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Conserved domains on  [gi|148886618|sp|Q6ZPF4|]
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RecName: Full=Formin-like protein 3

Protein Classification

formin homology family protein( domain architecture ID 10273102)

formin homology family protein is a cytoskeletal remodeling protein that may be involved a diverse array of cellular functions including the regulation of actin dynamics as well as the stability and organization of microtubules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
561-926 5.87e-122

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 377.38  E-value: 5.87e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   561 IKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 640
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   641 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 720
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   721 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 799
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   800 KSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 870
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148886618   871 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 926
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
281-472 1.63e-56

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: 193.64  E-value: 1.63e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   281 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 359
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   360 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 436
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 148886618   437 LESIKETYENTSNQVHTLRRLIKEKeeaFQRRCHLE 472
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLE 189
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
27-278 5.51e-21

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: 91.61  E-value: 5.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    27 PMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflD 91
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--D 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    92 PNvtrkkfrrrvqeSTKVLRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrsw 171
Cdd:pfam06371   80 SI------------SSKQLESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   172 srsiedlqppnalsapftnslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHP 248
Cdd:pfam06371  119 ----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHP 158
                          250       260       270
                   ....*....|....*....|....*....|
gi 148886618   249 HAVNEIALSLNNKNPRTKALVLELLAAVCL 278
Cdd:pfam06371  159 SSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
561-926 5.87e-122

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 377.38  E-value: 5.87e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   561 IKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 640
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   641 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 720
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   721 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 799
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   800 KSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 870
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148886618   871 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 926
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
562-988 1.65e-102

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: 327.00  E-value: 1.65e-102
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    562 KKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKileDLDLDRFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 639
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    640 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 719
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    720 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 798
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    799 TKSTDRKMTLLHFIALTVKEKYpelanfwqelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 872
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    873 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 952
Cdd:smart00498  278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                           410       420       430
                    ....*....|....*....|....*....|....*.
gi 148886618    953 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 988
Cdd:smart00498  357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
281-472 1.63e-56

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: 193.64  E-value: 1.63e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   281 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 359
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   360 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 436
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 148886618   437 LESIKETYENTSNQVHTLRRLIKEKeeaFQRRCHLE 472
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLE 189
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
27-278 5.51e-21

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: 91.61  E-value: 5.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    27 PMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflD 91
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--D 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    92 PNvtrkkfrrrvqeSTKVLRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrsw 171
Cdd:pfam06371   80 SI------------SSKQLESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   172 srsiedlqppnalsapftnslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHP 248
Cdd:pfam06371  119 ----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHP 158
                          250       260       270
                   ....*....|....*....|....*....|
gi 148886618   249 HAVNEIALSLNNKNPRTKALVLELLAAVCL 278
Cdd:pfam06371  159 SSIDLLVQSLDSERLKTRKLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
396-463 2.90e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 2.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148886618  396 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENtsnqvhtLRRLIKEKEE 463
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIER-------LERELEEERE 486
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
561-926 5.87e-122

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 377.38  E-value: 5.87e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   561 IKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 640
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   641 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 720
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   721 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 799
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   800 KSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 870
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148886618   871 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 926
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
562-988 1.65e-102

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: 327.00  E-value: 1.65e-102
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    562 KKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKileDLDLDRFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 639
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    640 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 719
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    720 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 798
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    799 TKSTDRKMTLLHFIALTVKEKYpelanfwqelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 872
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    873 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 952
Cdd:smart00498  278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                           410       420       430
                    ....*....|....*....|....*....|....*.
gi 148886618    953 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 988
Cdd:smart00498  357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
281-472 1.63e-56

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: 193.64  E-value: 1.63e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   281 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 359
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   360 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 436
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 148886618   437 LESIKETYENTSNQVHTLRRLIKEKeeaFQRRCHLE 472
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLE 189
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
27-278 5.51e-21

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: 91.61  E-value: 5.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    27 PMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflD 91
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--D 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618    92 PNvtrkkfrrrvqeSTKVLRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrsw 171
Cdd:pfam06371   80 SI------------SSKQLESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618   172 srsiedlqppnalsapftnslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHP 248
Cdd:pfam06371  119 ----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHP 158
                          250       260       270
                   ....*....|....*....|....*....|
gi 148886618   249 HAVNEIALSLNNKNPRTKALVLELLAAVCL 278
Cdd:pfam06371  159 SSIDLLVQSLDSERLKTRKLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
396-463 2.90e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 2.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148886618  396 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENtsnqvhtLRRLIKEKEE 463
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIER-------LERELEEERE 486
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
396-499 3.09e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148886618  396 EKVEELEEHVSHLTEKLLDLENENMM----RVAELEKQLLQREKELESIKETYENTSNQVHTLRRLIKEKEEAFQRRCHL 471
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEasfeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148886618  472 EPSARGLESMGGEALARVgPTELTE-----------GIP 499
Cdd:COG0542   491 EKELAELEEELAELAPLL-REEVTEediaevvsrwtGIP 528
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
386-447 7.98e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 7.98e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148886618   386 EDAETKNVALEKVEELEEHVSHLTEkllDLENENMMRvAELEKQLLQREKELESIKETYENT 447
Cdd:pfam01576  254 EETAQKNNALKKIRELEAQISELQE---DLESERAAR-NKAEKQRRDLGEELEALKTELEDT 311
 
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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