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Conserved domains on  [gi|237820620|ref|NP_113673|]
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glutamate-rich WD repeat-containing protein 1 [Homo sapiens]

Protein Classification

WD repeat RBAP46/RBAP48/MSI1 family protein( domain architecture ID 13780222)

WD repeat RBAP46/RBAP48/MSI1 family protein binds histones; contains an N-terminal alpha helical domain and WD40 repeats that fold into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome

CATH:  2.130.10.10
Gene Ontology:  GO:0005515|GO:0042393
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4005630|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 ...
 204-384 1.50e-29

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: 116.67  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 204 MKPIFSFAGHMGEGFALDWSPRvTGRLLTGDCQKNIHLWTPTDGGSwhvdQRPFVGHTRSVEDLQWSPTeNTVFASCSAD 283
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGEC----VRTLTGHTSYVSSVAFSPD-GRILSSSSRD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSKacmlTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHP 363
Cdd:cd00200  115 KTIKVWDVETGKCL----TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP 187

                        170       180
                 ....*....|....*....|.
gi 237820620 364 qDSGVFAASGADHQITQWDLA 384
Cdd:cd00200  188 -DGEKLLSSSSDGTIKLWDLS 207
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 44-112 2.50e-07

Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved heterotrimeric protein complex that promotes histone H3 and H4 deposition onto newly synthesized DNA during replication or DNA repair; specifically it facilitates replication-dependent nucleosome assembly with the major histone H3 (H3.1). This domain is an alpha helix which sits just upstream of the WD40 seven-bladed beta-propeller in the human RbAp46 protein. RbAp46 folds into the beta-propeller and binds histone H4 in a groove formed between this N-terminal helix and an extended loop inserted into blade six.


:

Pssm-ID: 463513  Cd Length: 69  Bit Score: 47.57  E-value: 2.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237820620   44 GEELVMDEEAYVLY---HRAQTGAPCLSFDIVRDHLGDNRTelpLTLYLCAGTQAESAQSNRLMMLRMHNLH 112
Cdd:pfam12265   1 EEYLIWKKNAPFLYdmlHTHALEWPSLSFDWFPDTSEGKNY---TVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 204-384 1.50e-29

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: 116.67  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 204 MKPIFSFAGHMGEGFALDWSPRvTGRLLTGDCQKNIHLWTPTDGGSwhvdQRPFVGHTRSVEDLQWSPTeNTVFASCSAD 283
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGEC----VRTLTGHTSYVSSVAFSPD-GRILSSSSRD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSKacmlTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHP 363
Cdd:cd00200  115 KTIKVWDVETGKCL----TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP 187

                        170       180
                 ....*....|....*....|.
gi 237820620 364 qDSGVFAASGADHQITQWDLA 384
Cdd:cd00200  188 -DGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
205-384 7.99e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 114.24  E-value: 7.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 205 KPIFSFAGHMGEGFALDWSPRvtGRLL-TGDCQKNIHLWTPTDGGSwhvdQRPFVGHTRSVEDLQWSPTENTVfASCSAD 283
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPD--GKLLaSGSADGTVRLWDLATGKL----LRTLTGHSGSVRSVAFSPDGRLL-ASGSAD 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSkacmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLrqfKSGSPVATFKQHVAPVTSVEWHP 363
Cdd:COG2319  268 GTVRLWDLATGEL----LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAVRSVAFSP 340

                        170       180
                 ....*....|....*....|.
gi 237820620 364 qDSGVFAASGADHQITQWDLA 384
Cdd:COG2319  341 -DGKTLASGSDDGTVRLWDLA 360
PTZ00420 PTZ00420
coronin; Provisional
 259-361 2.87e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 62.27  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 259 GHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPSKA-------CMLttaTAHDGDVNVISWSRREPFLL-SGGDDG 330
Cdd:PTZ00420  72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVkeikdpqCIL---KGHKKKISIIDWNPMNYYIMcSSGFDS 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 237820620 331 ALKIWDLRQFKSGSPVATFKQhvapVTSVEW 361
Cdd:PTZ00420 149 FVNIWDIENEKRAFQINMPKK----LSSLKW 175
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 44-112 2.50e-07

Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved heterotrimeric protein complex that promotes histone H3 and H4 deposition onto newly synthesized DNA during replication or DNA repair; specifically it facilitates replication-dependent nucleosome assembly with the major histone H3 (H3.1). This domain is an alpha helix which sits just upstream of the WD40 seven-bladed beta-propeller in the human RbAp46 protein. RbAp46 folds into the beta-propeller and binds histone H4 in a groove formed between this N-terminal helix and an extended loop inserted into blade six.


Pssm-ID: 463513  Cd Length: 69  Bit Score: 47.57  E-value: 2.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237820620   44 GEELVMDEEAYVLY---HRAQTGAPCLSFDIVRDHLGDNRTelpLTLYLCAGTQAESAQSNRLMMLRMHNLH 112
Cdd:pfam12265   1 EEYLIWKKNAPFLYdmlHTHALEWPSLSFDWFPDTSEGKNY---TVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 257-290 9.84e-07

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: 45.00  E-value: 9.84e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 237820620   257 FVGHTRSVEDLQWSPTeNTVFASCSADASIRIWD 290
Cdd:smart00320   8 LKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
301-336 5.24e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 5.24e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 237820620  301 LTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWD 336
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 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 ...
 204-384 1.50e-29

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: 116.67  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 204 MKPIFSFAGHMGEGFALDWSPRvTGRLLTGDCQKNIHLWTPTDGGSwhvdQRPFVGHTRSVEDLQWSPTeNTVFASCSAD 283
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGEC----VRTLTGHTSYVSSVAFSPD-GRILSSSSRD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSKacmlTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHP 363
Cdd:cd00200  115 KTIKVWDVETGKCL----TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP 187

                        170       180
                 ....*....|....*....|.
gi 237820620 364 qDSGVFAASGADHQITQWDLA 384
Cdd:cd00200  188 -DGEKLLSSSSDGTIKLWDLS 207
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 205-382 1.61e-29

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: 116.67  E-value: 1.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 205 KPIFSFAGHMGEGFALDWSPrvTGRLLTGDCQ-KNIHLWtptDGGSWHVDQRpFVGHTRSVEDLQWSPTENTvFASCSAD 283
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSP--DGTFVASSSQdGTIKLW---DLRTGKCVAT-LTGHTGEVNSVAFSPDGEK-LLSSSSD 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSKACMlttaTAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHP 363
Cdd:cd00200  199 GTIKLWDLSTGKCLGTL----RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR---TGECVQTLSGHTNSVTSLAWSP 271

                        170
                 ....*....|....*....
gi 237820620 364 qDSGVFAASGADHQITQWD 382
Cdd:cd00200  272 -DGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 205-383 1.05e-28

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: 114.35  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 205 KPIFSFAGHMGEGFALDWSPrvTGRLLTGD-CQKNIHLWTPTDGGSwhvdQRPFVGHTRSVEDLQWSPTENTVfASCSAD 283
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSP--DGRILSSSsRDKTIKVWDVETGKC----LTTLRGHTDWVNSVAFSPDGTFV-ASSSQD 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSKAcmltTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHP 363
Cdd:cd00200  157 GTIKLWDLRTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS---TGKCLGTLRGHENGVNSVAFSP 229

                        170       180
                 ....*....|....*....|
gi 237820620 364 qDSGVFAASGADHQITQWDL 383
Cdd:cd00200  230 -DGYLLASGSEDGTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
205-384 7.99e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 114.24  E-value: 7.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 205 KPIFSFAGHMGEGFALDWSPRvtGRLL-TGDCQKNIHLWTPTDGGSwhvdQRPFVGHTRSVEDLQWSPTENTVfASCSAD 283
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPD--GKLLaSGSADGTVRLWDLATGKL----LRTLTGHSGSVRSVAFSPDGRLL-ASGSAD 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSkacmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLrqfKSGSPVATFKQHVAPVTSVEWHP 363
Cdd:COG2319  268 GTVRLWDLATGEL----LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAVRSVAFSP 340

                        170       180
                 ....*....|....*....|.
gi 237820620 364 qDSGVFAASGADHQITQWDLA 384
Cdd:COG2319  341 -DGKTLASGSDDGTVRLWDLA 360
WD40 COG2319
WD40 repeat [General function prediction only];
205-384 1.28e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.77  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 205 KPIFSFAGHMGEGFALDWSPrvTGRLL-TGDCQKNIHLWTPTDGGSWhvdqRPFVGHTRSVEDLQWSPTENTVfASCSAD 283
Cdd:COG2319  237 KLLRTLTGHSGSVRSVAFSP--DGRLLaSGSADGTVRLWDLATGELL----RTLTGHSGGVNSVAFSPDGKLL-ASGSDD 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 284 ASIRIWDIRAAPSkacmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHP 363
Cdd:COG2319  310 GTVRLWDLATGKL----LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA---TGELLRTLTGHTGAVTSVAFSP 382

                        170       180
                 ....*....|....*....|.
gi 237820620 364 qDSGVFAASGADHQITQWDLA 384
Cdd:COG2319  383 -DGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
205-384 9.47e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.46  E-value: 9.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 205 KPIFSFAGHMGEGFALDWSPRvTGRLLTGDCQKNIHLWTPTDGGSWHVdqrpFVGHTRSVEDLQWSPTENTVfASCSADA 284
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLATGKLLRT----LTGHSGAVTSVAFSPDGKLL-ASGSDDG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 285 SIRIWDIRAAPSkacmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRqfkSGSPVATFKQHVAPVTSVEWHPq 364
Cdd:COG2319  185 TVRLWDLATGKL----LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA---TGKLLRTLTGHSGSVRSVAFSP- 256

                        170       180
                 ....*....|....*....|
gi 237820620 365 DSGVFAASGADHQITQWDLA 384
Cdd:COG2319  257 DGRLLASGSADGTVRLWDLA 276
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 257-384 3.17e-22

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: 96.25  E-value: 3.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 257 FVGHTRSVEDLQWSPTENTVfASCSADASIRIWDIraapSKACMLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWD 336
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLL-ATGSGDGTIKVWDL----ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 237820620 337 LrqfKSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADHQITQWDLA 384
Cdd:cd00200   80 L---ETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVE 123
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 202-336 6.00e-18

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: 83.92  E-value: 6.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 202 AQMKPIFSFAGHMGEGFALDWSPRvTGRLLTGDCQKNIHLWTPTDGgsWHVDQrpFVGHTRSVEDLQWSPTENtVFASCS 281
Cdd:cd00200  165 RTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDGTIKLWDLSTG--KCLGT--LRGHENGVNSVAFSPDGY-LLASGS 238

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 237820620 282 ADASIRIWDIRaapSKACMlTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWD 336
Cdd:cd00200  239 EDGTIRVWDLR---TGECV-QTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 300-383 1.22e-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: 65.05  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 300 MLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLrqfKSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADHQIT 379
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL---ETGELLRTLKGHTGPVRDVAASA-DGTYLASGSSDKTIR 76


                 ....
gi 237820620 380 QWDL 383
Cdd:cd00200   77 LWDL 80
WD40 COG2319
WD40 repeat [General function prediction only];
241-384 9.04e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.39  E-value: 9.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 241 LWTPTDGGSWHVDQRPFVGHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPskacmLTTATAHDGDVNVISWSRRE 320
Cdd:COG2319   16 LALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLSVAFSPDG 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237820620 321 PFLLSGGDDGALKIWDLrqfKSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADHQITQWDLA 384
Cdd:COG2319   91 RLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLA 150
PTZ00420 PTZ00420
coronin; Provisional
 259-361 2.87e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 62.27  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 259 GHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPSKA-------CMLttaTAHDGDVNVISWSRREPFLL-SGGDDG 330
Cdd:PTZ00420  72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVkeikdpqCIL---KGHKKKISIIDWNPMNYYIMcSSGFDS 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 237820620 331 ALKIWDLRQFKSGSPVATFKQhvapVTSVEW 361
Cdd:PTZ00420 149 FVNIWDIENEKRAFQINMPKK----LSSLKW 175
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 269-390 1.91e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.63  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 269 WSPTENTVFASCSADASIRIWDIraapSKACMLTTATAHDGDVNVISWSRREPFLL-SGGDDGALKIWDLRQfksGSPVA 347
Cdd:PLN00181 540 WNSYIKSQVASSNFEGVVQVWDV----ARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQ---GVSIG 612

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 237820620 348 TFKQHvAPVTSVEWhPQDSGVFAASG-ADHQITQWDLaveRDPE 390
Cdd:PLN00181 613 TIKTK-ANICCVQF-PSESGRSLAFGsADHKVYYYDL---RNPK 651
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 44-112 2.50e-07

Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved heterotrimeric protein complex that promotes histone H3 and H4 deposition onto newly synthesized DNA during replication or DNA repair; specifically it facilitates replication-dependent nucleosome assembly with the major histone H3 (H3.1). This domain is an alpha helix which sits just upstream of the WD40 seven-bladed beta-propeller in the human RbAp46 protein. RbAp46 folds into the beta-propeller and binds histone H4 in a groove formed between this N-terminal helix and an extended loop inserted into blade six.


Pssm-ID: 463513  Cd Length: 69  Bit Score: 47.57  E-value: 2.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237820620   44 GEELVMDEEAYVLY---HRAQTGAPCLSFDIVRDHLGDNRTelpLTLYLCAGTQAESAQSNRLMMLRMHNLH 112
Cdd:pfam12265   1 EEYLIWKKNAPFLYdmlHTHALEWPSLSFDWFPDTSEGKNY---TVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 257-290 9.84e-07

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: 45.00  E-value: 9.84e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 237820620   257 FVGHTRSVEDLQWSPTeNTVFASCSADASIRIWD 290
Cdd:smart00320   8 LKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 301-336 1.75e-06

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: 44.61  E-value: 1.75e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 237820620   301 LTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWD 336
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 342-382 2.92e-06

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: 43.84  E-value: 2.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 237820620   342 SGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADHQITQWD 382
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
301-336 5.24e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 5.24e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 237820620  301 LTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWD 336
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
257-290 8.73e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 8.73e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 237820620  257 FVGHTRSVEDLQWSPTeNTVFASCSADASIRIWD 290
Cdd:pfam00400   7 LEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
343-382 9.31e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 9.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 237820620  343 GSPVATFKQHVAPVTSVEWHPqDSGVFAASGADHQITQWD 382
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 259-352 5.40e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 39.11  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820620 259 GHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPSKacmlTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLR 338
Cdd:PTZ00421 123 GHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAV----EVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPR 198

                         90
                 ....*....|....
gi 237820620 339 qfkSGSPVATFKQH 352
Cdd:PTZ00421 199 ---DGTIVSSVEAH 209
 
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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