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Conserved domains on  [gi|216548347|ref|NP_055784|]
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WD repeat-containing protein 47 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
607-916 1.64e-53

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 192.05  E-value: 1.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVcaypdvIDPSAHETPKQPvvrfkrnKHHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:COG2319   78 TAAVLSVAFSPDGRLLASASADGTVRL------WDLATGLLLRTL-------TGHTGAVRSVAFSPDGKTLASGSADGTV 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVlpFNAetcnATGPDL-EFSMHDGTIRDLAFmegpeSG-GAILISAGAgDCNIYTTDCQRGQGLHALSGHTGHILALyT 764
Cdd:COG2319  145 RL--WDL----ATGKLLrTLTGHSGAVTSVAF-----SPdGKLLASGSD-DGTVRLWDLATGKLLRTLTGHTGAVRSV-A 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 765 WS--GWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPH 842
Cdd:COG2319  212 FSpdGKLLASGSADGTVRLWDLATGKLLR----TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 216548347 843 SSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQ-GDLTKQLPimvvgEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:COG2319  288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLT-----GHTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 45-102 8.41e-13

C-terminal to LisH motif; Alpha-helical motif of unknown function.


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 63.74  E-value: 8.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 216548347    45 FSDDMLFLRQLILDGQWDEVLQFIQPLECMEKFDKKRFRYIILKQKFLEALCVNNAMS 102
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
LisH_TPL super family cl39307
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 13-40 2.60e-05

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


The actual alignment was detected with superfamily member pfam17814:

Pssm-ID: 375350  Cd Length: 30  Bit Score: 41.61  E-value: 2.60e-05
                          10        20
                  ....*....|....*....|....*...
gi 216548347   13 EIIKLILDFLNSKKLHISMLALEKESGV 40
Cdd:pfam17814   3 DVVRLILQFLKENGLHRTLQALQTESGV 30
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
607-916 1.64e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 192.05  E-value: 1.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVcaypdvIDPSAHETPKQPvvrfkrnKHHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:COG2319   78 TAAVLSVAFSPDGRLLASASADGTVRL------WDLATGLLLRTL-------TGHTGAVRSVAFSPDGKTLASGSADGTV 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVlpFNAetcnATGPDL-EFSMHDGTIRDLAFmegpeSG-GAILISAGAgDCNIYTTDCQRGQGLHALSGHTGHILALyT 764
Cdd:COG2319  145 RL--WDL----ATGKLLrTLTGHSGAVTSVAF-----SPdGKLLASGSD-DGTVRLWDLATGKLLRTLTGHTGAVRSV-A 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 765 WS--GWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPH 842
Cdd:COG2319  212 FSpdGKLLASGSADGTVRLWDLATGKLLR----TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 216548347 843 SSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQ-GDLTKQLPimvvgEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:COG2319  288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLT-----GHTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-916 3.60e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 181.76  E-value: 3.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVCaypDVIDPSAHETPKQpvvrfkrnkhHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVW---DLETGELLRTLKG----------HTGPVRDVAASADGTYLASGSSDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVLPFNAETCNATgpdleFSMHDGTIRDLAFMEGPEsggaiLISAGAGDCNIYTTDCQRGQGLHALSGHTGHILAL-YTW 765
Cdd:cd00200   76 RLWDLETGECVRT-----LTGHTSYVSSVAFSPDGR-----ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVaFSP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 766 SGWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSSD 845
Cdd:cd00200  146 DGTFVASSSQDGTIKLWDLRTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 216548347 846 VRSVRFSPGAHYLLTGSYDMKIKVTDLQgdltKQLPIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:cd00200  222 VNSVAFSPDGYLLASGSEDGTIRVWDLR----TGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 45-102 8.41e-13

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 63.74  E-value: 8.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 216548347    45 FSDDMLFLRQLILDGQWDEVLQFIQPLECMEKFDKKRFRYIILKQKFLEALCVNNAMS 102
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 659-688 1.76e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.08  E-value: 1.76e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 216548347   659 KHHKGSIYCVAWSPCGQLLATGSNDKYVKV 688
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 pfam00400
WD domain, G-beta repeat;
659-688 1.59e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.59e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 216548347  659 KHHKGSIYCVAWSPCGQLLATGSNDKYVKV 688
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 13-40 2.60e-05

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 41.61  E-value: 2.60e-05
                          10        20
                  ....*....|....*....|....*...
gi 216548347   13 EIIKLILDFLNSKKLHISMLALEKESGV 40
Cdd:pfam17814   3 DVVRLILQFLKENGLHRTLQALQTESGV 30
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 9-42 3.20e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.87  E-value: 3.20e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 216548347     9 VKEVEIIKLILDFLNSKKLHISMLALEKESGVIN 42
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
607-916 1.64e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 192.05  E-value: 1.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVcaypdvIDPSAHETPKQPvvrfkrnKHHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:COG2319   78 TAAVLSVAFSPDGRLLASASADGTVRL------WDLATGLLLRTL-------TGHTGAVRSVAFSPDGKTLASGSADGTV 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVlpFNAetcnATGPDL-EFSMHDGTIRDLAFmegpeSG-GAILISAGAgDCNIYTTDCQRGQGLHALSGHTGHILALyT 764
Cdd:COG2319  145 RL--WDL----ATGKLLrTLTGHSGAVTSVAF-----SPdGKLLASGSD-DGTVRLWDLATGKLLRTLTGHTGAVRSV-A 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 765 WS--GWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPH 842
Cdd:COG2319  212 FSpdGKLLASGSADGTVRLWDLATGKLLR----TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 216548347 843 SSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQ-GDLTKQLPimvvgEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:COG2319  288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLT-----GHTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 COG2319
WD40 repeat [General function prediction only];
607-916 3.73e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.20  E-value: 3.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVCaypDVIDPSAHETPKqpvvrfkrnkHHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:COG2319  120 TGAVRSVAFSPDGKTLASGSADGTVRLW---DLATGKLLRTLT----------GHSGAVTSVAFSPDGKLLASGSDDGTV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVlpFNAetcnATGPDL-EFSMHDGTIRDLAFmeGPEsgGAILISAGAgDCNIYTTDCQRGQGLHALSGHTGHILALyTW 765
Cdd:COG2319  187 RL--WDL----ATGKLLrTLTGHTGAVRSVAF--SPD--GKLLASGSA-DGTVRLWDLATGKLLRTLTGHSGSVRSV-AF 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 766 S--GWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHS 843
Cdd:COG2319  255 SpdGRLLASGSADGTVRLWDLATGELLR----TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT 330

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 216548347 844 SDVRSVRFSPGAHYLLTGSYDMKIKVTDLQGdltkQLPIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:COG2319  331 GAVRSVAFSPDGKTLASGSDDGTVRLWDLAT----GELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-916 3.60e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 181.76  E-value: 3.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVCaypDVIDPSAHETPKQpvvrfkrnkhHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVW---DLETGELLRTLKG----------HTGPVRDVAASADGTYLASGSSDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVLPFNAETCNATgpdleFSMHDGTIRDLAFMEGPEsggaiLISAGAGDCNIYTTDCQRGQGLHALSGHTGHILAL-YTW 765
Cdd:cd00200   76 RLWDLETGECVRT-----LTGHTSYVSSVAFSPDGR-----ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVaFSP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 766 SGWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSSD 845
Cdd:cd00200  146 DGTFVASSSQDGTIKLWDLRTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 216548347 846 VRSVRFSPGAHYLLTGSYDMKIKVTDLQgdltKQLPIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:cd00200  222 VNSVAFSPDGYLLASGSEDGTIRVWDLR----TGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
607-874 1.25e-46

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.40  E-value: 1.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 607 TQAVRAVAFHPAGGLYAVGSNSKTLRVCaypDVIDPsahetpkQPVVRFKrnkHHKGSIYCVAWSPCGQLLATGSNDKYV 686
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLW---DLATG-------KLLRTLT---GHTGAVRSVAFSPDGKLLASGSADGTV 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 687 KVlpFNAETCNATGPdleFSMHDGTIRDLAFMegpeSGGAILISAGAgDCNIYTTDCQRGQGLHALSGHTGHILALyTWS 766
Cdd:COG2319  229 RL--WDLATGKLLRT---LTGHSGSVRSVAFS----PDGRLLASGSA-DGTVRLWDLATGELLRTLTGHSGGVNSV-AFS 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 767 --GWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSS 844
Cdd:COG2319  298 pdGKLLASGSDDGTVRLWDLATGKLLR----TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                        250       260       270
                 ....*....|....*....|....*....|
gi 216548347 845 DVRSVRFSPGAHYLLTGSYDMKIKVTDLQG 874
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 661-916 1.14e-43

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 160.19  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 661 HKGSIYCVAWSPCGQLLATGSNDKYVKVlpFNAETCNatgPDLEFSMHDGTIRDLAFMEgpeSGGAILISAGAGDCNIYt 740
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKV--WDLETGE---LLRTLKGHTGPVRDVAASA---DGTYLASGSSDKTIRLW- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 741 tDCQRGQGLHALSGHTGHILAL-YTWSGWMIASGSQDKTVRFWDLRVPSCVrvvgTTFHGTGSAVASVAVDPSGRLLATG 819
Cdd:cd00200   79 -DLETGECVRTLTGHTSYVSSVaFSPDGRILSSSSRDKTIKVWDVETGKCL----TTLRGHTDWVNSVAFSPDGTFVASS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 820 QEDSSCMLYDIRGGRMVQSYHPHSSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQ-GDLTKQLPimvvgEHKDKVIQCRWH 898
Cdd:cd00200  154 SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLStGKCLGTLR-----GHENGVNSVAFS 228

                        250
                 ....*....|....*...
gi 216548347 899 TQDLSFLSSSADRTVTLW 916
Cdd:cd00200  229 PDGYLLASGSEDGTIRVW 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 600-829 3.54e-32

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 127.07  E-value: 3.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 600 CINILED-TQAVRAVAFHPAGGLYAVGSNSKTLRVcaypdvidpsaHETPK-QPVVRFKrnkHHKGSIYCVAWSPCGQLL 677
Cdd:cd00200   85 CVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKV-----------WDVETgKCLTTLR---GHTDWVNSVAFSPDGTFV 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 678 ATGSNDKYVKVLPFNAETCNATgpdleFSMHDGTIRDLAFMEgpeSGGAILISAGAGDCNIYttDCQRGQGLHALSGHTG 757
Cdd:cd00200  151 ASSSQDGTIKLWDLRTGKCVAT-----LTGHTGEVNSVAFSP---DGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHEN 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 216548347 758 HILAL-YTWSGWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYD 829
Cdd:cd00200  221 GVNSVaFSPDGYLLASGSEDGTIRVWDLRTGECVQ----TLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
606-832 2.01e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.00  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 606 DTQAVRAVAFHPAGGLYAVGSNSKTLRVCaypDVidpsaheTPKQPVVRFkrnKHHKGSIYCVAWSPCGQLLATGSNDKY 685
Cdd:COG2319  245 HSGSVRSVAFSPDGRLLASGSADGTVRLW---DL-------ATGELLRTL---TGHSGGVNSVAFSPDGKLLASGSDDGT 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 686 VKVlpFNAETcnatgpdlefsmhdgtirdlafmegpesggailisagagdcniyttdcqrGQGLHALSGHTGHILALyTW 765
Cdd:COG2319  312 VRL--WDLAT--------------------------------------------------GKLLRTLTGHTGAVRSV-AF 338

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 216548347 766 S--GWMIASGSQDKTVRFWDLRVPSCVRvvgtTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRG 832
Cdd:COG2319  339 SpdGKTLASGSDDGTVRLWDLATGELLR----TLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 597-783 1.85e-21

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 95.48  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 597 QFVCINILED-TQAVRAVAFHPAGGLYAVGSNSKTLRVCaypdviDPSAHETpkqpvvrFKRNKHHKGSIYCVAWSPCGQ 675
Cdd:cd00200  124 TGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDGTIKLW------DLRTGKC-------VATLTGHTGEVNSVAFSPDGE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 676 LLATGSNDKYVKVLPFNAETCNATgpdleFSMHDGTIRDLAFMEGPEsggaiLISAGAGDCNIYTTDCQRGQGLHALSGH 755
Cdd:cd00200  191 KLLSSSSDGTIKLWDLSTGKCLGT-----LRGHENGVNSVAFSPDGY-----LLASGSEDGTIRVWDLRTGECVQTLSGH 260

                        170       180       190
                 ....*....|....*....|....*....|
gi 216548347 756 TGHILALyTWS--GWMIASGSQDKTVRFWD 783
Cdd:cd00200  261 TNSVTSL-AWSpdGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 796-916 2.62e-17

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 83.54  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548347 796 TFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQgd 875
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE-- 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 216548347 876 lTKQLPIMVVGeHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:cd00200   82 -TGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVW 120
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 45-102 8.41e-13

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 63.74  E-value: 8.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 216548347    45 FSDDMLFLRQLILDGQWDEVLQFIQPLECMEKFDKKRFRYIILKQKFLEALCVNNAMS 102
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 842-920 7.00e-11

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 64.28  E-value: 7.00e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 216548347 842 HSSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQGDLtkqlPIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLWTYNG 920
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGE----LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 659-688 1.76e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.08  E-value: 1.76e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 216548347   659 KHHKGSIYCVAWSPCGQLLATGSNDKYVKV 688
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 pfam00400
WD domain, G-beta repeat;
659-688 1.59e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.59e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 216548347  659 KHHKGSIYCVAWSPCGQLLATGSNDKYVKV 688
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 833-871 2.39e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.00  E-value: 2.39e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 216548347   833 GRMVQSYHPHSSDVRSVRFSPGAHYLLTGSYDMKIKVTD 871
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
833-871 8.35e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.49  E-value: 8.35e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 216548347  833 GRMVQSYHPHSSDVRSVRFSPGAHYLLTGSYDMKIKVTD 871
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 746-783 1.47e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.68  E-value: 1.47e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 216548347   746 GQGLHALSGHTGHILALyTWS--GWMIASGSQDKTVRFWD 783
Cdd:smart00320   2 GELLKTLKGHTGPVTSV-AFSpdGKYLASGSDDGTIKLWD 40
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 13-40 2.60e-05

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 41.61  E-value: 2.60e-05
                          10        20
                  ....*....|....*....|....*...
gi 216548347   13 EIIKLILDFLNSKKLHISMLALEKESGV 40
Cdd:pfam17814   3 DVVRLILQFLKENGLHRTLQALQTESGV 30
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 791-846 7.45e-04

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 39.57  E-value: 7.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 216548347  791 RVVGTTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSSDV 846
Cdd:pfam12894  28 RVWTLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLI 83
WD40 pfam00400
WD domain, G-beta repeat;
749-783 9.07e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 9.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 216548347  749 LHALSGHTGHILAL-YTWSGWMIASGSQDKTVRFWD 783
Cdd:pfam00400   4 LKTLEGHTGSVTSLaFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 796-829 1.38e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.29  E-value: 1.38e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 216548347   796 TFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYD 829
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
795-829 1.88e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 216548347  795 TTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYD 829
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 9-42 3.20e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.87  E-value: 3.20e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 216548347     9 VKEVEIIKLILDFLNSKKLHISMLALEKESGVIN 42
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 881-916 4.24e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.75  E-value: 4.24e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 216548347   881 PIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLW 916
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
 
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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