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Conserved domains on  [gi|2048775005|ref|NP_001382058|]
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FH1/FH2 domain-containing protein 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
631-1003 3.02e-102

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 328.08  E-value: 3.02e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  631 DGPRHPTKRKTVKLFWRELKPTGSPGcsrsrfgpcpTLWASLEPVS----VDTARLEHLFESRAK----DVLPTKKAGEG 702
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG----------TVWDKLDDESfeldGDLSELEELFSAKAKtkknKKSEDKSSSKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  703 RRTMTIVLDPKRSNAINIGLTTL-PPVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIeeAQLANPDVPLGPAEN 781
Cdd:pfam02181   71 KPKEVSLLDPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  782 FLMTLASIGGLAARLQLWAFKLDYESMEREIAEPLFDLKVGMEQLVHNATFRCILATLLAVGNFLNGS----QSSGFELS 857
Cdd:pfam02181  149 FLLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGtrrgQAKGFKLS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  858 YLEKVSEVKDTVRRQSLLYHLCSLVLQTRPDSSDLYSEIPALTRCAKVDFEQLTENLGQLECRSQAAEDSLRSLAK-HEL 936
Cdd:pfam02181  229 SLLKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHP 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048775005  937 SPALRARLTHFLAQCTRRVAMLRVVHRRVCNRFHAFLLYLGytaQAAREVRIMQFCHTLREFALEYR 1003
Cdd:pfam02181  309 DDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFG---EDPKETSPEEFFKILRDFLKEFK 372
Formin_GBD_N super family cl39720
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
17-135 1.58e-54

Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD) pfam02181. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat.


The actual alignment was detected with superfamily member pfam18382:

Pssm-ID: 465735  Cd Length: 119  Bit Score: 185.25  E-value: 1.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   17 TVRVQYLEDTDPFAC-ANFPEPRRAPTCSLDGALPLSAQIPALHRLLGAPLKLEDCALQV---SPSGYYLDPELSLEEQR 92
Cdd:pfam18382    1 TCRVQYLNDTDPFACtSNFPEPTRPPTFTFNEDLPLSEQLAGVHRLLQAPHKLEDCALQVyrdGDYGNYLDLDSSLAEQR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2048775005   93 EMLEGFYEEiskgRKPTLILRTQLSVRVNAILEKLYGSSGPEL 135
Cdd:pfam18382   81 EELEGFQED----RKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
359-530 2.36e-04

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  359 PSSEEGKRSRRSLEGGGCPVRTPEPG-PTGSASPVGSASFTDSTSPTSSAfSPTGPAS-----GLHTSVNLFPTISVGPS 432
Cdd:PTZ00449   588 PKDPEEPKKPKRPRSAQRPTRPKSPKlPELLDIPKSPKRPESPKSPKRPP-PPQRPSSperpeGPKIIKSPKPPKSPKPP 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  433 VDTScersvYKARFLENV--AAAETEkqaalaqgraETLAGATVDETDESSGTRELwdsSEPASAPRPPQSPVSPIVLRT 510
Cdd:PTZ00449   667 FDPK-----FKEKFYDDYldAAAKSK----------ETKTTVVLDESFESILKETL---PETPGTPFTTPRPLPPKLPRD 728
                          170       180
                   ....*....|....*....|
gi 2048775005  511 QRSLEPEPKEPVSPRSPKTE 530
Cdd:PTZ00449   729 EEFPFEPIGDPDAEQPDDIE 748
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
631-1003 3.02e-102

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 328.08  E-value: 3.02e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  631 DGPRHPTKRKTVKLFWRELKPTGSPGcsrsrfgpcpTLWASLEPVS----VDTARLEHLFESRAK----DVLPTKKAGEG 702
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG----------TVWDKLDDESfeldGDLSELEELFSAKAKtkknKKSEDKSSSKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  703 RRTMTIVLDPKRSNAINIGLTTL-PPVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIeeAQLANPDVPLGPAEN 781
Cdd:pfam02181   71 KPKEVSLLDPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  782 FLMTLASIGGLAARLQLWAFKLDYESMEREIAEPLFDLKVGMEQLVHNATFRCILATLLAVGNFLNGS----QSSGFELS 857
Cdd:pfam02181  149 FLLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGtrrgQAKGFKLS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  858 YLEKVSEVKDTVRRQSLLYHLCSLVLQTRPDSSDLYSEIPALTRCAKVDFEQLTENLGQLECRSQAAEDSLRSLAK-HEL 936
Cdd:pfam02181  229 SLLKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHP 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048775005  937 SPALRARLTHFLAQCTRRVAMLRVVHRRVCNRFHAFLLYLGytaQAAREVRIMQFCHTLREFALEYR 1003
Cdd:pfam02181  309 DDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFG---EDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
635-1074 4.36e-87

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: 287.71  E-value: 4.36e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   635 HPTKRKTVKLFWRELKPTGSPGCsrsrfgpcptLWASLEPVS-VDTARLEHLFESRAKDVLPTKKAGEGR-------RTM 706
Cdd:smart00498    4 PKPKKKLKPLHWDKLNPSDLSGT----------VWDKIDEESeGDLDELEELFSAKEKTKSASKDVSEKKsilkkkaSQE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   707 TIVLDPKRSNAINIGLTTLP-PVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIEEAQLANPDvPLGPAENFLMT 785
Cdd:smart00498   74 FKILDPKRSQNLAILLRKLHmSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPE-ELARAEQFLLL 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   786 LASIGGLAARLQLWAFKLDYESMEREIAEPLFDLKVGMEQLVHNATFRCILATLLAVGNFLNG----SQSSGFELSYLEK 861
Cdd:smart00498  153 ISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgsrrGQAYGFKLSSLLK 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   862 VSEVKDTVRRQSLLYHLCSLVLqtrpdssdlyseipaltrcakvdfeqltenlgqlecrsqaaEDSLRSLAKHE-LSPAL 940
Cdd:smart00498  233 LSDVKSADNKTTLLHFLVKIIR-----------------------------------------KKYLGGLSDPEnLDDKF 271
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   941 RARLTHFLAQCTRRVAMLRVVHRRVCNRFHAFLLYLGYTAQaarEVRIMQFCHTLREFALEYRTCRErvlQQQQKRATYR 1020
Cdd:smart00498  272 IEVMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPK---DTSPEEFFKDFNEFLKEFSKAAE---ENIKKEEEEE 345
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2048775005  1021 ERNKTRGRMITETEKFSGVAGEVpSNLSVPVAVGsgpgrgdaDNHASMKSLLTS 1074
Cdd:smart00498  346 ERRKKLVKETTEYEQSSSRQKER-NPSMDFEVER--------DFLGVLDSLLEE 390
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
17-135 1.58e-54

Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD) pfam02181. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat.


Pssm-ID: 465735  Cd Length: 119  Bit Score: 185.25  E-value: 1.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   17 TVRVQYLEDTDPFAC-ANFPEPRRAPTCSLDGALPLSAQIPALHRLLGAPLKLEDCALQV---SPSGYYLDPELSLEEQR 92
Cdd:pfam18382    1 TCRVQYLNDTDPFACtSNFPEPTRPPTFTFNEDLPLSEQLAGVHRLLQAPHKLEDCALQVyrdGDYGNYLDLDSSLAEQR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2048775005   93 EMLEGFYEEiskgRKPTLILRTQLSVRVNAILEKLYGSSGPEL 135
Cdd:pfam18382   81 EELEGFQED----RKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
359-530 2.36e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  359 PSSEEGKRSRRSLEGGGCPVRTPEPG-PTGSASPVGSASFTDSTSPTSSAfSPTGPAS-----GLHTSVNLFPTISVGPS 432
Cdd:PTZ00449   588 PKDPEEPKKPKRPRSAQRPTRPKSPKlPELLDIPKSPKRPESPKSPKRPP-PPQRPSSperpeGPKIIKSPKPPKSPKPP 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  433 VDTScersvYKARFLENV--AAAETEkqaalaqgraETLAGATVDETDESSGTRELwdsSEPASAPRPPQSPVSPIVLRT 510
Cdd:PTZ00449   667 FDPK-----FKEKFYDDYldAAAKSK----------ETKTTVVLDESFESILKETL---PETPGTPFTTPRPLPPKLPRD 728
                          170       180
                   ....*....|....*....|
gi 2048775005  511 QRSLEPEPKEPVSPRSPKTE 530
Cdd:PTZ00449   729 EEFPFEPIGDPDAEQPDDIE 748
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
365-531 5.30e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.54  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  365 KRSRRS--LEGGGCPVRTPEPGPTGSASPvGSASFTDSTSPTSSAFSPTGPASglhtsvnlfPTISVGPSVDTS---CER 439
Cdd:pfam13254  186 RQSRASvdLGRPNSFKEVTPVGLMRSPAP-GGHSKSPSVSGISADSSPTKEEP---------SEEADTLSTDKEqspAPT 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  440 SVYKARFLENVAAAETEKQAALAQGRAETlagATVDETDESSGTRELWDSSEP-ASAPRPPQSPVSPIVLRTQRSLEPEP 518
Cdd:pfam13254  256 SASEPPPKTKELPKDSEEPAAPSKSAEAS---TEKKEPDTESSPETSSEKSAPsLLSPVSKASIDKPLSSPDRDPLSPKP 332
                          170       180
                   ....*....|....*....|....*...
gi 2048775005  519 K---------------EPVSPRSPKTEP 531
Cdd:pfam13254  333 KpqsppkdfranlrsrEVPKDKSKKDEP 360
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
631-1003 3.02e-102

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 328.08  E-value: 3.02e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  631 DGPRHPTKRKTVKLFWRELKPTGSPGcsrsrfgpcpTLWASLEPVS----VDTARLEHLFESRAK----DVLPTKKAGEG 702
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRG----------TVWDKLDDESfeldGDLSELEELFSAKAKtkknKKSEDKSSSKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  703 RRTMTIVLDPKRSNAINIGLTTL-PPVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIeeAQLANPDVPLGPAEN 781
Cdd:pfam02181   71 KPKEVSLLDPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  782 FLMTLASIGGLAARLQLWAFKLDYESMEREIAEPLFDLKVGMEQLVHNATFRCILATLLAVGNFLNGS----QSSGFELS 857
Cdd:pfam02181  149 FLLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGtrrgQAKGFKLS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  858 YLEKVSEVKDTVRRQSLLYHLCSLVLQTRPDSSDLYSEIPALTRCAKVDFEQLTENLGQLECRSQAAEDSLRSLAK-HEL 936
Cdd:pfam02181  229 SLLKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHP 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048775005  937 SPALRARLTHFLAQCTRRVAMLRVVHRRVCNRFHAFLLYLGytaQAAREVRIMQFCHTLREFALEYR 1003
Cdd:pfam02181  309 DDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFG---EDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
635-1074 4.36e-87

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: 287.71  E-value: 4.36e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   635 HPTKRKTVKLFWRELKPTGSPGCsrsrfgpcptLWASLEPVS-VDTARLEHLFESRAKDVLPTKKAGEGR-------RTM 706
Cdd:smart00498    4 PKPKKKLKPLHWDKLNPSDLSGT----------VWDKIDEESeGDLDELEELFSAKEKTKSASKDVSEKKsilkkkaSQE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   707 TIVLDPKRSNAINIGLTTLP-PVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIEEAQLANPDvPLGPAENFLMT 785
Cdd:smart00498   74 FKILDPKRSQNLAILLRKLHmSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPE-ELARAEQFLLL 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   786 LASIGGLAARLQLWAFKLDYESMEREIAEPLFDLKVGMEQLVHNATFRCILATLLAVGNFLNG----SQSSGFELSYLEK 861
Cdd:smart00498  153 ISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgsrrGQAYGFKLSSLLK 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   862 VSEVKDTVRRQSLLYHLCSLVLqtrpdssdlyseipaltrcakvdfeqltenlgqlecrsqaaEDSLRSLAKHE-LSPAL 940
Cdd:smart00498  233 LSDVKSADNKTTLLHFLVKIIR-----------------------------------------KKYLGGLSDPEnLDDKF 271
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   941 RARLTHFLAQCTRRVAMLRVVHRRVCNRFHAFLLYLGYTAQaarEVRIMQFCHTLREFALEYRTCRErvlQQQQKRATYR 1020
Cdd:smart00498  272 IEVMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPK---DTSPEEFFKDFNEFLKEFSKAAE---ENIKKEEEEE 345
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2048775005  1021 ERNKTRGRMITETEKFSGVAGEVpSNLSVPVAVGsgpgrgdaDNHASMKSLLTS 1074
Cdd:smart00498  346 ERRKKLVKETTEYEQSSSRQKER-NPSMDFEVER--------DFLGVLDSLLEE 390
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
17-135 1.58e-54

Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD) pfam02181. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat.


Pssm-ID: 465735  Cd Length: 119  Bit Score: 185.25  E-value: 1.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005   17 TVRVQYLEDTDPFAC-ANFPEPRRAPTCSLDGALPLSAQIPALHRLLGAPLKLEDCALQV---SPSGYYLDPELSLEEQR 92
Cdd:pfam18382    1 TCRVQYLNDTDPFACtSNFPEPTRPPTFTFNEDLPLSEQLAGVHRLLQAPHKLEDCALQVyrdGDYGNYLDLDSSLAEQR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2048775005   93 EMLEGFYEEiskgRKPTLILRTQLSVRVNAILEKLYGSSGPEL 135
Cdd:pfam18382   81 EELEGFQED----RKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
359-530 2.36e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  359 PSSEEGKRSRRSLEGGGCPVRTPEPG-PTGSASPVGSASFTDSTSPTSSAfSPTGPAS-----GLHTSVNLFPTISVGPS 432
Cdd:PTZ00449   588 PKDPEEPKKPKRPRSAQRPTRPKSPKlPELLDIPKSPKRPESPKSPKRPP-PPQRPSSperpeGPKIIKSPKPPKSPKPP 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  433 VDTScersvYKARFLENV--AAAETEkqaalaqgraETLAGATVDETDESSGTRELwdsSEPASAPRPPQSPVSPIVLRT 510
Cdd:PTZ00449   667 FDPK-----FKEKFYDDYldAAAKSK----------ETKTTVVLDESFESILKETL---PETPGTPFTTPRPLPPKLPRD 728
                          170       180
                   ....*....|....*....|
gi 2048775005  511 QRSLEPEPKEPVSPRSPKTE 530
Cdd:PTZ00449   729 EEFPFEPIGDPDAEQPDDIE 748
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
365-531 5.30e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.54  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  365 KRSRRS--LEGGGCPVRTPEPGPTGSASPvGSASFTDSTSPTSSAFSPTGPASglhtsvnlfPTISVGPSVDTS---CER 439
Cdd:pfam13254  186 RQSRASvdLGRPNSFKEVTPVGLMRSPAP-GGHSKSPSVSGISADSSPTKEEP---------SEEADTLSTDKEqspAPT 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048775005  440 SVYKARFLENVAAAETEKQAALAQGRAETlagATVDETDESSGTRELWDSSEP-ASAPRPPQSPVSPIVLRTQRSLEPEP 518
Cdd:pfam13254  256 SASEPPPKTKELPKDSEEPAAPSKSAEAS---TEKKEPDTESSPETSSEKSAPsLLSPVSKASIDKPLSSPDRDPLSPKP 332
                          170       180
                   ....*....|....*....|....*...
gi 2048775005  519 K---------------EPVSPRSPKTEP 531
Cdd:pfam13254  333 KpqsppkdfranlrsrEVPKDKSKKDEP 360
 
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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