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Conserved domains on  [gi|888310286|ref|NP_001297552|]
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formin-like protein 3 isoform 3 [Mus musculus]

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;
510-875 8.31e-123

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 378.54  E-value: 8.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  510 IKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 589
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  590 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 669
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  670 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 748
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  749 KSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 819
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 888310286  820 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 875
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
230-421 9.90e-57

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: 194.03  E-value: 9.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  230 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 308
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  309 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 385
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 888310286  386 LESIKETYENTSNQVHTLRRLIKEKeeaFQRRCHLE 421
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, ...
27-227 9.75e-28

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: 110.87  E-value: 9.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   27 PMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflD 91
Cdd:pfam06371   2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   92 PNvtrkkfrrrvqeSTKVLRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmystlpgrraLKNSRLVSQKD 171
Cdd:pfam06371  80 SI------------SSKQLESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS----------------KINRKKSQEEE 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 888310286  172 DV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 227
Cdd:pfam06371 130 DLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
510-875 8.31e-123

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 378.54  E-value: 8.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  510 IKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 589
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  590 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 669
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  670 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 748
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  749 KSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 819
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 888310286  820 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 875
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
511-937 3.21e-103

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: 327.77  E-value: 3.21e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   511 KKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKileDLDLDRFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 588
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   589 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 668
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   669 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 747
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   748 TKSTDRKMTLLHFIALTVKEKYpelanfwqelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 821
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   822 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 901
Cdd:smart00498 278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 888310286   902 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 937
Cdd:smart00498 357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
230-421 9.90e-57

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: 194.03  E-value: 9.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  230 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 308
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  309 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 385
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 888310286  386 LESIKETYENTSNQVHTLRRLIKEKeeaFQRRCHLE 421
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLE 189
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
27-227 9.75e-28

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: 110.87  E-value: 9.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   27 PMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflD 91
Cdd:pfam06371   2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   92 PNvtrkkfrrrvqeSTKVLRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmystlpgrraLKNSRLVSQKD 171
Cdd:pfam06371  80 SI------------SSKQLESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS----------------KINRKKSQEEE 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 888310286  172 DV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 227
Cdd:pfam06371 130 DLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
345-412 2.70e-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: 2.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 888310286 345 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENtsnqvhtLRRLIKEKEE 412
Cdd:COG2433  420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIER-------LERELEEERE 486
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
510-875 8.31e-123

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 378.54  E-value: 8.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  510 IKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 589
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  590 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 669
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  670 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 748
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  749 KSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 819
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 888310286  820 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 875
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
511-937 3.21e-103

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: 327.77  E-value: 3.21e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   511 KKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKileDLDLDRFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 588
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   589 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 668
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   669 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 747
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   748 TKSTDRKMTLLHFIALTVKEKYpelanfwqelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 821
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   822 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 901
Cdd:smart00498 278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 888310286   902 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 937
Cdd:smart00498 357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
230-421 9.90e-57

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: 194.03  E-value: 9.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  230 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 308
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286  309 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 385
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 888310286  386 LESIKETYENTSNQVHTLRRLIKEKeeaFQRRCHLE 421
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLE 189
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
27-227 9.75e-28

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: 110.87  E-value: 9.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   27 PMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflD 91
Cdd:pfam06371   2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286   92 PNvtrkkfrrrvqeSTKVLRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmystlpgrraLKNSRLVSQKD 171
Cdd:pfam06371  80 SI------------SSKQLESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS----------------KINRKKSQEEE 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 888310286  172 DV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 227
Cdd:pfam06371 130 DLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
345-412 2.70e-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: 2.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 888310286 345 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENtsnqvhtLRRLIKEKEE 412
Cdd:COG2433  420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIER-------LERELEEERE 486
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
345-448 2.98e-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: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 888310286 345 EKVEELEEHVSHLTEKLLDLENENMM----RVAELEKQLLQREKELESIKETYENTSNQVHTLRRLIKEKEEAFQRRCHL 420
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKEQDEasfeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 888310286 421 EPSARGLESMGGEALARVgPTELTE-----------GIP 448
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 ...
335-396 7.20e-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: 7.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 888310286   335 EDAETKNVALEKVEELEEHVSHLTEkllDLENENMMRvAELEKQLLQREKELESIKETYENT 396
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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