NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217262503|ref|NP_001390829|]
View 

FH1/FH2 domain-containing protein 3 isoform 4 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1039-1410 3.10e-112

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 360.05  E-value: 3.10e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1039 GQPAFTKKKKTIRLFWNEVRPFEWpsknnrrcREFLWSKLEP----IKVDTSRLEHLFESKSKELSV---TKKTAADGKR 1111
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQD--------RGTVWDKLDDesfeLDGDLSELEELFSAKAKTKKNkksEDKSSSKKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1112 QEIIVLDSKRSNAINIGLTVL-PPPRTIKIAILNFDEYALNKEGIEKILTMIPTEEEKQKIqeAQLANPEVPLGSAEQFL 1190
Cdd:pfam02181   73 KEVSLLDPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQFL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1191 LTLSSISELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGT----NAKAFELSYL 1266
Cdd:pfam02181  151 LELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGtrrgQAKGFKLSSL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1267 EKVPEVKDTVHKQSLLHHVCTMVVENFPDSSDLYSEIGAITRSAKVDFDQLQDNLCQMERRCKASWDHLKAIAK-HEMKP 1345
Cdd:pfam02181  231 LKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHPDD 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217262503 1346 VLKQRMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPyaiREVNINKFCRIISEFALEYR 1410
Cdd:pfam02181  311 KFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDP---KETSPEEFFKILRDFLKEFK 372
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
6-123 4.42e-65

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: 216.07  E-value: 4.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503    6 CRVQFLDDTDPFNST-NFPEPSRPPLFTFREDLALGTQLAGVHRLLRAPHKLDDCTLQL---SHNGAYLDLEATLAEQRD 81
Cdd:pfam18382    2 CRVQYLNDTDPFACTsNFPEPTRPPTFTFNEDLPLSEQLAGVHRLLQAPHKLEDCALQVyrdGDYGNYLDLDSSLAEQRE 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217262503   82 ELEGFQDDtgrgKKNSIILRTQLSVRVHACIEKLYNSSGRDL 123
Cdd:pfam18382   82 ELEGFQED----RKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
327-513 4.01e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  327 GDETAEPPPSG--------------HRDRRRASMCSGGTVGEQQGLDRRRsrrhsiqniKSPLSAPTSPCSPSVPAFKPS 392
Cdd:PHA03307   179 PEETARAPSSPpaepppstppaaasPRPPRRSSPISASASSPAPAPGRSA---------ADDAGASSSDSSSSESSGCGW 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  393 QVRDLCEKDEEEEEEEEQPITEPNSEEEREDDAQCQGKDSKASSASGQSSPGKDAAPESSALHTTSSptSQGRWLSASTA 472
Cdd:PHA03307   250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS--SSSSSRESSSS 327
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217262503  473 ARSPV------LGGTSGPEASR------PAARLLPPSPGLATRPSTAPKVSPT 513
Cdd:PHA03307   328 STSSSsessrgAAVSPGPSPSRspspsrPPPPADPSSPRKRPRPSRAPSSPAA 380
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1039-1410 3.10e-112

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 360.05  E-value: 3.10e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1039 GQPAFTKKKKTIRLFWNEVRPFEWpsknnrrcREFLWSKLEP----IKVDTSRLEHLFESKSKELSV---TKKTAADGKR 1111
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQD--------RGTVWDKLDDesfeLDGDLSELEELFSAKAKTKKNkksEDKSSSKKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1112 QEIIVLDSKRSNAINIGLTVL-PPPRTIKIAILNFDEYALNKEGIEKILTMIPTEEEKQKIqeAQLANPEVPLGSAEQFL 1190
Cdd:pfam02181   73 KEVSLLDPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQFL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1191 LTLSSISELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGT----NAKAFELSYL 1266
Cdd:pfam02181  151 LELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGtrrgQAKGFKLSSL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1267 EKVPEVKDTVHKQSLLHHVCTMVVENFPDSSDLYSEIGAITRSAKVDFDQLQDNLCQMERRCKASWDHLKAIAK-HEMKP 1345
Cdd:pfam02181  231 LKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHPDD 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217262503 1346 VLKQRMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPyaiREVNINKFCRIISEFALEYR 1410
Cdd:pfam02181  311 KFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDP---KETSPEEFFKILRDFLKEFK 372
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
6-123 4.42e-65

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: 216.07  E-value: 4.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503    6 CRVQFLDDTDPFNST-NFPEPSRPPLFTFREDLALGTQLAGVHRLLRAPHKLDDCTLQL---SHNGAYLDLEATLAEQRD 81
Cdd:pfam18382    2 CRVQYLNDTDPFACTsNFPEPTRPPTFTFNEDLPLSEQLAGVHRLLQAPHKLEDCALQVyrdGDYGNYLDLDSSLAEQRE 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217262503   82 ELEGFQDDtgrgKKNSIILRTQLSVRVHACIEKLYNSSGRDL 123
Cdd:pfam18382   82 ELEGFQED----RKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1046-1463 1.60e-58

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: 207.59  E-value: 1.60e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1046 KKKTIRLFWNEVRPfewpsknnRRCREFLWSKL-EPIKVDTSRLEHLFESKSKELSVtKKTAADGK-------RQEIIVL 1117
Cdd:smart00498    7 KKKLKPLHWDKLNP--------SDLSGTVWDKIdEESEGDLDELEELFSAKEKTKSA-SKDVSEKKsilkkkaSQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1118 DSKRSNAINIGLTVLPPPRT-IKIAILNFDEYALNKEGIEKILTMIPTEEEKQKIQEAQLANPEvPLGSAEQFLLTLSSI 1196
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEeIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPE-ELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1197 SELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGT----NAKAFELSYLEKVPEV 1272
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsrrgQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1273 KDTVHKQSLLHHVCTMVVE----NFPDSSDLYSEIGAItrsakvdfdqlqdnlcqmerrckaswdhlkaiakhemkpvlk 1348
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRKkylgGLSDPENLDDKFIEV------------------------------------------ 274
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1349 qrMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPyaiREVNINKFCRIISEFALEYRTTRErvlQQKQKRANHRE 1428
Cdd:smart00498  275 --MKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDP---KDTSPEEFFKDFNEFLKEFSKAAE---ENIKKEEEEEE 346
                           410       420       430
                    ....*....|....*....|....*....|....*
gi 2217262503  1429 RNKTRGKMITDtddedeaesgKFSGSSPAAPSQPQ 1463
Cdd:smart00498  347 RRKKLVKETTE----------YEQSSSRQKERNPS 371
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
327-513 4.01e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  327 GDETAEPPPSG--------------HRDRRRASMCSGGTVGEQQGLDRRRsrrhsiqniKSPLSAPTSPCSPSVPAFKPS 392
Cdd:PHA03307   179 PEETARAPSSPpaepppstppaaasPRPPRRSSPISASASSPAPAPGRSA---------ADDAGASSSDSSSSESSGCGW 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  393 QVRDLCEKDEEEEEEEEQPITEPNSEEEREDDAQCQGKDSKASSASGQSSPGKDAAPESSALHTTSSptSQGRWLSASTA 472
Cdd:PHA03307   250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS--SSSSSRESSSS 327
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217262503  473 ARSPV------LGGTSGPEASR------PAARLLPPSPGLATRPSTAPKVSPT 513
Cdd:PHA03307   328 STSSSsessrgAAVSPGPSPSRspspsrPPPPADPSSPRKRPRPSRAPSSPAA 380
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1039-1410 3.10e-112

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 360.05  E-value: 3.10e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1039 GQPAFTKKKKTIRLFWNEVRPFEWpsknnrrcREFLWSKLEP----IKVDTSRLEHLFESKSKELSV---TKKTAADGKR 1111
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQD--------RGTVWDKLDDesfeLDGDLSELEELFSAKAKTKKNkksEDKSSSKKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1112 QEIIVLDSKRSNAINIGLTVL-PPPRTIKIAILNFDEYALNKEGIEKILTMIPTEEEKQKIqeAQLANPEVPLGSAEQFL 1190
Cdd:pfam02181   73 KEVSLLDPKRAQNIAILLRKLkLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKL--KEYKGDPSELGRAEQFL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1191 LTLSSISELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGT----NAKAFELSYL 1266
Cdd:pfam02181  151 LELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGtrrgQAKGFKLSSL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503 1267 EKVPEVKDTVHKQSLLHHVCTMVVENFPDSSDLYSEIGAITRSAKVDFDQLQDNLCQMERRCKASWDHLKAIAK-HEMKP 1345
Cdd:pfam02181  231 LKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdEHPDD 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217262503 1346 VLKQRMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPyaiREVNINKFCRIISEFALEYR 1410
Cdd:pfam02181  311 KFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDP---KETSPEEFFKILRDFLKEFK 372
Formin_GBD_N pfam18382
Formin N-terminal GTPase-binding domain; This is the N-terminal GTPase-binding domain (GBD) of ...
6-123 4.42e-65

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: 216.07  E-value: 4.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503    6 CRVQFLDDTDPFNST-NFPEPSRPPLFTFREDLALGTQLAGVHRLLRAPHKLDDCTLQL---SHNGAYLDLEATLAEQRD 81
Cdd:pfam18382    2 CRVQYLNDTDPFACTsNFPEPTRPPTFTFNEDLPLSEQLAGVHRLLQAPHKLEDCALQVyrdGDYGNYLDLDSSLAEQRE 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217262503   82 ELEGFQDDtgrgKKNSIILRTQLSVRVHACIEKLYNSSGRDL 123
Cdd:pfam18382   82 ELEGFQED----RKNSLVLRTQLSVRVHAIIEKLLNSSGREL 119
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1046-1463 1.60e-58

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: 207.59  E-value: 1.60e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1046 KKKTIRLFWNEVRPfewpsknnRRCREFLWSKL-EPIKVDTSRLEHLFESKSKELSVtKKTAADGK-------RQEIIVL 1117
Cdd:smart00498    7 KKKLKPLHWDKLNP--------SDLSGTVWDKIdEESEGDLDELEELFSAKEKTKSA-SKDVSEKKsilkkkaSQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1118 DSKRSNAINIGLTVLPPPRT-IKIAILNFDEYALNKEGIEKILTMIPTEEEKQKIQEAQLANPEvPLGSAEQFLLTLSSI 1196
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEeIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPE-ELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1197 SELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGT----NAKAFELSYLEKVPEV 1272
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsrrgQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1273 KDTVHKQSLLHHVCTMVVE----NFPDSSDLYSEIGAItrsakvdfdqlqdnlcqmerrckaswdhlkaiakhemkpvlk 1348
Cdd:smart00498  237 KSADNKTTLLHFLVKIIRKkylgGLSDPENLDDKFIEV------------------------------------------ 274
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  1349 qrMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPyaiREVNINKFCRIISEFALEYRTTRErvlQQKQKRANHRE 1428
Cdd:smart00498  275 --MKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDP---KDTSPEEFFKDFNEFLKEFSKAAE---ENIKKEEEEEE 346
                           410       420       430
                    ....*....|....*....|....*....|....*
gi 2217262503  1429 RNKTRGKMITDtddedeaesgKFSGSSPAAPSQPQ 1463
Cdd:smart00498  347 RRKKLVKETTE----------YEQSSSRQKERNPS 371
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
327-513 4.01e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  327 GDETAEPPPSG--------------HRDRRRASMCSGGTVGEQQGLDRRRsrrhsiqniKSPLSAPTSPCSPSVPAFKPS 392
Cdd:PHA03307   179 PEETARAPSSPpaepppstppaaasPRPPRRSSPISASASSPAPAPGRSA---------ADDAGASSSDSSSSESSGCGW 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262503  393 QVRDLCEKDEEEEEEEEQPITEPNSEEEREDDAQCQGKDSKASSASGQSSPGKDAAPESSALHTTSSptSQGRWLSASTA 472
Cdd:PHA03307   250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS--SSSSSRESSSS 327
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217262503  473 ARSPV------LGGTSGPEASR------PAARLLPPSPGLATRPSTAPKVSPT 513
Cdd:PHA03307   328 STSSSsessrgAAVSPGPSPSRspspsrPPPPADPSSPRKRPRPSRAPSSPAA 380
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH