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Conserved domains on  [gi|1958786637|ref|XP_038969335|]
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inverted formin-2 isoform X6 [Rattus norvegicus]

Protein Classification

Drf_FH3 and FH2 domain-containing protein( domain architecture ID 10273080)

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
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
181-366 7.25e-42

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: 151.27  E-value: 7.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 181 EGHALTLDALDHYKMVCSQQYRFSVIMNELSD--SDNVPYVVTLLSVINALILGPEDLRTRAQLRSEFIGLQLLDILTRL 258
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSseNDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 259 RDLEDADLLIQLEAFEEAKAEDEEELQRVSD--GINMNSHQEVFTSLFHKVSCSPASAQLLSVLQGLMHLEPAARSGQLL 336
Cdd:pfam06367  81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958786637 337 WEALENLVNRAVLLAS-----DAEACTLEEVVERL 366
Cdd:pfam06367 161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
FH2 super family cl19758
Formin Homology 2 Domain;
603-759 2.33e-30

Formin Homology 2 Domain;


The actual alignment was detected with superfamily member pfam02181:

Pssm-ID: 418645  Cd Length: 372  Bit Score: 123.53  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 603 HRRVNPPTLRMKKLNWQKLpsNVARERNSMWATLSSPcTAEVEPDFSSIEQLFSfpmAKPKEPSAAP------ARKEPKE 676
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDDE-SFELDGDLSELEELFS---AKAKTKKNKKsedkssSKKKPKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 677 VTFLDSKKSLNLNIFLKQFKCSNEEVTGMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEDRAKLASADQFYILLL 756
Cdd:pfam02181  75 VSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                  ...
gi 1958786637 757 DIP 759
Cdd:pfam02181 155 KIP 157
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
24-177 2.20e-16

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: 77.74  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  24 NKMSVKEGAQR---------KW--------AALKEKLGPQDSDptEANLESAEPELCIRLLQM-PSVVNY-SGLRKRLES 84
Cdd:pfam06371  18 EEMNLPEEKRRpmlakpiekKWqlivqyksTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  85 SDGSWMVQFLEQSGLDLLLEALARLSGRGVARIADALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMV 164
Cdd:pfam06371  96 QPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKT 175
                         170
                  ....*....|...
gi 1958786637 165 KKQVFELLAALCI 177
Cdd:pfam06371 176 RKLVLELLTALCL 188
 
Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
181-366 7.25e-42

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: 151.27  E-value: 7.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 181 EGHALTLDALDHYKMVCSQQYRFSVIMNELSD--SDNVPYVVTLLSVINALILGPEDLRTRAQLRSEFIGLQLLDILTRL 258
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSseNDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 259 RDLEDADLLIQLEAFEEAKAEDEEELQRVSD--GINMNSHQEVFTSLFHKVSCSPASAQLLSVLQGLMHLEPAARSGQLL 336
Cdd:pfam06367  81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958786637 337 WEALENLVNRAVLLAS-----DAEACTLEEVVERL 366
Cdd:pfam06367 161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
FH2 pfam02181
Formin Homology 2 Domain;
603-759 2.33e-30

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 123.53  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 603 HRRVNPPTLRMKKLNWQKLpsNVARERNSMWATLSSPcTAEVEPDFSSIEQLFSfpmAKPKEPSAAP------ARKEPKE 676
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDDE-SFELDGDLSELEELFS---AKAKTKKNKKsedkssSKKKPKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 677 VTFLDSKKSLNLNIFLKQFKCSNEEVTGMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEDRAKLASADQFYILLL 756
Cdd:pfam02181  75 VSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                  ...
gi 1958786637 757 DIP 759
Cdd:pfam02181 155 KIP 157
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
606-759 1.30e-22

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: 100.89  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  606 VNPPTLRMKKLNWQKLpsNVARERNSMWATlsspCTAEVEPDFSSIEQLFSfpmAKPKEPSAAPARKEPK---------E 676
Cdd:smart00498   3 EPKPKKKLKPLHWDKL--NPSDLSGTVWDK----IDEESEGDLDELEELFS---AKEKTKSASKDVSEKKsilkkkasqE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  677 VTFLDSKKSLNLNIFLKQFKCSNEEVTGMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEDRA-KLASADQFYILL 755
Cdd:smart00498  74 FKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLI 153

                   ....
gi 1958786637  756 LDIP 759
Cdd:smart00498 154 SNIP 157
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
24-177 2.20e-16

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: 77.74  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  24 NKMSVKEGAQR---------KW--------AALKEKLGPQDSDptEANLESAEPELCIRLLQM-PSVVNY-SGLRKRLES 84
Cdd:pfam06371  18 EEMNLPEEKRRpmlakpiekKWqlivqyksTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  85 SDGSWMVQFLEQSGLDLLLEALARLSGRGVARIADALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMV 164
Cdd:pfam06371  96 QPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKT 175
                         170
                  ....*....|...
gi 1958786637 165 KKQVFELLAALCI 177
Cdd:pfam06371 176 RKLVLELLTALCL 188
 
Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
181-366 7.25e-42

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: 151.27  E-value: 7.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 181 EGHALTLDALDHYKMVCSQQYRFSVIMNELSD--SDNVPYVVTLLSVINALILGPEDLRTRAQLRSEFIGLQLLDILTRL 258
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSseNDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 259 RDLEDADLLIQLEAFEEAKAEDEEELQRVSD--GINMNSHQEVFTSLFHKVSCSPASAQLLSVLQGLMHLEPAARSGQLL 336
Cdd:pfam06367  81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958786637 337 WEALENLVNRAVLLAS-----DAEACTLEEVVERL 366
Cdd:pfam06367 161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
FH2 pfam02181
Formin Homology 2 Domain;
603-759 2.33e-30

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 123.53  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 603 HRRVNPPTLRMKKLNWQKLpsNVARERNSMWATLSSPcTAEVEPDFSSIEQLFSfpmAKPKEPSAAP------ARKEPKE 676
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDDE-SFELDGDLSELEELFS---AKAKTKKNKKsedkssSKKKPKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637 677 VTFLDSKKSLNLNIFLKQFKCSNEEVTGMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEDRAKLASADQFYILLL 756
Cdd:pfam02181  75 VSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                  ...
gi 1958786637 757 DIP 759
Cdd:pfam02181 155 KIP 157
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
606-759 1.30e-22

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: 100.89  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  606 VNPPTLRMKKLNWQKLpsNVARERNSMWATlsspCTAEVEPDFSSIEQLFSfpmAKPKEPSAAPARKEPK---------E 676
Cdd:smart00498   3 EPKPKKKLKPLHWDKL--NPSDLSGTVWDK----IDEESEGDLDELEELFS---AKEKTKSASKDVSEKKsilkkkasqE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  677 VTFLDSKKSLNLNIFLKQFKCSNEEVTGMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEDRA-KLASADQFYILL 755
Cdd:smart00498  74 FKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLI 153

                   ....
gi 1958786637  756 LDIP 759
Cdd:smart00498 154 SNIP 157
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
24-177 2.20e-16

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: 77.74  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  24 NKMSVKEGAQR---------KW--------AALKEKLGPQDSDptEANLESAEPELCIRLLQM-PSVVNY-SGLRKRLES 84
Cdd:pfam06371  18 EEMNLPEEKRRpmlakpiekKWqlivqyksTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786637  85 SDGSWMVQFLEQSGLDLLLEALARLSGRGVARIADALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMV 164
Cdd:pfam06371  96 QPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKT 175
                         170
                  ....*....|...
gi 1958786637 165 KKQVFELLAALCI 177
Cdd:pfam06371 176 RKLVLELLTALCL 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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