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Conserved domains on  [gi|71284432|ref|NP_848565|]
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DDB1- and CUL4-associated factor 12-like protein 1 [Homo sapiens]

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
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

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 ...
 89-227 4.28e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 4.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  89 ERQLELGTVNKVFASQWLNSRQVVCGTKCNTLFVVDVESGHIARIpllrdsearLAQDQQgcGIHAIELNPSKTLLATGG 168
Cdd:cd00200  44 LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT---------LTGHTS--YVSSVAFSPDGRILSSSS 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432 169 ENpNSLAIYQLPSLDplCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKF 227
Cdd:cd00200 113 RD-KTIKVWDVETGK--CLTTLRGHTDWVNSVAFSPDgTFVASSSQDGTIKLWDLRTGKC 169
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 89-227 4.28e-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: 57.34  E-value: 4.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  89 ERQLELGTVNKVFASQWLNSRQVVCGTKCNTLFVVDVESGHIARIpllrdsearLAQDQQgcGIHAIELNPSKTLLATGG 168
Cdd:cd00200  44 LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT---------LTGHTS--YVSSVAFSPDGRILSSSS 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432 169 ENpNSLAIYQLPSLDplCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKF 227
Cdd:cd00200 113 RD-KTIKVWDVETGK--CLTTLRGHTDWVNSVAFSPDgTFVASSSQDGTIKLWDLRTGKC 169
WD40 COG2319
WD40 repeat [General function prediction only];
19-235 1.00e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.76  E-value: 1.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  19 DAESSPSQGLAAADGEGPLLLKRQRRPATYRSMAHYLKVREVGGWGPARLQGFDGELRGYAVQRLPELLTERQLELGTVN 98
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  99 KVFASQWLNSRQVVCGTKCNTLFVVDVESGHIARIPLLRDSearlaqdqqgcGIHAIELNPSKTLLATGGENpNSLAIYQ 178
Cdd:COG2319  81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG-----------AVRSVAFSPDGKTLASGSAD-GTVRLWD 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71284432 179 LPSLDplCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKFDDTVAWHS 235
Cdd:COG2319 149 LATGK--LLRTLTGHSGAVTSVAFSPDgKLLASGSDDGTVRLWDLATGKLLRTLTGHT 204
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 186-220 5.23e-05

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: 40.37  E-value: 5.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 71284432    186 CLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALW 220
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDgKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
186-220 1.13e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 71284432   186 CLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALW 220
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDgKLLASGSDDGTVKVW 38
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 89-227 4.28e-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: 57.34  E-value: 4.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  89 ERQLELGTVNKVFASQWLNSRQVVCGTKCNTLFVVDVESGHIARIpllrdsearLAQDQQgcGIHAIELNPSKTLLATGG 168
Cdd:cd00200  44 LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT---------LTGHTS--YVSSVAFSPDGRILSSSS 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432 169 ENpNSLAIYQLPSLDplCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKF 227
Cdd:cd00200 113 RD-KTIKVWDVETGK--CLTTLRGHTDWVNSVAFSPDgTFVASSSQDGTIKLWDLRTGKC 169
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 98-381 1.82e-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: 55.42  E-value: 1.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  98 NKVFASQWLNSRQVVC-GTKCNTLFVVDVESGHIARipllrdsearlaqdqQGCGiHAIELN-----PSKTLLATGGENp 171
Cdd:cd00200  10 GGVTCVAFSPDGKLLAtGSGDGTIKVWDLETGELLR---------------TLKG-HTGPVRdvaasADGTYLASGSSD- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432 172 NSLAIYQLPSLDplCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKFDDTVAWHSevglpvyahirpRDV 250
Cdd:cd00200  73 KTIRLWDLETGE--CVRTLTGHTSYVSSVAFSPDgRILSSSSRDKTIKVWDVETGKCLTTLRGHT------------DWV 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432 251 EAIPraiINPSNRkvraLACGGknqelgavSLDGYFHLW--KAGSALSRLLSirlpyFRDNV-CLTYCDDMSVYAVGSHS 327
Cdd:cd00200 139 NSVA---FSPDGT----FVASS--------SQDGTIKLWdlRTGKCVATLTG-----HTGEVnSVAFSPDGEKLLSSSSD 198

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71284432 328 HVSFL-DLRQDQQnirpLCSREG-GTGVRSLSFY--RHIITVGTGQGSLLFYDVRAQK 381
Cdd:cd00200 199 GTIKLwDLSTGKC----LGTLRGhENGVNSVAFSpdGYLLASGSEDGTIRVWDLRTGE 252
WD40 COG2319
WD40 repeat [General function prediction only];
19-235 1.00e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.76  E-value: 1.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  19 DAESSPSQGLAAADGEGPLLLKRQRRPATYRSMAHYLKVREVGGWGPARLQGFDGELRGYAVQRLPELLTERQLELGTVN 98
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  99 KVFASQWLNSRQVVCGTKCNTLFVVDVESGHIARIPLLRDSearlaqdqqgcGIHAIELNPSKTLLATGGENpNSLAIYQ 178
Cdd:COG2319  81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG-----------AVRSVAFSPDGKTLASGSAD-GTVRLWD 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71284432 179 LPSLDplCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKFDDTVAWHS 235
Cdd:COG2319 149 LATGK--LLRTLTGHSGAVTSVAFSPDgKLLASGSDDGTVRLWDLATGKLLRTLTGHT 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 95-236 3.00e-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: 51.95  E-value: 3.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  95 GTVNKVFASQwlNSRQVVCGTKCNTLFVVDVESGHIARipLLRDSEarlaqdqqgCGIHAIELNPSKTLLATGGENpNSL 174
Cdd:cd00200 136 DWVNSVAFSP--DGTFVASSSQDGTIKLWDLRTGKCVA--TLTGHT---------GEVNSVAFSPDGEKLLSSSSD-GTI 201

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71284432 175 AIYQLPSLDplCLGDRHGHKDWIFAVAWLSDT-VAVSGSRDGTVALWRMDPDKFDDTVAWHSE 236
Cdd:cd00200 202 KLWDLSTGK--CLGTLRGHENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTN 262
WD40 COG2319
WD40 repeat [General function prediction only];
70-223 4.85e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.84  E-value: 4.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432  70 GFDGELRGYAVQRlPELLTERQLELGTVNKVFASQwlNSRQVVCGTKCNTLFVVDVESGHIARIplLRDSEARlaqdqqg 149
Cdd:COG2319 265 SADGTVRLWDLAT-GELLRTLTGHSGGVNSVAFSP--DGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGA------- 332

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71284432 150 cgIHAIELNPSKTLLATGGENpNSLAIYQLPSldPLCLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMD 223
Cdd:COG2319 333 --VRSVAFSPDGKTLASGSDD-GTVRLWDLAT--GELLRTLTGHTGAVTSVAFSPDgRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
107-235 1.32e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 1.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284432 107 NSRQVVCGTKCNTLFVVDVESGHIARIPllrdsearlaqDQQGCGIHAIELNPSKTLLATGGENpNSLAIYQLPSLDplC 186
Cdd:COG2319 257 DGRLLASGSADGTVRLWDLATGELLRTL-----------TGHSGGVNSVAFSPDGKLLASGSDD-GTVRLWDLATGK--L 322

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 71284432 187 LGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALWRMDPDKFDDTVAWHS 235
Cdd:COG2319 323 LRTLTGHTGAVRSVAFSPDgKTLASGSDDGTVRLWDLATGELLRTLTGHT 372
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 186-220 5.23e-05

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: 40.37  E-value: 5.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 71284432    186 CLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALW 220
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDgKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
186-220 1.13e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 71284432   186 CLGDRHGHKDWIFAVAWLSD-TVAVSGSRDGTVALW 220
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDgKLLASGSDDGTVKVW 38
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 192-235 9.38e-04

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: 41.17  E-value: 9.38e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71284432 192 GHKDWIFAVAWLSDT-VAVSGSRDGTVALWRMDPDKFDDTVAWHS 235
Cdd:cd00200   7 GHTGGVTCVAFSPDGkLLATGSGDGTIKVWDLETGELLRTLKGHT 51
 
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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