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Conserved domains on  [gi|568984332|ref|XP_006517647|]
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WD repeat-containing protein 41 isoform X2 [Mus musculus]

Protein Classification

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

WD40 repeat domain-containing protein 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

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 ...
 87-304 3.57e-10

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: 60.04  E-value: 3.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  87 EVKRLLDHQDNILSLANINDTGF-VTGSHVGELLIWDaldWTVQACERTFWSPTAQLdaqqeiklfqkqNDISinhFTCD 165
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLlATGSGDGTIKVWD---LETGELLRTLKGHTGPV------------RDVA---ASAD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 166 EENIFAA-VGRGLYVYNLQLKRVIACQkTAHDSNILHIDKLPNRQLI-SCSEDGAVRMWEVREKQQLAAEPVPTGFFNMW 243
Cdd:cd00200   63 GTYLASGsSDKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDGRILsSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568984332 244 GFGRVNKQasqpvkkqeenVTTCS------------LELIGDLIGHSSSVEMFLYFED-HGLVTCSADHLIILW 304
Cdd:cd00200  142 AFSPDGTF-----------VASSSqdgtiklwdlrtGKCVATLTGHTGEVNSVAFSPDgEKLLSSSSDGTIKLW 204
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 87-304 3.57e-10

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: 60.04  E-value: 3.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  87 EVKRLLDHQDNILSLANINDTGF-VTGSHVGELLIWDaldWTVQACERTFWSPTAQLdaqqeiklfqkqNDISinhFTCD 165
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLlATGSGDGTIKVWD---LETGELLRTLKGHTGPV------------RDVA---ASAD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 166 EENIFAA-VGRGLYVYNLQLKRVIACQkTAHDSNILHIDKLPNRQLI-SCSEDGAVRMWEVREKQQLAAEPVPTGFFNMW 243
Cdd:cd00200   63 GTYLASGsSDKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDGRILsSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568984332 244 GFGRVNKQasqpvkkqeenVTTCS------------LELIGDLIGHSSSVEMFLYFED-HGLVTCSADHLIILW 304
Cdd:cd00200  142 AFSPDGTF-----------VASSSqdgtiklwdlrtGKCVATLTGHTGEVNSVAFSPDgEKLLSSSSDGTIKLW 204
WD40 COG2319
WD40 repeat [General function prediction only];
15-238 1.44e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.36  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  15 LQRLDIWLSGGSDLGVWNRKLDLLCKTSHLSDTGISALVEIPGNCVAAAVGRELIIfRLvtpteelpeWDI---IEVKRL 91
Cdd:COG2319   47 DGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTV-RL---------WDLatgLLLRTL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  92 LDHQDNILSLAnINDTG--FVTGSHVGELLIWDALDWTvqaCERTF-----------WSPTAQL----DAQQEIKLFQKQ 154
Cdd:COG2319  117 TGHTGAVRSVA-FSPDGktLASGSADGTVRLWDLATGK---LLRTLtghsgavtsvaFSPDGKLlasgSDDGTVRLWDLA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 155 NDISINHFTCDEENIFAAV-------------GRGLYVYNLQLKRVIAcQKTAHDSNILHIDKLPN-RQLISCSEDGAVR 220
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAfspdgkllasgsaDGTVRLWDLATGKLLR-TLTGHSGSVRSVAFSPDgRLLASGSADGTVR 271

                        250
                 ....*....|....*...
gi 568984332 221 MWEVREKQQLAAEPVPTG 238
Cdd:COG2319  272 LWDLATGELLRTLTGHSG 289
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 87-304 3.57e-10

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: 60.04  E-value: 3.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  87 EVKRLLDHQDNILSLANINDTGF-VTGSHVGELLIWDaldWTVQACERTFWSPTAQLdaqqeiklfqkqNDISinhFTCD 165
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLlATGSGDGTIKVWD---LETGELLRTLKGHTGPV------------RDVA---ASAD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 166 EENIFAA-VGRGLYVYNLQLKRVIACQkTAHDSNILHIDKLPNRQLI-SCSEDGAVRMWEVREKQQLAAEPVPTGFFNMW 243
Cdd:cd00200   63 GTYLASGsSDKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDGRILsSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568984332 244 GFGRVNKQasqpvkkqeenVTTCS------------LELIGDLIGHSSSVEMFLYFED-HGLVTCSADHLIILW 304
Cdd:cd00200  142 AFSPDGTF-----------VASSSqdgtiklwdlrtGKCVATLTGHTGEVNSVAFSPDgEKLLSSSSDGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 83-305 2.35e-08

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: 54.26  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  83 WDII---EVKRLLDHQDNILSLANINDTGFVTGSHV-GELLIWDaldwtvqacertfwsptaqLDAQQEIKLFQKQNDiS 158
Cdd:cd00200   78 WDLEtgeCVRTLTGHTSYVSSVAFSPDGRILSSSSRdKTIKVWD-------------------VETGKCLTTLRGHTD-W 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 159 INHFTCDEENIFAAVGRG---LYVYNLQLKRVIAcQKTAHDSNILHIDKLPN-RQLISCSEDGAVRMWEVREKQQLAAEP 234
Cdd:cd00200  138 VNSVAFSPDGTFVASSSQdgtIKLWDLRTGKCVA-TLTGHTGEVNSVAFSPDgEKLLSSSSDGTIKLWDLSTGKCLGTLR 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 235 VPTGFFN--MWGFGRvnkqasqpvkkqeENVTTCSL------------ELIGDLIGHSSSVEMFLYFED-HGLVTCSADH 299
Cdd:cd00200  217 GHENGVNsvAFSPDG-------------YLLASGSEdgtirvwdlrtgECVQTLSGHTNSVTSLAWSPDgKRLASGSADG 283


                 ....*.
gi 568984332 300 LIILWK 305
Cdd:cd00200  284 TIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
15-238 1.44e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.36  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  15 LQRLDIWLSGGSDLGVWNRKLDLLCKTSHLSDTGISALVEIPGNCVAAAVGRELIIfRLvtpteelpeWDI---IEVKRL 91
Cdd:COG2319   47 DGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTV-RL---------WDLatgLLLRTL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  92 LDHQDNILSLAnINDTG--FVTGSHVGELLIWDALDWTvqaCERTF-----------WSPTAQL----DAQQEIKLFQKQ 154
Cdd:COG2319  117 TGHTGAVRSVA-FSPDGktLASGSADGTVRLWDLATGK---LLRTLtghsgavtsvaFSPDGKLlasgSDDGTVRLWDLA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332 155 NDISINHFTCDEENIFAAV-------------GRGLYVYNLQLKRVIAcQKTAHDSNILHIDKLPN-RQLISCSEDGAVR 220
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAfspdgkllasgsaDGTVRLWDLATGKLLR-TLTGHSGSVRSVAFSPDgRLLASGSADGTVR 271

                        250
                 ....*....|....*...
gi 568984332 221 MWEVREKQQLAAEPVPTG 238
Cdd:COG2319  272 LWDLATGELLRTLTGHSG 289
WD40 COG2319
WD40 repeat [General function prediction only];
83-231 1.72e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984332  83 WDI---IEVKRLLDHQDNILSLAnINDTG--FVTGSHVGELLIWDaldwtvqacertfwsptaqLDAQQEIKLFQKQNDi 157
Cdd:COG2319  231 WDLatgKLLRTLTGHSGSVRSVA-FSPDGrlLASGSADGTVRLWD-------------------LATGELLRTLTGHSG- 289

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568984332 158 SINH--FTCDEENIFAA-VGRGLYVYNLQLKRVIAcQKTAHDSNILHIDKLPN-RQLISCSEDGAVRMWEVREKQQLA 231
Cdd:COG2319  290 GVNSvaFSPDGKLLASGsDDGTVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDgKTLASGSDDGTVRLWDLATGELLR 366
 
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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