NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217291980|ref|XP_047285816|]
View 

formin-like protein 3 isoform X7 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
528-893 1.21e-123

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 380.85  E-value: 1.21e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 528 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 607
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 608 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 687
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 688 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 766
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 767 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 837
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217291980 838 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 893
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
249-445 3.96e-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: 192.49  E-value: 3.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 249 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQS- 326
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 327 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 403
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217291980 404 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 445
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
64-246 3.21e-25

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: 103.94  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  64 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 128
Cdd:pfam06371  20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 129 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNY 205
Cdd:pfam06371  86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS----------------KINRKKSQEEEDLdreYEILKCLKALMNN 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217291980 206 QYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 246
Cdd:pfam06371 148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
528-893 1.21e-123

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 380.85  E-value: 1.21e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 528 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 607
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 608 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 687
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 688 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 766
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 767 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 837
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217291980 838 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 893
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
529-955 2.96e-104

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: 330.85  E-value: 2.96e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  529 KKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKileDLDLDKFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 606
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  607 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 686
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  687 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 765
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  766 TKSTDRKMTLLHFIALTVKEKYpdlanfwhelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 839
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  840 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 919
Cdd:smart00498 278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2217291980  920 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 955
Cdd:smart00498 357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
249-445 3.96e-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: 192.49  E-value: 3.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 249 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQS- 326
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 327 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 403
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217291980 404 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 445
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
64-246 3.21e-25

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: 103.94  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  64 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 128
Cdd:pfam06371  20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 129 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNY 205
Cdd:pfam06371  86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS----------------KINRKKSQEEEDLdreYEILKCLKALMNN 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217291980 206 QYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 246
Cdd:pfam06371 148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
363-434 1.79e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217291980 363 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQR 434
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
528-893 1.21e-123

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 380.85  E-value: 1.21e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 528 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 607
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 608 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 687
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 688 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 766
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 767 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 837
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217291980 838 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 893
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
529-955 2.96e-104

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: 330.85  E-value: 2.96e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  529 KKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKileDLDLDKFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 606
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  607 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 686
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  687 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 765
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  766 TKSTDRKMTLLHFIALTVKEKYpdlanfwhelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 839
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  840 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 919
Cdd:smart00498 278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2217291980  920 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 955
Cdd:smart00498 357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
249-445 3.96e-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: 192.49  E-value: 3.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 249 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQS- 326
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 327 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 403
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217291980 404 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 445
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
64-246 3.21e-25

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: 103.94  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980  64 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 128
Cdd:pfam06371  20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 129 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNY 205
Cdd:pfam06371  86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS----------------KINRKKSQEEEDLdreYEILKCLKALMNN 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217291980 206 QYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 246
Cdd:pfam06371 148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
363-434 1.79e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217291980 363 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQR 434
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
363-456 2.73e-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: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291980 363 EKVEELEEHVSHLTEKLLDLENENMM----RVAELEKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQRRCHL 438
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEasfeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
                          90       100       110
                  ....*....|....*....|....*....|
gi 2217291980 439 EPNVRGLES------------VDSEALARV 456
Cdd:COG0542   491 EKELAELEEelaelapllreeVTEEDIAEV 520
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
353-414 4.74e-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: 40.93  E-value: 4.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217291980  353 EDAETKNVALEKVEELEEHVSHLTEkllDLENENMMRvAELEKQLLQREKELESIKETYENT 414
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH