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Conserved domains on  [gi|6319579|ref|NP_009661|]
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Sif2p [Saccharomyces cerevisiae S288C]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 12094100)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  21468892|18925368|10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
220-472 3.66e-36

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.89  E-value: 3.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FElkeTGGSSINAENHSGDGSLgvdvewvdddkFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSAS 378
Cdd:COG2319 242 LT---GHSGSVRSVAFSPDGRL-----------LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS 307

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  379 DDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKY 457
Cdd:COG2319 308 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKtLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTL 387

                       250
                ....*....|....*
gi 6319579  458 AVAFMDGQVNVYDLK 472
Cdd:COG2319 388 ASGSADGTVRLWDLA 402
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.89e-06

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


:

Pssm-ID: 462501  Cd Length: 25  Bit Score: 42.69  E-value: 5.89e-06
                          10        20
                  ....*....|....*....|....*
gi 6319579      7 ELNYLIWRYCQEMGHEVSALALQDE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
220-472 3.66e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.89  E-value: 3.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FElkeTGGSSINAENHSGDGSLgvdvewvdddkFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSAS 378
Cdd:COG2319 242 LT---GHSGSVRSVAFSPDGRL-----------LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS 307

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  379 DDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKY 457
Cdd:COG2319 308 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKtLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTL 387

                       250
                ....*....|....*
gi 6319579  458 AVAFMDGQVNVYDLK 472
Cdd:COG2319 388 ASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 220-516 2.13e-30

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: 120.13  E-value: 2.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FElketggssinaeNHSGDGSlgvDVEWVDDDKFVIPGPK-GAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSA 377
Cdd:cd00200  89 LT------------GHTSYVS---SVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  378 SDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGD-DKVISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQK 456
Cdd:cd00200 154 SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYL 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  457 YAVAFMDGQVNVYDLKKlNSKSRSLYGNRDGILnplpiplyaSYQSSQDNDYIFDLSWNC 516
Cdd:cd00200 234 LASGSEDGTIRVWDLRT-GECVQTLSGHTNSVT---------SLAWSPDGKRLASGSADG 283
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 349-387 4.89e-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: 43.46  E-value: 4.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 6319579     349 KTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWH 387
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.89e-06

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 42.69  E-value: 5.89e-06
                          10        20
                  ....*....|....*....|....*
gi 6319579      7 ELNYLIWRYCQEMGHEVSALALQDE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
WD40 pfam00400
WD domain, G-beta repeat;
349-386 8.51e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 8.51e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6319579    349 KTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIW 386
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
 339-440 2.58e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 43.79  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579   339 GAIFVYQITEKTPTGKLIGHHGPISVLEFNDT-NKLLLSASDDGTLRIW---HGGNG-----NSQNCFYGHSQSIVSASW 409
Cdd:PTZ00420  54 GAIRLENQMRKPPVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWeipHNDESvkeikDPQCILKGHKKKISIIDW 133

                         90       100       110
                 ....*....|....*....|....*....|...
gi 6319579   410 VGDDKVISCS--MDGSVRLWSLkQNTLLALSIV 440
Cdd:PTZ00420 134 NPMNYYIMCSsgFDSFVNIWDI-ENEKRAFQIN 165
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 3-34 6.09e-04

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: 37.41  E-value: 6.09e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 6319579       3 ITSEELNYLIWRYCQEMGHEVSALALQDETRV 34
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGL 32
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
220-472 3.66e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.89  E-value: 3.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FElkeTGGSSINAENHSGDGSLgvdvewvdddkFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSAS 378
Cdd:COG2319 242 LT---GHSGSVRSVAFSPDGRL-----------LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS 307

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  379 DDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKY 457
Cdd:COG2319 308 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKtLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTL 387

                       250
                ....*....|....*
gi 6319579  458 AVAFMDGQVNVYDLK 472
Cdd:COG2319 388 ASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
220-488 1.65e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 137.35  E-value: 1.65e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:COG2319 120 TGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FElketggssinaenhsGDGSLGVDVEWVDDDKFVI-PGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSA 377
Cdd:COG2319 200 LT---------------GHTGAVRSVAFSPDGKLLAsGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASG 264

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  378 SDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQK 456
Cdd:COG2319 265 SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKlLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKT 344

                       250       260       270
                ....*....|....*....|....*....|..
gi 6319579  457 YAVAFMDGQVNVYDLKKlNSKSRSLYGNRDGI 488
Cdd:COG2319 345 LASGSDDGTVRLWDLAT-GELLRTLTGHTGAV 375
WD40 COG2319
WD40 repeat [General function prediction only];
164-472 4.48e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 124.64  E-value: 4.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  164 TWNPLDESILAYGEKNSVARLARIVETDQEGKKYWKLTIIAELRHPFALSASSGKTTNQVTCLAWSHDGNSIVTGVENGE 243
Cdd:COG2319  22 AAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  244 LRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQHFelketggssinaenhSGDGSLGV 322
Cdd:COG2319 102 VRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL---------------TGHSGAVT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  323 DVEWVDDDKFVIPGPK-GAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWHGGNGNSQNCFYGHS 401
Cdd:COG2319 167 SVAFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319579  402 QSIVSASWVGDDKVI-SCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKYAVAFMDGQVNVYDLK 472
Cdd:COG2319 247 GSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 220-516 2.13e-30

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: 120.13  E-value: 2.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FElketggssinaeNHSGDGSlgvDVEWVDDDKFVIPGPK-GAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSA 377
Cdd:cd00200  89 LT------------GHTSYVS---SVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  378 SDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGD-DKVISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQK 456
Cdd:cd00200 154 SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYL 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  457 YAVAFMDGQVNVYDLKKlNSKSRSLYGNRDGILnplpiplyaSYQSSQDNDYIFDLSWNC 516
Cdd:cd00200 234 LASGSEDGTIRVWDLRT-GECVQTLSGHTNSVT---------SLAWSPDGKRLASGSADG 283
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 220-428 6.07e-28

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: 113.20  E-value: 6.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  220 TNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQH 298
Cdd:cd00200  93 TSYVSSVAFSPDGRILSSSSRDKTIKVWDvETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  299 FELKETGGSSINAenhSGDGSlgvdvewvdddKFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSAS 378
Cdd:cd00200 173 LTGHTGEVNSVAF---SPDGE-----------KLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGS 238

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6319579  379 DDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWS 428
Cdd:cd00200 239 EDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
198-472 9.01e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.23  E-value: 9.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  198 WKLTIIAELRHPFALSASSGKTTNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHI 276
Cdd:COG2319  14 ADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDaAAGALLATLLGHTAAVLSVAFSPDGRLL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  277 ISMDVENVTILWNVISGTVMQHFELKETGGSSINAenhSGDGSLgvdvewvdddkFVIPGPKGAIFVYQITEKTPTGKLI 356
Cdd:COG2319  94 ASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAF---SPDGKT-----------LASGSADGTVRLWDLATGKLLRTLT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  357 GHHGPISVLEFNDTNKLLLSASDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDKVI-SCSMDGSVRLWSLKQNTLL 435
Cdd:COG2319 160 GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLL 239

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6319579  436 ALSIVDGVPIFAGRISQDGQKYAVAFMDGQVNVYDLK 472
Cdd:COG2319 240 RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 253-473 2.49e-24

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: 102.80  E-value: 2.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  253 LLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQHFElketggssinaeNHSGDgslgvdVEWV----D 328
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK------------GHTGP------VRDVaasaD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  329 DDKFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWHGGNGNSQNCFYGHSQSIVSAS 408
Cdd:cd00200  63 GTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVA 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319579  409 WVGDDKVI-SCSMDGSVRLWSLKQNTLLA-LSIVDGvPIFAGRISQDGQKYAVAFMDGQVNVYDLKK 473
Cdd:cd00200 143 FSPDGTFVaSSSQDGTIKLWDLRTGKCVAtLTGHTG-EVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
WD40 COG2319
WD40 repeat [General function prediction only];
227-472 2.31e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.13  E-value: 2.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  227 AWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQHFElkeTG 305
Cdd:COG2319   1 ALSADGAALAAASADLALALLAaALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLL---GH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  306 GSSINAENHSGDGSLgvdvewvdddkFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRI 385
Cdd:COG2319  78 TAAVLSVAFSPDGRL-----------LASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579  386 WHGGNGNSQNCFYGHSQSIVSASWVGDDKVI-SCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKYAVAFMDG 464
Cdd:COG2319 147 WDLATGKLLRTLTGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADG 226


                ....*...
gi 6319579  465 QVNVYDLK 472
Cdd:COG2319 227 TVRLWDLA 234
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 349-387 4.89e-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: 43.46  E-value: 4.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 6319579     349 KTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWH 387
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.89e-06

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 42.69  E-value: 5.89e-06
                          10        20
                  ....*....|....*....|....*
gi 6319579      7 ELNYLIWRYCQEMGHEVSALALQDE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
WD40 pfam00400
WD domain, G-beta repeat;
349-386 8.51e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 8.51e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6319579    349 KTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIW 386
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 213-272 2.03e-05

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: 43.04  E-value: 2.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319579    213 SASSGKTTNQVTCLAWSHDGNSIVTGVENGELRLWN-KTGALLNVLNFHRAPIVSVKWNKD 272
Cdd:pfam12894  31 TLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDaENGKIVHHFSAGSDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 390-428 2.15e-04

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: 38.83  E-value: 2.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 6319579     390 NGNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWS 428
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKyLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 339-440 2.58e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 43.79  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319579   339 GAIFVYQITEKTPTGKLIGHHGPISVLEFNDT-NKLLLSASDDGTLRIW---HGGNG-----NSQNCFYGHSQSIVSASW 409
Cdd:PTZ00420  54 GAIRLENQMRKPPVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWeipHNDESvkeikDPQCILKGHKKKISIIDW 133

                         90       100       110
                 ....*....|....*....|....*....|...
gi 6319579   410 VGDDKVISCS--MDGSVRLWSLkQNTLLALSIV 440
Cdd:PTZ00420 134 NPMNYYIMCSsgFDSFVNIWDI-ENEKRAFQIN 165
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 3-34 6.09e-04

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: 37.41  E-value: 6.09e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 6319579       3 ITSEELNYLIWRYCQEMGHEVSALALQDETRV 34
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGL 32
WD40 pfam00400
WD domain, G-beta repeat;
391-428 7.38e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 7.38e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 6319579    391 GNSQNCFYGHSQSIVSASWVGDDK-VISCSMDGSVRLWS 428
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKlLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 220-248 1.97e-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: 36.14  E-value: 1.97e-03
                           10        20
                   ....*....|....*....|....*....
gi 6319579     220 TNQVTCLAWSHDGNSIVTGVENGELRLWN 248
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
220-248 3.36e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 3.36e-03
                          10        20
                  ....*....|....*....|....*....
gi 6319579    220 TNQVTCLAWSHDGNSIVTGVENGELRLWN 248
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 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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