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Conserved domains on  [gi|767975885|ref|XP_011537272|]
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formin-like protein 3 isoform X2 [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

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
579-944 1.38e-123

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 382.00  E-value: 1.38e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   579 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 658
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   659 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 738
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   739 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 817
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   818 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 888
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767975885   889 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 944
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
300-496 3.02e-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: 192.87  E-value: 3.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   300 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQS- 377
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   378 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 454
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 767975885   455 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 496
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, ...
64-297 1.30e-18

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: 84.68  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    64 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 128
Cdd:pfam06371   20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   129 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrswsrsiedlqppsalsapft 208
Cdd:pfam06371   86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   209 nslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTK 285
Cdd:pfam06371  119 ----------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTR 176
                          250
                   ....*....|..
gi 767975885   286 ALVLELLAAVCL 297
Cdd:pfam06371  177 KLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
579-944 1.38e-123

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 382.00  E-value: 1.38e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   579 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 658
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   659 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 738
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   739 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 817
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   818 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 888
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767975885   889 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 944
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
580-1006 2.48e-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: 332.01  E-value: 2.48e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    580 KKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKileDLDLDKFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 657
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    658 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 737
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    738 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 816
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    817 TKSTDRKMTLLHFIALTVKEKYpdlanfwhelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 890
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    891 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 970
Cdd:smart00498  278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                           410       420       430
                    ....*....|....*....|....*....|....*.
gi 767975885    971 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 1006
Cdd:smart00498  357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
300-496 3.02e-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: 192.87  E-value: 3.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   300 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQS- 377
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   378 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 454
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 767975885   455 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 496
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
64-297 1.30e-18

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: 84.68  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    64 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 128
Cdd:pfam06371   20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   129 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrswsrsiedlqppsalsapft 208
Cdd:pfam06371   86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   209 nslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTK 285
Cdd:pfam06371  119 ----------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTR 176
                          250
                   ....*....|..
gi 767975885   286 ALVLELLAAVCL 297
Cdd:pfam06371  177 KLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
414-485 1.84e-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: 1.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767975885  414 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQR 485
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
579-944 1.38e-123

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 382.00  E-value: 1.38e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   579 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 658
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   659 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 738
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   739 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 817
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   818 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 888
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767975885   889 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 944
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
580-1006 2.48e-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: 332.01  E-value: 2.48e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    580 KKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKileDLDLDKFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 657
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    658 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 737
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    738 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 816
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    817 TKSTDRKMTLLHFIALTVKEKYpdlanfwhelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 890
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    891 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 970
Cdd:smart00498  278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                           410       420       430
                    ....*....|....*....|....*....|....*.
gi 767975885    971 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 1006
Cdd:smart00498  357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
300-496 3.02e-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: 192.87  E-value: 3.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   300 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQS- 377
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   378 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 454
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 767975885   455 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 496
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
64-297 1.30e-18

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: 84.68  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885    64 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 128
Cdd:pfam06371   20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   129 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrswsrsiedlqppsalsapft 208
Cdd:pfam06371   86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885   209 nslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTK 285
Cdd:pfam06371  119 ----------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTR 176
                          250
                   ....*....|..
gi 767975885   286 ALVLELLAAVCL 297
Cdd:pfam06371  177 KLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
414-485 1.84e-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: 1.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767975885  414 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQR 485
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
414-507 2.87e-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: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767975885  414 EKVEELEEHVSHLTEKLLDLENENMM----RVAELEKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQRRCHL 489
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEasfeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
                          90       100       110
                  ....*....|....*....|....*....|
gi 767975885  490 EPNVRGLES------------VDSEALARV 507
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 ...
404-465 4.50e-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: 41.31  E-value: 4.50e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767975885   404 EDAETKNVALEKVEELEEHVSHLTEkllDLENENMMRvAELEKQLLQREKELESIKETYENT 465
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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