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Conserved domains on  [gi|146149345|ref|NP_001025126|]
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DDB1- and CUL4-associated factor 4-like protein 1 [Homo sapiens]

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 ...
 210-368 3.25e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 63.51  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 210 LTSVATGHqqsfdtSSDVLAQQFASTAPLLFNGCRSGEIFAIDLRCRNRgkgwRATRLFHDSAVTSVQILQEEQCLMASD 289
Cdd:cd00200  127 CLTTLRGH------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC----VATLTGHTGEVNSVAFSPDGEKLLSSS 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146149345 290 MTGKIKLWDLRATKCVRQYEGHVNESAYlpLHVHEEEGIVVAVGQDCYTRIWSLHDAHLLRTIpspySASEDDIPSVAF 368
Cdd:cd00200  197 SDGTIKLWDLSTGKCLGTLRGHENGVNS--VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL----SGHTNSVTSLAW 269
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 210-368 3.25e-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: 63.51  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 210 LTSVATGHqqsfdtSSDVLAQQFASTAPLLFNGCRSGEIFAIDLRCRNRgkgwRATRLFHDSAVTSVQILQEEQCLMASD 289
Cdd:cd00200  127 CLTTLRGH------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC----VATLTGHTGEVNSVAFSPDGEKLLSSS 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146149345 290 MTGKIKLWDLRATKCVRQYEGHVNESAYlpLHVHEEEGIVVAVGQDCYTRIWSLHDAHLLRTIpspySASEDDIPSVAF 368
Cdd:cd00200  197 SDGTIKLWDLSTGKCLGTLRGHENGVNS--VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL----SGHTNSVTSLAW 269
WD40 COG2319
WD40 repeat [General function prediction only];
186-368 1.13e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 186 WSCAWSLNTRayHCFSAGLSQQVLLTSVATGHQQSF--DTSSDVLAQQFASTAPLLFNGCRSGEIFAIDLRcrnrgkGWR 263
Cdd:COG2319  208 RSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTltGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA------TGE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 264 ATRLF--HDSAVTSVQILQEEQCLMASDMTGKIKLWDLRATKCVRQYEGHVNESayLPLHVHEEEGIVVAVGQDCYTRIW 341
Cdd:COG2319  280 LLRTLtgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAV--RSVAFSPDGKTLASGSDDGTVRLW 357

                        170       180
                 ....*....|....*....|....*..
gi 146149345 342 SLHDAHLLRTIpspySASEDDIPSVAF 368
Cdd:COG2319  358 DLATGELLRTL----TGHTGAVTSVAF 380
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 210-368 3.25e-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: 63.51  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 210 LTSVATGHqqsfdtSSDVLAQQFASTAPLLFNGCRSGEIFAIDLRCRNRgkgwRATRLFHDSAVTSVQILQEEQCLMASD 289
Cdd:cd00200  127 CLTTLRGH------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC----VATLTGHTGEVNSVAFSPDGEKLLSSS 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146149345 290 MTGKIKLWDLRATKCVRQYEGHVNESAYlpLHVHEEEGIVVAVGQDCYTRIWSLHDAHLLRTIpspySASEDDIPSVAF 368
Cdd:cd00200  197 SDGTIKLWDLSTGKCLGTLRGHENGVNS--VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL----SGHTNSVTSLAW 269
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 269-368 1.28e-09

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: 58.89  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 269 HDSAVTSVQILQEEQCLMASDMTGKIKLWDLRATKCVRQYEGHvnESAYLPLHVHEEEGIVVAVGQDCYTRIWSLHDAHL 348
Cdd:cd00200   92 HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH--TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC 169

                         90       100
                 ....*....|....*....|
gi 146149345 349 LRTIpspySASEDDIPSVAF 368
Cdd:cd00200  170 VATL----TGHTGEVNSVAF 185
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 210-368 4.34e-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: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 210 LTSVATGHqqsfdtSSDVLAQQFASTAPLLFNGCRSGEIFAIDL---RCRNRGKGwratrlfHDSAVTSVQILQEEQCLM 286
Cdd:cd00200    1 LRRTLKGH------TGGVTCVAFSPDGKLLATGSGDGTIKVWDLetgELLRTLKG-------HTGPVRDVAASADGTYLA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 287 ASDMTGKIKLWDLRATKCVRQYEGHvnESAYLPLHVHEEEGIVVAVGQDCYTRIWSLHDAHLLRTIPSPysasEDDIPSV 366
Cdd:cd00200   68 SGSSDKTIRLWDLETGECVRTLTGH--TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH----TDWVNSV 141


                 ..
gi 146149345 367 AF 368
Cdd:cd00200  142 AF 143
WD40 COG2319
WD40 repeat [General function prediction only];
186-368 1.13e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 186 WSCAWSLNTRayHCFSAGLSQQVLLTSVATGHQQSF--DTSSDVLAQQFASTAPLLFNGCRSGEIFAIDLRcrnrgkGWR 263
Cdd:COG2319  208 RSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTltGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA------TGE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 264 ATRLF--HDSAVTSVQILQEEQCLMASDMTGKIKLWDLRATKCVRQYEGHVNESayLPLHVHEEEGIVVAVGQDCYTRIW 341
Cdd:COG2319  280 LLRTLtgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAV--RSVAFSPDGKTLASGSDDGTVRLW 357

                        170       180
                 ....*....|....*....|....*..
gi 146149345 342 SLHDAHLLRTIpspySASEDDIPSVAF 368
Cdd:COG2319  358 DLATGELLRTL----TGHTGAVTSVAF 380
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 215-342 1.21e-07

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: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 215 TGHQqsfdtsSDVLAQQFASTAPLLFNGCRSGEIFAIDLRCrnrGKgWRATRLFHDSAVTSVQILQEEQCLMASDMTGKI 294
Cdd:cd00200  174 TGHT------GEVNSVAFSPDGEKLLSSSSDGTIKLWDLST---GK-CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 146149345 295 KLWDLRATKCVRQYEGHvNESAYLpLHVHEEEGIVVAVGQDCYTRIWS 342
Cdd:cd00200  244 RVWDLRTGECVQTLSGH-TNSVTS-LAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
201-368 4.43e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.45  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 201 SAGLSQQVLLTSVATGHQQSFDTSSDVLAQQFASTAPLLFNGCRSGEIFAIDLRcrnrGKGWRATRLFHDSAVTSVQILQ 280
Cdd:COG2319   13 SADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA----AGALLATLLGHTAAVLSVAFSP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 281 EEQCLMASDMTGKIKLWDLRATKCVRQYEGH---VNESAYLPlhvheeEG-IVVAVGQDCYTRIWSLHDAHLLRTIPSPy 356
Cdd:COG2319   89 DGRLLASASADGTVRLWDLATGLLLRTLTGHtgaVRSVAFSP------DGkTLASGSADGTVRLWDLATGKLLRTLTGH- 161

                        170
                 ....*....|..
gi 146149345 357 sasEDDIPSVAF 368
Cdd:COG2319  162 ---SGAVTSVAF 170
WD40 COG2319
WD40 repeat [General function prediction only];
185-368 6.78e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.07  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 185 AWSCAWSLNTRAYhcFSAGLSQQVLLTSVATGHQQSFDT--SSDVLAQQFASTAPLLFNGCRSGEIFAIDLRcrnRGKgW 262
Cdd:COG2319   81 VLSVAFSPDGRLL--ASASADGTVRLWDLATGLLLRTLTghTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TGK-L 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146149345 263 RATRLFHDSAVTSVQILQEEQCLMASDMTGKIKLWDLRATKCVRQYEGH---VNESAYLPlhvheeEG-IVVAVGQDCYT 338
Cdd:COG2319  155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHtgaVRSVAFSP------DGkLLASGSADGTV 228

                        170       180       190
                 ....*....|....*....|....*....|
gi 146149345 339 RIWSLHDAHLLRTIPSPysasEDDIPSVAF 368
Cdd:COG2319  229 RLWDLATGKLLRTLTGH----SGSVRSVAF 254
 
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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