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Conserved domains on  [gi|1206876213|ref|NP_001339376|]
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DDB1- and CUL4-associated factor 4 isoform 6 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to 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
PubMed:  10322433|8090199
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];
71-255 3.30e-11

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.01  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213  71 AWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLrcgnQGKGWKA 150
Cdd:COG2319    39 VASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL----ATGLLLR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 151 TRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRI 226
Cdd:COG2319   115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHsgaVTSVAFSP------DGkLLASGSDDGTVRL 188
                         170       180
                  ....*....|....*....|....*....
gi 1206876213 227 WSLHDARLLRTIpspyPASKADIPSVAFS 255
Cdd:COG2319   189 WDLATGKLLRTL----TGHTGAVRSVAFS 213
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
71-255 3.30e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.01  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213  71 AWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLrcgnQGKGWKA 150
Cdd:COG2319    39 VASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL----ATGLLLR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 151 TRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRI 226
Cdd:COG2319   115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHsgaVTSVAFSP------DGkLLASGSDDGTVRL 188
                         170       180
                  ....*....|....*....|....*....
gi 1206876213 227 WSLHDARLLRTIpspyPASKADIPSVAFS 255
Cdd:COG2319   189 WDLATGKLLRTL----TGHTGAVRSVAFS 213
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
101-228 2.46e-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: 59.66  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 101 TGHrqsfgtNSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNqgkgWKATRLFHDSAVTSVRILQDEQYLMASDMAGKI 180
Cdd:cd00200   174 TGH------TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK----CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1206876213 181 KLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIWS 228
Cdd:cd00200   244 RVWDLRTGECVQTLSGHTNSvTS---LAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
155-184 4.48e-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: 34.21  E-value: 4.48e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1206876213  155 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 184
Cdd:smart00320  11 HTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
155-184 5.43e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.86  E-value: 5.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1206876213 155 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 184
Cdd:pfam00400  10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
71-255 3.30e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.01  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213  71 AWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLrcgnQGKGWKA 150
Cdd:COG2319    39 VASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL----ATGLLLR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 151 TRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRI 226
Cdd:COG2319   115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHsgaVTSVAFSP------DGkLLASGSDDGTVRL 188
                         170       180
                  ....*....|....*....|....*....
gi 1206876213 227 WSLHDARLLRTIpspyPASKADIPSVAFS 255
Cdd:COG2319   189 WDLATGKLLRTL----TGHTGAVRSVAFS 213
WD40 COG2319
WD40 repeat [General function prediction only];
155-255 7.94e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 7.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 155 HDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRIWSLH 230
Cdd:COG2319   245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHsggVNSVAFSP------DGkLLASGSDDGTVRLWDLA 318
                          90       100
                  ....*....|....*....|....*
gi 1206876213 231 DARLLRTIpspyPASKADIPSVAFS 255
Cdd:COG2319   319 TGKLLRTL----TGHTGAVRSVAFS 339
WD40 COG2319
WD40 repeat [General function prediction only];
155-255 9.12e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 9.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 155 HDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGHVNeyAYLPLHVHEEEGILVAVGQDCYTRIWSLHDARL 234
Cdd:COG2319   287 HSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG--AVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
                          90       100
                  ....*....|....*....|.
gi 1206876213 235 LRTIpspyPASKADIPSVAFS 255
Cdd:COG2319   365 LRTL----TGHTGAVTSVAFS 381
WD40 COG2319
WD40 repeat [General function prediction only];
155-255 1.68e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 155 HDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRIWSLH 230
Cdd:COG2319   161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHtgaVRSVAFSP------DGkLLASGSADGTVRLWDLA 234
                          90       100
                  ....*....|....*....|....*
gi 1206876213 231 DARLLRTIPSPypasKADIPSVAFS 255
Cdd:COG2319   235 TGKLLRTLTGH----SGSVRSVAFS 255
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
101-228 2.46e-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: 59.66  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 101 TGHrqsfgtNSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNqgkgWKATRLFHDSAVTSVRILQDEQYLMASDMAGKI 180
Cdd:cd00200   174 TGH------TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK----CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1206876213 181 KLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIWS 228
Cdd:cd00200   244 RVWDLRTGECVQTLSGHTNSvTS---LAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
149-256 3.48e-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: 59.27  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 149 KATRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIW 227
Cdd:cd00200   128 LTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEvNS---VAFSPDGEKLLSSSSDGTIKLW 204
                          90       100
                  ....*....|....*....|....*....
gi 1206876213 228 SLHDARLLRTipspYPASKADIPSVAFSS 256
Cdd:cd00200   205 DLSTGKCLGT----LRGHENGVNSVAFSP 229
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
96-255 4.36e-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: 58.89  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213  96 LTNVVTGHRqsfgtnSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNQgkgwKATRLFHDSAVTSVRILQDEQYLMASD 175
Cdd:cd00200     1 LRRTLKGHT------GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL----LRTLKGHTGPVRDVAASADGTYLASGS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 176 MAGKIKLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIWSLHDARLLRTIPSPypasKADIPSVAF 254
Cdd:cd00200    71 SDKTIRLWDLETGECVRTLTGHTSYvSS---VAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH----TDWVNSVAF 143

                  .
gi 1206876213 255 S 255
Cdd:cd00200   144 S 144
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
154-235 1.05e-03

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 39.90  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 154 FHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEG----HVNEyaylpLHVHEEEGILVAVGQDCYTRIWSL 229
Cdd:cd22857   221 FGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCFKGkcggSIRS-----IARHPELPLIASCGLDRYLRIWDT 295

                  ....*.
gi 1206876213 230 HDARLL 235
Cdd:cd22857   296 ETRQLL 301
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
155-184 4.48e-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: 34.21  E-value: 4.48e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1206876213  155 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 184
Cdd:smart00320  11 HTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
155-184 5.43e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.86  E-value: 5.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1206876213 155 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 184
Cdd:pfam00400  10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 COG2319
WD40 repeat [General function prediction only];
150-255 7.59e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 37.58  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206876213 150 ATRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGHVNeyAYLPLHVHEEEGILVAVGQDCYTRIWSL 229
Cdd:COG2319    30 LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA--AVLSVAFSPDGRLLASASADGTVRLWDL 107
                          90       100
                  ....*....|....*....|....*.
gi 1206876213 230 HDARLLRTIpspyPASKADIPSVAFS 255
Cdd:COG2319   108 ATGLLLRTL----TGHTGAVRSVAFS 129
 
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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