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Conserved domains on  [gi|149999378|ref|NP_001026884|]
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inverted formin-2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 super family cl19758
Formin Homology 2 Domain;
554-920 1.65e-75

Formin Homology 2 Domain;


The actual alignment was detected with superfamily member pfam02181:

Pssm-ID: 418645  Cd Length: 372  Bit Score: 254.89  E-value: 1.65e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   554 HRRVNPPTLRMKKLNWQKLpsNVAREHNSMWASLSSpDAEAVEPDFSSIERLFSFPAAKPKE-PTMVAPRARKEPKEITF 632
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDD-ESFELDGDLSELEELFSAKAKTKKNkKSEDKSSSKKKPKEVSL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   633 LDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIP 712
Cdd:pfam02181   78 LDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   713 CYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETK 792
Cdd:pfam02181  158 RLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   793 SQQNRVTLLHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEAS---SNLKKlLETERKVSASVAEVQEQYTERL 869
Cdd:pfam02181  238 STDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKqleRGLKK-LERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 149999378   870 QASISA----FRALDELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLF 920
Cdd:pfam02181  317 KEFLKSaeekLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
156-341 2.45e-38

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: 142.03  E-value: 2.45e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   156 EGHVLTLDALDHYKTVCSQQYRFSIVMNEL--SGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARL 233
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALdsSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   234 RDLEDADLLIQLEAFEEAKAEDEEELLRVSG--GVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLL 311
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 149999378   312 WEALESLVNRAVLLAS-----DAQECTLEEVVERL 341
Cdd:pfam06367  161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
966-995 9.13e-15

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


:

Pssm-ID: 409204  Cd Length: 30  Bit Score: 69.10  E-value: 9.13e-15
                          10        20        30
                  ....*....|....*....|....*....|
gi 149999378  966 KQEEVCVIDALLADIRKGFQLRKTARGRGD 995
Cdd:cd22061     1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
8-152 2.49e-14

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: 72.73  E-value: 2.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378     8 QRKWAALKEKLGPQDSDptEANLESADPELCIRLLQM-PSVVNY-SGLRKRLEGSDGGWMVQFLEQSGLDLLLEALARLS 85
Cdd:pfam06371   44 QYKSTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKIN 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149999378    86 GRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCI 152
Cdd:pfam06371  122 RKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
990-1237 7.96e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378  990 ARGRGDTDGGSKAASMDPPRATEPVAtsnPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQleeGGP 1069
Cdd:PHA03307  158 SPAAVASDAASSRQAALPLSSPEETA---RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA---ADD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378 1070 RPLERRSSWYVDASDVLTTEDPQCPQPLEG--------AWPVTLGDAQALKPLKFSSNQPPAAGSSRQDAKD-----PTS 1136
Cdd:PHA03307  232 AGASSSDSSSSESSGCGWGPENECPLPRPApitlptriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPgsgpaPSS 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378 1137 LLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKS---FSEDAVTDSSGSGTLPRARGR 1213
Cdd:PHA03307  312 PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKrprPSRAPSSPAASAGRPTRRRAR 391
                         250       260
                  ....*....|....*....|....
gi 149999378 1214 ASKGTGKRRKKRPSRsQEGLRPRP 1237
Cdd:PHA03307  392 AAVAGRARRRDATGR-FPAGRPRP 414
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
554-920 1.65e-75

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 254.89  E-value: 1.65e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   554 HRRVNPPTLRMKKLNWQKLpsNVAREHNSMWASLSSpDAEAVEPDFSSIERLFSFPAAKPKE-PTMVAPRARKEPKEITF 632
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDD-ESFELDGDLSELEELFSAKAKTKKNkKSEDKSSSKKKPKEVSL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   633 LDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIP 712
Cdd:pfam02181   78 LDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   713 CYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETK 792
Cdd:pfam02181  158 RLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   793 SQQNRVTLLHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEAS---SNLKKlLETERKVSASVAEVQEQYTERL 869
Cdd:pfam02181  238 STDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKqleRGLKK-LERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 149999378   870 QASISA----FRALDELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLF 920
Cdd:pfam02181  317 KEFLKSaeekLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
557-954 1.60e-57

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: 204.12  E-value: 1.60e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    557 VNPPTLRMKKLNWQKLPSNVAREhnSMWASLSSPDaeavEPDFSSIERLFS------FPAAKPKEPTMVAPRarKEPKEI 630
Cdd:smart00498    3 EPKPKKKLKPLHWDKLNPSDLSG--TVWDKIDEES----EGDLDELEELFSakektkSASKDVSEKKSILKK--KASQEF 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    631 TFLDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERA-KLASADHFYLLLL 709
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLIS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    710 AIPCYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLT 789
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    790 ETKSQQNRVTLLHHVLEEAEKSHpdLLQLPRDLEQPSqaaginleiirseassnlkKLLEterKVSASVAEVQEQYtERL 869
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY--LGGLSDPENLDD-------------------KFIE---VMKPFLKAAKEKY-DKL 289
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    870 QasiSAFRALDELFEaieqkqrELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQaakAERRKQQLAEEEA 949
Cdd:smart00498  290 Q---KDLSDLKTRFE-------KLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEE---EEERRKKLVKETT 356

                    ....*
gi 149999378    950 RRPRG 954
Cdd:smart00498  357 EYEQS 361
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
156-341 2.45e-38

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: 142.03  E-value: 2.45e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   156 EGHVLTLDALDHYKTVCSQQYRFSIVMNEL--SGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARL 233
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALdsSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   234 RDLEDADLLIQLEAFEEAKAEDEEELLRVSG--GVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLL 311
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 149999378   312 WEALESLVNRAVLLAS-----DAQECTLEEVVERL 341
Cdd:pfam06367  161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
966-995 9.13e-15

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


Pssm-ID: 409204  Cd Length: 30  Bit Score: 69.10  E-value: 9.13e-15
                          10        20        30
                  ....*....|....*....|....*....|
gi 149999378  966 KQEEVCVIDALLADIRKGFQLRKTARGRGD 995
Cdd:cd22061     1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
8-152 2.49e-14

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: 72.73  E-value: 2.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378     8 QRKWAALKEKLGPQDSDptEANLESADPELCIRLLQM-PSVVNY-SGLRKRLEGSDGGWMVQFLEQSGLDLLLEALARLS 85
Cdd:pfam06371   44 QYKSTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKIN 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149999378    86 GRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCI 152
Cdd:pfam06371  122 RKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
990-1237 7.96e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378  990 ARGRGDTDGGSKAASMDPPRATEPVAtsnPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQleeGGP 1069
Cdd:PHA03307  158 SPAAVASDAASSRQAALPLSSPEETA---RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA---ADD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378 1070 RPLERRSSWYVDASDVLTTEDPQCPQPLEG--------AWPVTLGDAQALKPLKFSSNQPPAAGSSRQDAKD-----PTS 1136
Cdd:PHA03307  232 AGASSSDSSSSESSGCGWGPENECPLPRPApitlptriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPgsgpaPSS 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378 1137 LLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKS---FSEDAVTDSSGSGTLPRARGR 1213
Cdd:PHA03307  312 PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKrprPSRAPSSPAASAGRPTRRRAR 391
                         250       260
                  ....*....|....*....|....
gi 149999378 1214 ASKGTGKRRKKRPSRsQEGLRPRP 1237
Cdd:PHA03307  392 AAVAGRARRRDATGR-FPAGRPRP 414
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
554-920 1.65e-75

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 254.89  E-value: 1.65e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   554 HRRVNPPTLRMKKLNWQKLpsNVAREHNSMWASLSSpDAEAVEPDFSSIERLFSFPAAKPKE-PTMVAPRARKEPKEITF 632
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDD-ESFELDGDLSELEELFSAKAKTKKNkKSEDKSSSKKKPKEVSL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   633 LDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIP 712
Cdd:pfam02181   78 LDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   713 CYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETK 792
Cdd:pfam02181  158 RLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   793 SQQNRVTLLHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEAS---SNLKKlLETERKVSASVAEVQEQYTERL 869
Cdd:pfam02181  238 STDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKqleRGLKK-LERELELSALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 149999378   870 QASISA----FRALDELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLF 920
Cdd:pfam02181  317 KEFLKSaeekLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
557-954 1.60e-57

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: 204.12  E-value: 1.60e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    557 VNPPTLRMKKLNWQKLPSNVAREhnSMWASLSSPDaeavEPDFSSIERLFS------FPAAKPKEPTMVAPRarKEPKEI 630
Cdd:smart00498    3 EPKPKKKLKPLHWDKLNPSDLSG--TVWDKIDEES----EGDLDELEELFSakektkSASKDVSEKKSILKK--KASQEF 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    631 TFLDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERA-KLASADHFYLLLL 709
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLIS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    710 AIPCYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLT 789
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    790 ETKSQQNRVTLLHHVLEEAEKSHpdLLQLPRDLEQPSqaaginleiirseassnlkKLLEterKVSASVAEVQEQYtERL 869
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY--LGGLSDPENLDD-------------------KFIE---VMKPFLKAAKEKY-DKL 289
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378    870 QasiSAFRALDELFEaieqkqrELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQaakAERRKQQLAEEEA 949
Cdd:smart00498  290 Q---KDLSDLKTRFE-------KLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEE---EEERRKKLVKETT 356

                    ....*
gi 149999378    950 RRPRG 954
Cdd:smart00498  357 EYEQS 361
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
156-341 2.45e-38

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: 142.03  E-value: 2.45e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   156 EGHVLTLDALDHYKTVCSQQYRFSIVMNEL--SGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARL 233
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALdsSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378   234 RDLEDADLLIQLEAFEEAKAEDEEELLRVSG--GVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLL 311
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 149999378   312 WEALESLVNRAVLLAS-----DAQECTLEEVVERL 341
Cdd:pfam06367  161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
966-995 9.13e-15

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


Pssm-ID: 409204  Cd Length: 30  Bit Score: 69.10  E-value: 9.13e-15
                          10        20        30
                  ....*....|....*....|....*....|
gi 149999378  966 KQEEVCVIDALLADIRKGFQLRKTARGRGD 995
Cdd:cd22061     1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
8-152 2.49e-14

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: 72.73  E-value: 2.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378     8 QRKWAALKEKLGPQDSDptEANLESADPELCIRLLQM-PSVVNY-SGLRKRLEGSDGGWMVQFLEQSGLDLLLEALARLS 85
Cdd:pfam06371   44 QYKSTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKIN 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149999378    86 GRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCI 152
Cdd:pfam06371  122 RKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
990-1237 7.96e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378  990 ARGRGDTDGGSKAASMDPPRATEPVAtsnPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQleeGGP 1069
Cdd:PHA03307  158 SPAAVASDAASSRQAALPLSSPEETA---RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA---ADD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378 1070 RPLERRSSWYVDASDVLTTEDPQCPQPLEG--------AWPVTLGDAQALKPLKFSSNQPPAAGSSRQDAKD-----PTS 1136
Cdd:PHA03307  232 AGASSSDSSSSESSGCGWGPENECPLPRPApitlptriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPgsgpaPSS 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999378 1137 LLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKS---FSEDAVTDSSGSGTLPRARGR 1213
Cdd:PHA03307  312 PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKrprPSRAPSSPAASAGRPTRRRAR 391
                         250       260
                  ....*....|....*....|....
gi 149999378 1214 ASKGTGKRRKKRPSRsQEGLRPRP 1237
Cdd:PHA03307  392 AAVAGRARRRDATGR-FPAGRPRP 414
 
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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