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Conserved domains on  [gi|32425708|gb|AAH01710|]
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FMNL1 protein, partial [Homo sapiens]

Protein Classification

FH2 domain-containing protein( domain architecture ID 10490182)

FH2 domain-containing protein similar to formin homology proteins that control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarization

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1-366 4.05e-134

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 391.63  E-value: 4.05e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708     1 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSaLKSKAAQKAPSKATLIEA 80
Cdd:pfam02181   2 KKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    81 NRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREqrpMEELSEEDRFMLCFSRIP 160
Cdd:pfam02181  81 KRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKIP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708   161 RLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLEMK 239
Cdd:pfam02181 158 RLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708   240 STDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDD--------CMVLK 311
Cdd:pfam02181 238 STDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdehpddkfREVLK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32425708   312 EFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYK 366
Cdd:pfam02181 318 EFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1-366 4.05e-134

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 391.63  E-value: 4.05e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708     1 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSaLKSKAAQKAPSKATLIEA 80
Cdd:pfam02181   2 KKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    81 NRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREqrpMEELSEEDRFMLCFSRIP 160
Cdd:pfam02181  81 KRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKIP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708   161 RLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLEMK 239
Cdd:pfam02181 158 RLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708   240 STDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDD--------CMVLK 311
Cdd:pfam02181 238 STDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdehpddkfREVLK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32425708   312 EFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYK 366
Cdd:pfam02181 318 EFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1-428 2.05e-114

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: 342.02  E-value: 2.05e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708      1 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEkvlQELDMSDFEEQF--KTKSQGPSLDLSALKSKAAQKAPSKATLI 78
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEE---SEGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708     79 EANRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQrpMEELSEEDRFMLCFSR 158
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    159 IPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLE 237
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    238 MKSTDRKQTLLHYLVKVIAEKYPQltgfhsdlhfldkagsvsldsVLADVRSLqrgleltqrefvrqDD--CMVLKEFLR 315
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKYLG---------------------GLSDPENL--------------DDkfIEVMKPFLK 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    316 ANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEvEQWKKEAAAQEAGADTPGKGEPP 395
Cdd:smart00498 281 AAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEE-NIKKEEEEEERRKKLVKETTEYE 359
                          410       420       430
                   ....*....|....*....|....*....|...
gi 32425708    396 APKSPPKARRPQMDLISELKRRQQKEPLIYESD 428
Cdd:smart00498 360 QSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1-366 4.05e-134

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 391.63  E-value: 4.05e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708     1 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSaLKSKAAQKAPSKATLIEA 80
Cdd:pfam02181   2 KKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    81 NRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREqrpMEELSEEDRFMLCFSRIP 160
Cdd:pfam02181  81 KRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKIP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708   161 RLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLEMK 239
Cdd:pfam02181 158 RLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708   240 STDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDD--------CMVLK 311
Cdd:pfam02181 238 STDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdehpddkfREVLK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32425708   312 EFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYK 366
Cdd:pfam02181 318 EFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1-428 2.05e-114

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: 342.02  E-value: 2.05e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708      1 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEkvlQELDMSDFEEQF--KTKSQGPSLDLSALKSKAAQKAPSKATLI 78
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEE---SEGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708     79 EANRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQrpMEELSEEDRFMLCFSR 158
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    159 IPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLE 237
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    238 MKSTDRKQTLLHYLVKVIAEKYPQltgfhsdlhfldkagsvsldsVLADVRSLqrgleltqrefvrqDD--CMVLKEFLR 315
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKYLG---------------------GLSDPENL--------------DDkfIEVMKPFLK 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32425708    316 ANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEvEQWKKEAAAQEAGADTPGKGEPP 395
Cdd:smart00498 281 AAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEE-NIKKEEEEEERRKKLVKETTEYE 359
                          410       420       430
                   ....*....|....*....|....*....|...
gi 32425708    396 APKSPPKARRPQMDLISELKRRQQKEPLIYESD 428
Cdd:smart00498 360 QSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
 
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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