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Conserved domains on  [gi|1034645341|ref|XP_016865089|]
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WD repeat-containing protein 55 isoform X2 [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 ...
 6-169 1.57e-20

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: 87.01  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET-GECV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMVPV-TESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDMA 164
Cdd:cd00200    87 RTLTGHTSYVSSVAFSpDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIKLWDLR 165


                  ....*
gi 1034645341 165 QLRAV 169
Cdd:cd00200   166 TGKCV 170
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 6-169 1.57e-20

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: 87.01  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET-GECV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMVPV-TESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDMA 164
Cdd:cd00200    87 RTLTGHTSYVSSVAFSpDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIKLWDLR 165


                  ....*
gi 1034645341 165 QLRAV 169
Cdd:cd00200   166 TGKCV 170
WD40 COG2319
WD40 repeat [General function prediction only];
6-171 7.15e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.33  E-value: 7.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:COG2319   203 HTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMV--PvTESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDM 163
Cdd:COG2319   282 RTLTGHSGGVNSVAfsP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKTLASGSDDGTVRLWDL 359


                  ....*...
gi 1034645341 164 AQLRAVVV 171
Cdd:COG2319   360 ATGELLRT 367
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 122-162 1.66e-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: 35.37  E-value: 1.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034645341  122 PNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWD 162
Cdd:smart00320   1 SGELLKTLKGHTG-PVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
123-162 8.33e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.09  E-value: 8.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034645341 123 NRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWD 162
Cdd:pfam00400   1 GKLLKTLEGHTG-SVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 6-169 1.57e-20

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: 87.01  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET-GECV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMVPV-TESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDMA 164
Cdd:cd00200    87 RTLTGHTSYVSSVAFSpDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIKLWDLR 165


                  ....*
gi 1034645341 165 QLRAV 169
Cdd:cd00200   166 TGKCV 170
WD40 COG2319
WD40 repeat [General function prediction only];
6-171 7.15e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.33  E-value: 7.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:COG2319   203 HTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMV--PvTESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDM 163
Cdd:COG2319   282 RTLTGHSGGVNSVAfsP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKTLASGSDDGTVRLWDL 359


                  ....*...
gi 1034645341 164 AQLRAVVV 171
Cdd:COG2319   360 ATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
6-164 6.92e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 6.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:COG2319   245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLL 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMV--PVTESLLcTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDM 163
Cdd:COG2319   324 RTLTGHTGAVRSVAfsPDGKTLA-SGSDDGTVRLWDLATGELLRTLTGHTG-AVTSVAFSPDGRTLASGSADGTVRLWDL 401


                  .
gi 1034645341 164 A 164
Cdd:COG2319   402 A 402
WD40 COG2319
WD40 repeat [General function prediction only];
6-195 1.89e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.48  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGATS 85
Cdd:COG2319   119 HTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  86 DRFALRAESIDCMV--PvTESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWDm 163
Cdd:COG2319   198 RTLTGHTGAVRSVAfsP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWD- 274

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034645341 164 aqlravvVDDYRRRKKKGGPLRALSSKTWSTD 195
Cdd:COG2319   275 -------LATGELLRTLTGHSGGVNSVAFSPD 299
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-163 3.98e-14

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: 69.67  E-value: 3.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   3 MRQHEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGFG 82
Cdd:cd00200    89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  83 aTSDRFALRAESIDCMVPV-TESLLCTGSTDGVIRAVNILPNRVVGSVGQHTgEPVEELALSHCGRFLASSGHDQRLKFW 161
Cdd:cd00200   169 -CVATLTGHTGEVNSVAFSpDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHE-NGVNSVAFSPDGYLLASGSEDGTIRVW 246


                  ..
gi 1034645341 162 DM 163
Cdd:cd00200   247 DL 248
WD40 COG2319
WD40 repeat [General function prediction only];
4-169 2.24e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.01  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   4 RQHEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGfGA 83
Cdd:COG2319    75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-GK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  84 TSDRFALRAESIDCMV--PVTESLLcTGSTDGVIRAVNILPNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFW 161
Cdd:COG2319   154 LLRTLTGHSGAVTSVAfsPDGKLLA-SGSDDGTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLW 231


                  ....*...
gi 1034645341 162 DMAQLRAV 169
Cdd:COG2319   232 DLATGKLL 239
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-162 4.80e-12

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: 4.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341   3 MRQHEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLfnWN-GF 81
Cdd:cd00200   131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL--WDlST 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645341  82 GATSDRFALRAESIDCMVP-VTESLLCTGSTDGVIRAVNILPNRVVGSVGQHTgEPVEELALSHCGRFLASSGHDQRLKF 160
Cdd:cd00200   209 GKCLGTLRGHENGVNSVAFsPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT-NSVTSLAWSPDGKRLASGSADGTIRI 287


                  ..
gi 1034645341 161 WD 162
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
6-80 7.55e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 7.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034645341   6 HEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNG 80
Cdd:COG2319   329 HTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 122-162 1.66e-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: 35.37  E-value: 1.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034645341  122 PNRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWD 162
Cdd:smart00320   1 SGELLKTLKGHTG-PVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
123-162 8.33e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.09  E-value: 8.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034645341 123 NRVVGSVGQHTGePVEELALSHCGRFLASSGHDQRLKFWD 162
Cdd:pfam00400   1 GKLLKTLEGHTG-SVTSLAFSPDGKLLASGSDDGTVKVWD 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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