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  114 PKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTG------SLKRSRQISPQEFIHELKMGS 187
Cdd:pfam06371   1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTNFQKEgggsksDSESNETGSPEYYVKKLKDDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978152  188 ADErlvTCLESLRVSLTSNPVSWVESF-GHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSE 266
Cdd:pfam06371  81 ISS---KQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGH 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767978152  267 ERSLSLLAKAVDPRHPNMMTDVVKLLSAVCI 297
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
FH2 pfam02181
Formin Homology 2 Domain;
636-691 3.99e-07

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 52.66  E-value: 3.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767978152  636 PKKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENKYENVDLLCKLENTFCCQQK 691
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRG-TVWDKLDDESFELDGDLSELEELFSAKAK 55
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
637-704 6.14e-06

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: 49.27  E-value: 6.14e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767978152   637 KKEFKPEISMRRLNWLKIRPHEMTEnCFWIKVNENkyeNVDLLCKLENTFCCQQKVDDISRGNTKSGE 704
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSG-TVWDKIDEE---SEGDLDELEELFSAKEKTKSASKDVSEKKS 64
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
499-552 8.88e-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: 8.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767978152 499 QAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFG 552
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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