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Conserved domains on  [gi|2217291982|ref|XP_047285817|]
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formin-like protein 3 isoform X8 [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

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
517-882 6.74e-122

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 376.23  E-value: 6.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 517 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 596
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 597 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 676
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 677 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 755
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 756 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 826
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217291982 827 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 882
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
237-434 2.90e-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: 195.57  E-value: 2.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 237 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 315
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 316 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 392
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217291982 393 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 434
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, ...
1-234 3.25e-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: 83.52  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982   1 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 65
Cdd:pfam06371  20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  66 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrswsrsiedlqppsalsapft 145
Cdd:pfam06371  86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 146 nslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTK 222
Cdd:pfam06371 119 ----------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTR 176
                         250
                  ....*....|..
gi 2217291982 223 ALVLELLAAVCL 234
Cdd:pfam06371 177 KLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
517-882 6.74e-122

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 376.23  E-value: 6.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 517 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 596
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 597 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 676
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 677 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 755
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 756 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 826
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217291982 827 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 882
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
518-944 2.07e-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: 325.84  E-value: 2.07e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  518 KKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKileDLDLDKFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 595
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  596 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 675
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  676 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 754
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  755 TKSTDRKMTLLHFIALTVKEKYpdlanfwhelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 828
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  829 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 908
Cdd:smart00498 278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2217291982  909 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 944
Cdd:smart00498 357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
237-434 2.90e-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: 195.57  E-value: 2.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 237 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 315
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 316 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 392
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217291982 393 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 434
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
1-234 3.25e-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: 83.52  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982   1 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 65
Cdd:pfam06371  20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  66 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrswsrsiedlqppsalsapft 145
Cdd:pfam06371  86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 146 nslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTK 222
Cdd:pfam06371 119 ----------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTR 176
                         250
                  ....*....|..
gi 2217291982 223 ALVLELLAAVCL 234
Cdd:pfam06371 177 KLVLELLTALCL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
352-423 2.51e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217291982 352 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQR 423
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
517-882 6.74e-122

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 376.23  E-value: 6.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 517 IKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLIcSKNKTAQKAASKVTLLE 596
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 597 ANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERErqpLEELAAEDRFMLLFSKV 676
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 677 ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 755
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 756 KSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNS---------VL 826
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfreVL 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217291982 827 RNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYK 882
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
518-944 2.07e-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: 325.84  E-value: 2.07e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  518 KKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKileDLDLDKFEELF--KTKAQGPALDLICSKNKTAQKAASKVTLL 595
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  596 EANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERqpLEELAAEDRFMLLFSK 675
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  676 VERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 754
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  755 TKSTDRKMTLLHFIALTVKEKYpdlanfwhelhfvekaaavslenvlldvkelgrgmeliRRECSIHDNS------VLRN 828
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKY--------------------------------------LGGLSDPENLddkfieVMKP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  829 FLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEvMREKQLAQEAK 908
Cdd:smart00498 278 FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEE-ERRKKLVKETT 356
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2217291982  909 KLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEG 944
Cdd:smart00498 357 EYEQSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
237-434 2.90e-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: 195.57  E-value: 2.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 237 GGHEIILAAFDNFKEVCKELHRFEKLMEYFRN-EDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKS 315
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 316 RHTESEKLQVQIQAYLDNVF-DVGGLLEDAETKNVALEKVEELEEhvsHLTEKLLDLENENMMrVAELEKQLL--QREKE 392
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPHL-LSILQHLLLirDDEEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217291982 393 LESIKETYENTSHQVHTLRRLIKEKeeaFQRRCHLEPNVRGL 434
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPK---FDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
1-234 3.25e-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: 83.52  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982   1 MNLPPDKARLLRQYDNEKKWDLICDQ-------ERFQVKNP--------PHTYIQKLQSflDPSvtrkkfrrrvqeSTKV 65
Cdd:pfam06371  20 MNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD--DSI------------SSKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982  66 LRELEISLRTNHIGWVREFLndENKGLDVLVDYLSfaqcsvmfdfeglesgddgafdklrswsrsiedlqppsalsapft 145
Cdd:pfam06371  86 LESLRVALRTQPLSWVRRFI--EAQGLGALLNVLS--------------------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 146 nslarsarqsvlrystlpgrraLKNSRLVSQKDDV---HVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTK 222
Cdd:pfam06371 119 ----------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTR 176
                         250
                  ....*....|..
gi 2217291982 223 ALVLELLAAVCL 234
Cdd:pfam06371 177 KLVLELLTALCL 188
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
308-420 1.06e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 308 LEEFLQKSR--HTESEKLQVQIQAYLDNVFDVGGLLEDAETKNVAleKVEELEEHVSHLTEKLLDLENEnMMRVAELEKQ 385
Cdd:pfam07888  85 LKEELRQSRekHEELEEKYKELSASSEELSEEKDALLAQRAAHEA--RIRELEEDIKTLTQRVLERETE-LERMKERAKK 161
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217291982 386 LLQREKELESIKETYENTSHQ-VHTLRRLIKEKEEA 420
Cdd:pfam07888 162 AGAQRKEEEAERKQLQAKLQQtEEELRSLSKEFQEL 197
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
352-423 2.51e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217291982 352 EKVEELEEHVSHLTEKLLDLENENMMRVAEL------EKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQR 423
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
352-445 3.76e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291982 352 EKVEELEEHVSHLTEKLLDLENENMM----RVAELEKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQRRCHL 427
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEasfeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
                          90       100       110
                  ....*....|....*....|....*....|
gi 2217291982 428 EPNVRGLES------------VDSEALARV 445
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 ...
342-403 8.46e-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: 8.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217291982  342 EDAETKNVALEKVEELEEHVSHLTEkllDLENENMMRvAELEKQLLQREKELESIKETYENT 403
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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