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Conserved domains on  [gi|386771481|ref|NP_001034035|]
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uncharacterized protein Dmel_CG33969, isoform C [Drosophila melanogaster]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 1000017)

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:  10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 180-388 5.46e-06

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 47.71  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 180 HPANEYLYCVDFVKdLYATSTDHCCRLW-----QRAQEFGMtHFDQVMhlphafrSLELSSDGQWLYGGlYTDNgrqALR 254
Cdd:cd00200   52 GPVRDVAASADGTY-LASGSSDKTIRLWdletgECVRTLTG-HTSYVS-------SVAFSPDGRILSSS-SRDK---TIK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 255 AVHVESGEEL-VFSSKTMSIYDLKL-KDDQVIFTANFDSTFRMFDRRVDRDVAIWDDpFDSSFYSLEY--DGLHAVLVGT 330
Cdd:cd00200  119 VWDVETGKCLtTLRGHTDWVNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFspDGEKLLSSSS 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771481 331 NRHARvnLYDIRMKKYVQLYfpgrtRSHNGlsPVYSLA-CDSQYMFVATDHN--MRVFDFK 388
Cdd:cd00200  198 DGTIK--LWDLSTGKCLGTL-----RGHEN--GVNSVAfSPDGYLLASGSEDgtIRVWDLR 249
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 180-388 5.46e-06

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: 47.71  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 180 HPANEYLYCVDFVKdLYATSTDHCCRLW-----QRAQEFGMtHFDQVMhlphafrSLELSSDGQWLYGGlYTDNgrqALR 254
Cdd:cd00200   52 GPVRDVAASADGTY-LASGSSDKTIRLWdletgECVRTLTG-HTSYVS-------SVAFSPDGRILSSS-SRDK---TIK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 255 AVHVESGEEL-VFSSKTMSIYDLKL-KDDQVIFTANFDSTFRMFDRRVDRDVAIWDDpFDSSFYSLEY--DGLHAVLVGT 330
Cdd:cd00200  119 VWDVETGKCLtTLRGHTDWVNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFspDGEKLLSSSS 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771481 331 NRHARvnLYDIRMKKYVQLYfpgrtRSHNGlsPVYSLA-CDSQYMFVATDHN--MRVFDFK 388
Cdd:cd00200  198 DGTIK--LWDLSTGKCLGTL-----RGHEN--GVNSVAfSPDGYLLASGSEDgtIRVWDLR 249
WD40 COG2319
WD40 repeat [General function prediction only];
195-386 3.93e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.21  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 195 LYATSTDHCCRLW-----QRAQEFGmTHFDQVmhlphafRSLELSSDGQWLYGGlytdNGRQALRAVHVESGEEL-VFSS 268
Cdd:COG2319  135 LASGSADGTVRLWdlatgKLLRTLT-GHSGAV-------TSVAFSPDGKLLASG----SDDGTVRLWDLATGKLLrTLTG 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 269 KTMSIYDLKL-KDDQVIFTANFDSTFRMFDRRVDRDVAIWDDPfDSSFYSLEY--DGLHAVLVGTNRHARvnLYDIRMKK 345
Cdd:COG2319  203 HTGAVRSVAFsPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-SGSVRSVAFspDGRLLASGSADGTVR--LWDLATGE 279

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386771481 346 YVQLYfpgrtRSHNGlsPVYSLAC--DSQYMFVAT-DHNMRVFD 386
Cdd:COG2319  280 LLRTL-----TGHSG--GVNSVAFspDGKLLASGSdDGTVRLWD 316
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 180-388 5.46e-06

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: 47.71  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 180 HPANEYLYCVDFVKdLYATSTDHCCRLW-----QRAQEFGMtHFDQVMhlphafrSLELSSDGQWLYGGlYTDNgrqALR 254
Cdd:cd00200   52 GPVRDVAASADGTY-LASGSSDKTIRLWdletgECVRTLTG-HTSYVS-------SVAFSPDGRILSSS-SRDK---TIK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 255 AVHVESGEEL-VFSSKTMSIYDLKL-KDDQVIFTANFDSTFRMFDRRVDRDVAIWDDpFDSSFYSLEY--DGLHAVLVGT 330
Cdd:cd00200  119 VWDVETGKCLtTLRGHTDWVNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFspDGEKLLSSSS 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771481 331 NRHARvnLYDIRMKKYVQLYfpgrtRSHNGlsPVYSLA-CDSQYMFVATDHN--MRVFDFK 388
Cdd:cd00200  198 DGTIK--LWDLSTGKCLGTL-----RGHEN--GVNSVAfSPDGYLLASGSEDgtIRVWDLR 249
WD40 COG2319
WD40 repeat [General function prediction only];
195-386 3.93e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.21  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 195 LYATSTDHCCRLW-----QRAQEFGmTHFDQVmhlphafRSLELSSDGQWLYGGlytdNGRQALRAVHVESGEEL-VFSS 268
Cdd:COG2319  135 LASGSADGTVRLWdlatgKLLRTLT-GHSGAV-------TSVAFSPDGKLLASG----SDDGTVRLWDLATGKLLrTLTG 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771481 269 KTMSIYDLKL-KDDQVIFTANFDSTFRMFDRRVDRDVAIWDDPfDSSFYSLEY--DGLHAVLVGTNRHARvnLYDIRMKK 345
Cdd:COG2319  203 HTGAVRSVAFsPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-SGSVRSVAFspDGRLLASGSADGTVR--LWDLATGE 279

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386771481 346 YVQLYfpgrtRSHNGlsPVYSLAC--DSQYMFVAT-DHNMRVFD 386
Cdd:COG2319  280 LLRTL-----TGHSG--GVNSVAFspDGKLLASGSdDGTVRLWD 316
 
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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