NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564347527|ref|XP_006236840|]
View 

WD repeat-containing protein 54 isoform X1 [Rattus norvegicus]

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
SCOP:  4002744

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
131-280 8.06e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 52.72  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 131 HFICVGTWSGRILVFDIPakgpNIVLNEELAGHQTPITDIAteraQGQDGvADMVTADDSGVLCVWRSgPEFTLLTRIAG 210
Cdd:cd00200  148 TFVASSSQDGTIKLWDLR----TGKCVATLTGHTGEVNSVA----FSPDG-EKLLSSSSDGTIKLWDL-STGKCLGTLRG 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564347527 211 FGVPCPSVQL--WQGIVAAGYGNGQVRLYDAGTGALHIQISAHARTISALDLAPEVGKLLSAAEDTFVHIWK 280
Cdd:cd00200  218 HENGVNSVAFspDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 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 ...
131-280 8.06e-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: 52.72  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 131 HFICVGTWSGRILVFDIPakgpNIVLNEELAGHQTPITDIAteraQGQDGvADMVTADDSGVLCVWRSgPEFTLLTRIAG 210
Cdd:cd00200  148 TFVASSSQDGTIKLWDLR----TGKCVATLTGHTGEVNSVA----FSPDG-EKLLSSSSDGTIKLWDL-STGKCLGTLRG 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564347527 211 FGVPCPSVQL--WQGIVAAGYGNGQVRLYDAGTGALHIQISAHARTISALDLAPEVGKLLSAAEDTFVHIWK 280
Cdd:cd00200  218 HENGVNSVAFspDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
135-282 9.75e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.91  E-value: 9.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 135 VGTWSGRILVFDIpAKGPNIVLneeLAGHQTPITDIATeRAQGQDgvadMVTADDSGVLCVWrSGPEFTLLTRIAGFGVP 214
Cdd:COG2319  263 SGSADGTVRLWDL-ATGELLRT---LTGHSGGVNSVAF-SPDGKL----LASGSDDGTVRLW-DLATGKLLRTLTGHTGA 332
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 215 CPSVQL--WQGIVAAGYGNGQVRLYDAGTGALHIQISAHARTISALDLAPEVGKLLSAAEDTFVHIWKLN 282
Cdd:COG2319  333 VRSVAFspDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
131-280 8.06e-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: 52.72  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 131 HFICVGTWSGRILVFDIPakgpNIVLNEELAGHQTPITDIAteraQGQDGvADMVTADDSGVLCVWRSgPEFTLLTRIAG 210
Cdd:cd00200  148 TFVASSSQDGTIKLWDLR----TGKCVATLTGHTGEVNSVA----FSPDG-EKLLSSSSDGTIKLWDL-STGKCLGTLRG 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564347527 211 FGVPCPSVQL--WQGIVAAGYGNGQVRLYDAGTGALHIQISAHARTISALDLAPEVGKLLSAAEDTFVHIWK 280
Cdd:cd00200  218 HENGVNSVAFspDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
135-282 9.75e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.91  E-value: 9.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 135 VGTWSGRILVFDIpAKGPNIVLneeLAGHQTPITDIATeRAQGQDgvadMVTADDSGVLCVWrSGPEFTLLTRIAGFGVP 214
Cdd:COG2319  263 SGSADGTVRLWDL-ATGELLRT---LTGHSGGVNSVAF-SPDGKL----LASGSDDGTVRLW-DLATGKLLRTLTGHTGA 332
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 215 CPSVQL--WQGIVAAGYGNGQVRLYDAGTGALHIQISAHARTISALDLAPEVGKLLSAAEDTFVHIWKLN 282
Cdd:COG2319  333 VRSVAFspDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
99-314 2.85e-05

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: 45.02  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527  99 SDGSVMVyWHaLDSGDASSVQ---AMFARGIAASVH--FICVGTWSGRILVFDIpaKGPNIVlnEELAGHQTPITDIAte 173
Cdd:cd00200   29 GDGTIKV-WD-LETGELLRTLkghTGPVRDVAASADgtYLASGSSDKTIRLWDL--ETGECV--RTLTGHTSYVSSVA-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 174 rAQGQDGVAdmVTADDSGVLCVWrSGPEFTLLTRIAGF--GVPCPSVQLWQGIVAAGYGNGQVRLYDAGTGALHIQISAH 251
Cdd:cd00200  101 -FSPDGRIL--SSSSRDKTIKVW-DVETGKCLTTLRGHtdWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564347527 252 ARTISALDLAPEVGKLLSAAEDTFVHIWKLNrnpesgsieVEHCHGECISDTQ-VCGARFCDPG 314
Cdd:cd00200  177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS---------TGKCLGTLRGHENgVNSVAFSPDG 231
WD40 COG2319
WD40 repeat [General function prediction only];
160-281 9.47e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.75  E-value: 9.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 160 LAGHQTPITDIATERAQGQDGVADMVTADDSGVLCVWRSGPEFTLLTRIAGFGVPCPSVQLWQGIVAAGYGNGQVRLYDA 239
Cdd:COG2319   28 LLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL 107
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 564347527 240 GTGALHIQISAHARTISALDLAPEVGKLLSAAEDTFVHIWKL 281
Cdd:COG2319  108 ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL 149
WD40 COG2319
WD40 repeat [General function prediction only];
135-282 1.07e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.75  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347527 135 VGTWSGRILVFDIpAKGPNIvlnEELAGHQTPITDIATeRAQGQDgvadMVTADDSGVLCVWRSgPEFTLLTRIAGFGVP 214
Cdd:COG2319  137 SGSADGTVRLWDL-ATGKLL---RTLTGHSGAVTSVAF-SPDGKL----LASGSDDGTVRLWDL-ATGKLLRTLTGHTGA 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564347527 215 CPSVQLWQG--IVAAGYGNGQVRLYDAGTGALHIQISAHARTISALDLAPEvGKLL-SAAEDTFVHIWKLN 282
Cdd:COG2319  207 VRSVAFSPDgkLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPD-GRLLaSGSADGTVRLWDLA 276
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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