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Conserved domains on  [gi|386770842|ref|NP_001246684|]
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formin homology 2 domain containing, isoform H [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1236-1600 9.93e-106

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 342.71  E-value: 9.93e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1236 NTIKKNKKTVKLFWKEVREDMIPQvvgkTIWDELPDA----NVDTQKLEHLFESRAKDLM----TKKQQELNKSKEIIVL 1307
Cdd:pfam02181    3 KTPKPKKKLKPLHWDKVRPSQDRG----TVWDKLDDEsfelDGDLSELEELFSAKAKTKKnkksEDKSSSKKKPKEVSLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1308 DHKRSNAINIAITKL-PPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIqeAQLSNPELPLGSAEQFLLTLASI 1386
Cdd:pfam02181   79 DPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1387 SELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNG----APVKGFQIEYLAKVPEV 1462
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgtrrGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1463 KDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAK-HDCPPPLKQKL 1541
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770842  1542 VDFLADCAERIIILQIVHRRVMNRYRKFLLWLGmpqHSVAESRPNEFCRTLSEFALEYR 1600
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFG---EDPKETSPEEFFKILRDFLKEFK 372
Formin_GBD_N super family cl39720
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
390-481 4.29e-34

Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD) pfam02181. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat.


The actual alignment was detected with superfamily member pfam18382:

Pssm-ID: 465735  Cd Length: 119  Bit Score: 127.47  E-value: 4.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   390 DVEWLDNGSNFYEPPEQRQH-------------------QPPRRIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNV 450
Cdd:pfam18382    9 DTDPFACTSNFPEPTRPPTFtfnedlplseqlagvhrllQAPHKLEDCALQVYRDGDYGNYLDLDSSLAEQREELEGFQE 88
                           90       100       110
                   ....*....|....*....|....*....|.
gi 386770842   451 SRKNSLVVRTQLNVRVQAIIEKLLSAQGSDL 481
Cdd:pfam18382   89 DRKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1236-1600 9.93e-106

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 342.71  E-value: 9.93e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1236 NTIKKNKKTVKLFWKEVREDMIPQvvgkTIWDELPDA----NVDTQKLEHLFESRAKDLM----TKKQQELNKSKEIIVL 1307
Cdd:pfam02181    3 KTPKPKKKLKPLHWDKVRPSQDRG----TVWDKLDDEsfelDGDLSELEELFSAKAKTKKnkksEDKSSSKKKPKEVSLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1308 DHKRSNAINIAITKL-PPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIqeAQLSNPELPLGSAEQFLLTLASI 1386
Cdd:pfam02181   79 DPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1387 SELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNG----APVKGFQIEYLAKVPEV 1462
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgtrrGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1463 KDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAK-HDCPPPLKQKL 1541
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770842  1542 VDFLADCAERIIILQIVHRRVMNRYRKFLLWLGmpqHSVAESRPNEFCRTLSEFALEYR 1600
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFG---EDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1236-1636 5.08e-56

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: 200.65  E-value: 5.08e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1236 NTIKKNKKTVKLFWKEVREDMIPqvvgKTIWDELPD-ANVDTQKLEHLFESRAKDLMTKKQQELNKS-------KEIIVL 1307
Cdd:smart00498    2 KEPKPKKKLKPLHWDKLNPSDLS----GTVWDKIDEeSEGDLDELEELFSAKEKTKSASKDVSEKKSilkkkasQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1308 DHKRSNAINIAITKLPPPRA-IKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPElPLGSAEQFLLTLASI 1386
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEeIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPE-ELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1387 SELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAP----VKGFQIEYLAKVPEV 1462
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSrrgqAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1463 KDTVHKHSLLHHLCHMVMEsssdtsdlySEIGpitRASKADFTDlahnlnqleaeckacwDRLKLIAKHdcppplkqklv 1542
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRK---------KYLG---GLSDPENLD----------------DKFIEVMKP----------- 277
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1543 dFLADCAERIIILQIVHRRVMNRYRKFLLWLG-MPQhsvaESRPNEFCRTLSEFALEYRTTRErvqQQLEKKANHRERNK 1621
Cdd:smart00498  278 -FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGeDPK----DTSPEEFFKDFNEFLKEFSKAAE---ENIKKEEEEEERRK 349
                           410
                    ....*....|....*
gi 386770842   1622 TRGKLIIDMAKFKTK 1636
Cdd:smart00498  350 KLVKETTEYEQSSSR 364
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
390-481 4.29e-34

Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD) pfam02181. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat.


Pssm-ID: 465735  Cd Length: 119  Bit Score: 127.47  E-value: 4.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   390 DVEWLDNGSNFYEPPEQRQH-------------------QPPRRIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNV 450
Cdd:pfam18382    9 DTDPFACTSNFPEPTRPPTFtfnedlplseqlagvhrllQAPHKLEDCALQVYRDGDYGNYLDLDSSLAEQREELEGFQE 88
                           90       100       110
                   ....*....|....*....|....*....|.
gi 386770842   451 SRKNSLVVRTQLNVRVQAIIEKLLSAQGSDL 481
Cdd:pfam18382   89 DRKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1236-1600 9.93e-106

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 342.71  E-value: 9.93e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1236 NTIKKNKKTVKLFWKEVREDMIPQvvgkTIWDELPDA----NVDTQKLEHLFESRAKDLM----TKKQQELNKSKEIIVL 1307
Cdd:pfam02181    3 KTPKPKKKLKPLHWDKVRPSQDRG----TVWDKLDDEsfelDGDLSELEELFSAKAKTKKnkksEDKSSSKKKPKEVSLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1308 DHKRSNAINIAITKL-PPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIqeAQLSNPELPLGSAEQFLLTLASI 1386
Cdd:pfam02181   79 DPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1387 SELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNG----APVKGFQIEYLAKVPEV 1462
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgtrrGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842  1463 KDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAK-HDCPPPLKQKL 1541
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770842  1542 VDFLADCAERIIILQIVHRRVMNRYRKFLLWLGmpqHSVAESRPNEFCRTLSEFALEYR 1600
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFG---EDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1236-1636 5.08e-56

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: 200.65  E-value: 5.08e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1236 NTIKKNKKTVKLFWKEVREDMIPqvvgKTIWDELPD-ANVDTQKLEHLFESRAKDLMTKKQQELNKS-------KEIIVL 1307
Cdd:smart00498    2 KEPKPKKKLKPLHWDKLNPSDLS----GTVWDKIDEeSEGDLDELEELFSAKEKTKSASKDVSEKKSilkkkasQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1308 DHKRSNAINIAITKLPPPRA-IKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPElPLGSAEQFLLTLASI 1386
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEeIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPE-ELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1387 SELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAP----VKGFQIEYLAKVPEV 1462
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSrrgqAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1463 KDTVHKHSLLHHLCHMVMEsssdtsdlySEIGpitRASKADFTDlahnlnqleaeckacwDRLKLIAKHdcppplkqklv 1542
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRK---------KYLG---GLSDPENLD----------------DKFIEVMKP----------- 277
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   1543 dFLADCAERIIILQIVHRRVMNRYRKFLLWLG-MPQhsvaESRPNEFCRTLSEFALEYRTTRErvqQQLEKKANHRERNK 1621
Cdd:smart00498  278 -FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGeDPK----DTSPEEFFKDFNEFLKEFSKAAE---ENIKKEEEEEERRK 349
                           410
                    ....*....|....*
gi 386770842   1622 TRGKLIIDMAKFKTK 1636
Cdd:smart00498  350 KLVKETTEYEQSSSR 364
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
390-481 4.29e-34

Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD) pfam02181. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat.


Pssm-ID: 465735  Cd Length: 119  Bit Score: 127.47  E-value: 4.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770842   390 DVEWLDNGSNFYEPPEQRQH-------------------QPPRRIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNV 450
Cdd:pfam18382    9 DTDPFACTSNFPEPTRPPTFtfnedlplseqlagvhrllQAPHKLEDCALQVYRDGDYGNYLDLDSSLAEQREELEGFQE 88
                           90       100       110
                   ....*....|....*....|....*....|.
gi 386770842   451 SRKNSLVVRTQLNVRVQAIIEKLLSAQGSDL 481
Cdd:pfam18382   89 DRKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
 
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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