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Conserved domains on  [gi|254553448|ref|NP_851938|]
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DDB1- and CUL4-associated factor 4 isoform 3 [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];
225-409 7.31e-11

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.39  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 225 AWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLrcgnQGKGWKA 304
Cdd:COG2319   39 VASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL----ATGLLLR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 305 TRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRI 380
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHsgaVTSVAFSP------DGkLLASGSDDGTVRL 188

                        170       180
                 ....*....|....*....|....*....
gi 254553448 381 WSLHDARLLRTIpspyPASKADIPSVAFS 409
Cdd:COG2319  189 WDLATGKLLRTL----TGHTGAVRSVAFS 213
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
225-409 7.31e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.39  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 225 AWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLrcgnQGKGWKA 304
Cdd:COG2319   39 VASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL----ATGLLLR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 305 TRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRI 380
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHsgaVTSVAFSP------DGkLLASGSDDGTVRL 188

                        170       180
                 ....*....|....*....|....*....
gi 254553448 381 WSLHDARLLRTIpspyPASKADIPSVAFS 409
Cdd:COG2319  189 WDLATGKLLRTL----TGHTGAVRSVAFS 213
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 255-382 2.41e-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: 61.20  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 255 TGHrqsfgtNSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNqgkgWKATRLFHDSAVTSVRILQDEQYLMASDMAGKI 334
Cdd:cd00200  174 TGH------TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK----CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 254553448 335 KLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIWS 382
Cdd:cd00200  244 RVWDLRTGECVQTLSGHTNSvTS---LAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 309-338 4.20e-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: 34.98  E-value: 4.20e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 254553448   309 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 338
Cdd:smart00320  11 HTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
309-338 5.40e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 5.40e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 254553448  309 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 338
Cdd:pfam00400  10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
225-409 7.31e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.39  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 225 AWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLrcgnQGKGWKA 304
Cdd:COG2319   39 VASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL----ATGLLLR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 305 TRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRI 380
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHsgaVTSVAFSP------DGkLLASGSDDGTVRL 188

                        170       180
                 ....*....|....*....|....*....
gi 254553448 381 WSLHDARLLRTIpspyPASKADIPSVAFS 409
Cdd:COG2319  189 WDLATGKLLRTL----TGHTGAVRSVAFS 213
WD40 COG2319
WD40 repeat [General function prediction only];
309-409 1.62e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 309 HDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRIWSLH 384
Cdd:COG2319  245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHsggVNSVAFSP------DGkLLASGSDDGTVRLWDLA 318

                         90       100
                 ....*....|....*....|....*
gi 254553448 385 DARLLRTIpspyPASKADIPSVAFS 409
Cdd:COG2319  319 TGKLLRTL----TGHTGAVRSVAFS 339
WD40 COG2319
WD40 repeat [General function prediction only];
309-409 2.11e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.24  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 309 HDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGHVNeyAYLPLHVHEEEGILVAVGQDCYTRIWSLHDARL 388
Cdd:COG2319  287 HSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG--AVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                         90       100
                 ....*....|....*....|.
gi 254553448 389 LRTIpspyPASKADIPSVAFS 409
Cdd:COG2319  365 LRTL----TGHTGAVTSVAFS 381
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 255-382 2.41e-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: 61.20  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 255 TGHrqsfgtNSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNqgkgWKATRLFHDSAVTSVRILQDEQYLMASDMAGKI 334
Cdd:cd00200  174 TGH------TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK----CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 254553448 335 KLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIWS 382
Cdd:cd00200  244 RVWDLRTGECVQTLSGHTNSvTS---LAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
309-409 3.48e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 309 HDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPlhvheeEG-ILVAVGQDCYTRIWSLH 384
Cdd:COG2319  161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHtgaVRSVAFSP------DGkLLASGSADGTVRLWDLA 234

                         90       100
                 ....*....|....*....|....*
gi 254553448 385 DARLLRTIPSPypasKADIPSVAFS 409
Cdd:COG2319  235 TGKLLRTLTGH----SGSVRSVAFS 255
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 250-409 3.85e-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: 60.43  E-value: 3.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 250 LTNVVTGHRqsfgtnSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNQgkgwKATRLFHDSAVTSVRILQDEQYLMASD 329
Cdd:cd00200    1 LRRTLKGHT------GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL----LRTLKGHTGPVRDVAASADGTYLASGS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 330 MAGKIKLWDLRTTKCVRQYEGH---VNEYAYLPLHvheeeGILVAVGQDCYTRIWSLHDARLLRTIPSPypasKADIPSV 406
Cdd:cd00200   71 SDKTIRLWDLETGECVRTLTGHtsyVSSVAFSPDG-----RILSSSSRDKTIKVWDVETGKCLTTLRGH----TDWVNSV 141


                 ...
gi 254553448 407 AFS 409
Cdd:cd00200  142 AFS 144
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 303-410 3.85e-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: 60.43  E-value: 3.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 303 KATRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGHVNE-YAylpLHVHEEEGILVAVGQDCYTRIW 381
Cdd:cd00200  128 LTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEvNS---VAFSPDGEKLLSSSSDGTIKLW 204

                         90       100
                 ....*....|....*....|....*....
gi 254553448 382 SLHDARLLRTipspYPASKADIPSVAFSS 410
Cdd:cd00200  205 DLSTGKCLGT----LRGHENGVNSVAFSP 229
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 308-389 2.58e-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: 39.52  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553448 308 FHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEG----HVNEyaylpLHVHEEEGILVAVGQDCYTRIWSL 383
Cdd:cd22857  221 FGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCFKGkcggSIRS-----IARHPELPLIASCGLDRYLRIWDT 295


                 ....*.
gi 254553448 384 HDARLL 389
Cdd:cd22857  296 ETRQLL 301
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 309-338 4.20e-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: 34.98  E-value: 4.20e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 254553448   309 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 338
Cdd:smart00320  11 HTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
309-338 5.40e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 5.40e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 254553448  309 HDSAVTSVRILQDEQYLMASDMAGKIKLWD 338
Cdd:pfam00400  10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
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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