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Conserved domains on  [gi|17508127|ref|NP_492552|]
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putative histone-binding protein lin-53 [Caenorhabditis elegans]

Protein Classification

WD repeat RBAP46/RBAP48/MSI1 family protein( domain architecture ID 12115235)

WD repeat RBAP46/RBAP48/MSI1 family protein binds histones, similar to human histone-binding proteins RBBP4 and RBBP7

CATH:  2.130.10.10
Gene Ontology:  GO:0005515|GO:0042393
SCOP:  4005630|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];
107-398 1.90e-40

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.52  E-value: 1.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 107 VNGKVEPDIRINHEGEVNRARYMPQkSNIIATKSPHADVYIFDylkhsavprDNTFNPLIRLKGHTKEGYGLSWNPNKEg 186
Cdd:COG2319 107 LATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWD---------LATGKLLRTLTGHSGAVTSVAFSPDGK- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 187 LILSASDDQTVCHWDINANQNVAgelqakdVFKGHESVVEDVAWHvlHDG-VFGSVGDDKKLLIWDVRTSTPGHCIDAHS 265
Cdd:COG2319 176 LLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFS--PDGkLLASGSADGTVRLWDLATGKLLRTLTGHS 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 266 AEVNCLAFNPYSEfILATGSADKTVALWDLRNLRMkLHSFESHRDEIFQVQWSPhNETILASSGTDKRLHVWDLSKiged 345
Cdd:COG2319 247 GSVRSVAFSPDGR-LLASGSADGTVRLWDLATGEL-LRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT---- 319
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508127 346 qsaedaedgpPELLFIHGGHTAKISDFSWNPNEPWVVcSVSEDNILQVWQMAD 398
Cdd:COG2319 320 ----------GKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDLAT 361
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
16-84 3.11e-31

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: 113.83  E-value: 3.11e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127    16 DEYKIWKKNTPFLYDLVMTHALEWPSLSVQWLPDVaKDNSDHTIHRLILGTHTSD-EQNHLLISKICMPT 84
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDT-SEGKNYTVQRLLLGTQTSGaEQNYLYVAKVSLPS 69
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
107-398 1.90e-40

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.52  E-value: 1.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 107 VNGKVEPDIRINHEGEVNRARYMPQkSNIIATKSPHADVYIFDylkhsavprDNTFNPLIRLKGHTKEGYGLSWNPNKEg 186
Cdd:COG2319 107 LATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWD---------LATGKLLRTLTGHSGAVTSVAFSPDGK- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 187 LILSASDDQTVCHWDINANQNVAgelqakdVFKGHESVVEDVAWHvlHDG-VFGSVGDDKKLLIWDVRTSTPGHCIDAHS 265
Cdd:COG2319 176 LLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFS--PDGkLLASGSADGTVRLWDLATGKLLRTLTGHS 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 266 AEVNCLAFNPYSEfILATGSADKTVALWDLRNLRMkLHSFESHRDEIFQVQWSPhNETILASSGTDKRLHVWDLSKiged 345
Cdd:COG2319 247 GSVRSVAFSPDGR-LLASGSADGTVRLWDLATGEL-LRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT---- 319
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508127 346 qsaedaedgpPELLFIHGGHTAKISDFSWNPNEPWVVcSVSEDNILQVWQMAD 398
Cdd:COG2319 320 ----------GKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
118-395 6.65e-40

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: 144.01  E-value: 6.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 118 NHEGEVNRARYMPQKSNIIATKSPHAdVYIFDYlkhsavprdNTFNPLIRLKGHTKEGYGLSWNPNKEgLILSASDDQTV 197
Cdd:cd00200  49 GHTGPVRDVAASADGTYLASGSSDKT-IRLWDL---------ETGECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 198 CHWDINANQNVAgelqakdVFKGHESVVEDVAWHvlHDGVFGSVG-DDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPy 276
Cdd:cd00200 118 KVWDVETGKCLT-------TLRGHTDWVNSVAFS--PDGTFVASSsQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSP- 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 277 SEFILATGSADKTVALWDLRNLRmKLHSFESHRDEIFQVQWSPHNEtILASSGTDKRLHVWDLSKIGEDQSAEdaedgpp 356
Cdd:cd00200 188 DGEKLLSSSSDGTIKLWDLSTGK-CLGTLRGHENGVNSVAFSPDGY-LLASGSEDGTIRVWDLRTGECVQTLS------- 258
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17508127 357 ellfihgGHTAKISDFSWNPNEPWvVCSVSEDNILQVWQ 395
Cdd:cd00200 259 -------GHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
16-84 3.11e-31

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: 113.83  E-value: 3.11e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127    16 DEYKIWKKNTPFLYDLVMTHALEWPSLSVQWLPDVaKDNSDHTIHRLILGTHTSD-EQNHLLISKICMPT 84
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDT-SEGKNYTVQRLLLGTQTSGaEQNYLYVAKVSLPS 69
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
164-340 1.93e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 68.96  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  164 PLIRLKGHTKEGyGLSWNPNKEGLILSASDDQTVCHWDINANQNVAGelqakdvFKGHESVVEDVAWHVLHDGVFGSVGD 243
Cdd:PLN00181 525 PVVELASRSKLS-GICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE-------MKEHEKRVWSIDYSSADPTLLASGSD 596
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  244 DKKLLIWDVRTSTPGHCIDAhSAEVNCLAFNPYSEFILATGSADKTVALWDLRNLRMKLHSFESHRDEIFQVQWSphNET 323
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKT-KANICCVQFPSESGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFV--DSS 673
                        170
                 ....*....|....*..
gi 17508127  324 ILASSGTDKRLHVWDLS 340
Cdd:PLN00181 674 TLVSSSTDNTLKLWDLS 690
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
254-294 1.72e-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: 44.23  E-value: 1.72e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 17508127    254 TSTPGHCIDAHSAEVNCLAFNPYSEFiLATGSADKTVALWD 294
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKY-LASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
255-294 8.66e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 8.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 17508127   255 STPGHCIDAHSAEVNCLAFNPYSEFiLATGSADKTVALWD 294
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKL-LASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
107-398 1.90e-40

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.52  E-value: 1.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 107 VNGKVEPDIRINHEGEVNRARYMPQkSNIIATKSPHADVYIFDylkhsavprDNTFNPLIRLKGHTKEGYGLSWNPNKEg 186
Cdd:COG2319 107 LATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWD---------LATGKLLRTLTGHSGAVTSVAFSPDGK- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 187 LILSASDDQTVCHWDINANQNVAgelqakdVFKGHESVVEDVAWHvlHDG-VFGSVGDDKKLLIWDVRTSTPGHCIDAHS 265
Cdd:COG2319 176 LLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFS--PDGkLLASGSADGTVRLWDLATGKLLRTLTGHS 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 266 AEVNCLAFNPYSEfILATGSADKTVALWDLRNLRMkLHSFESHRDEIFQVQWSPhNETILASSGTDKRLHVWDLSKiged 345
Cdd:COG2319 247 GSVRSVAFSPDGR-LLASGSADGTVRLWDLATGEL-LRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT---- 319
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508127 346 qsaedaedgpPELLFIHGGHTAKISDFSWNPNEPWVVcSVSEDNILQVWQMAD 398
Cdd:COG2319 320 ----------GKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
118-395 6.65e-40

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: 144.01  E-value: 6.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 118 NHEGEVNRARYMPQKSNIIATKSPHAdVYIFDYlkhsavprdNTFNPLIRLKGHTKEGYGLSWNPNKEgLILSASDDQTV 197
Cdd:cd00200  49 GHTGPVRDVAASADGTYLASGSSDKT-IRLWDL---------ETGECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 198 CHWDINANQNVAgelqakdVFKGHESVVEDVAWHvlHDGVFGSVG-DDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPy 276
Cdd:cd00200 118 KVWDVETGKCLT-------TLRGHTDWVNSVAFS--PDGTFVASSsQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSP- 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 277 SEFILATGSADKTVALWDLRNLRmKLHSFESHRDEIFQVQWSPHNEtILASSGTDKRLHVWDLSKIGEDQSAEdaedgpp 356
Cdd:cd00200 188 DGEKLLSSSSDGTIKLWDLSTGK-CLGTLRGHENGVNSVAFSPDGY-LLASGSEDGTIRVWDLRTGECVQTLS------- 258
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17508127 357 ellfihgGHTAKISDFSWNPNEPWvVCSVSEDNILQVWQ 395
Cdd:cd00200 259 -------GHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
119-396 2.75e-38

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: 139.78  E-value: 2.75e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 119 HEGEVNRARYMPQkSNIIATKSPHADVYIFDYlkhsavprdNTFNPLIRLKGHTKEGYGLSWNPNKEgLILSASDDQTVC 198
Cdd:cd00200   8 HTGGVTCVAFSPD-GKLLATGSGDGTIKVWDL---------ETGELLRTLKGHTGPVRDVAASADGT-YLASGSSDKTIR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 199 HWDINANQNVAgelqakdVFKGHESVVEDVAWHVLHDGVFGSvGDDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPYSE 278
Cdd:cd00200  77 LWDLETGECVR-------TLTGHTSYVSSVAFSPDGRILSSS-SRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 279 FIlATGSADKTVALWDLRNLRmKLHSFESHRDEIFQVQWSPHNETILASSGtDKRLHVWDLSKigedqsaedaedgpPEL 358
Cdd:cd00200 149 FV-ASSSQDGTIKLWDLRTGK-CVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLST--------------GKC 211
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17508127 359 LFIHGGHTAKISDFSWNPNEPWvVCSVSEDNILQVWQM 396
Cdd:cd00200 212 LGTLRGHENGVNSVAFSPDGYL-LASGSEDGTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
119-398 5.08e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.97  E-value: 5.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 119 HEGEVNRARYMPQkSNIIATKSPHADVYIFDYLkhsavprdnTFNPLIRLKGHTKEGYGLSWNPNKEgLILSASDDQTVC 198
Cdd:COG2319 161 HSGAVTSVAFSPD-GKLLASGSDDGTVRLWDLA---------TGKLLRTLTGHTGAVRSVAFSPDGK-LLASGSADGTVR 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 199 HWDINANQNVAgelqakdVFKGHESVVEDVAWHvlHDG-VFGSVGDDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPYS 277
Cdd:COG2319 230 LWDLATGKLLR-------TLTGHSGSVRSVAFS--PDGrLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDG 300
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 278 EFiLATGSADKTVALWDLRNLRmKLHSFESHRDEIFQVQWSPhNETILASSGTDKRLHVWDLSKigedqsaedaedgpPE 357
Cdd:COG2319 301 KL-LASGSDDGTVRLWDLATGK-LLRTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLAT--------------GE 363
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17508127 358 LLFIHGGHTAKISDFSWNPNEPWVVcSVSEDNILQVWQMAD 398
Cdd:COG2319 364 LLRTLTGHTGAVTSVAFSPDGRTLA-SGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
168-398 2.50e-32

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: 123.60  E-value: 2.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 168 LKGHTKEGYGLSWNPNKEgLILSASDDQTVCHWDINANQnvagelqAKDVFKGHESVVEDVAWhVLHDGVFGSVGDDKKL 247
Cdd:cd00200   5 LKGHTGGVTCVAFSPDGK-LLATGSGDGTIKVWDLETGE-------LLRTLKGHTGPVRDVAA-SADGTYLASGSSDKTI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 248 LIWDVRTSTPGHCIDAHSAEVNCLAFNPySEFILATGSADKTVALWDLRNlRMKLHSFESHRDEIFQVQWSPHNeTILAS 327
Cdd:cd00200  76 RLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDWVNSVAFSPDG-TFVAS 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17508127 328 SGTDKRLHVWDLSKIGEDQSAEdaedgppellfihgGHTAKISDFSWNPNEPWVVCSvSEDNILQVWQMAD 398
Cdd:cd00200 153 SSQDGTIKLWDLRTGKCVATLT--------------GHTGEVNSVAFSPDGEKLLSS-SSDGTIKLWDLST 208
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
16-84 3.11e-31

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: 113.83  E-value: 3.11e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127    16 DEYKIWKKNTPFLYDLVMTHALEWPSLSVQWLPDVaKDNSDHTIHRLILGTHTSD-EQNHLLISKICMPT 84
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDT-SEGKNYTVQRLLLGTQTSGaEQNYLYVAKVSLPS 69
WD40 COG2319
WD40 repeat [General function prediction only];
155-398 5.70e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.76  E-value: 5.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 155 AVPRDNTFNPLIRLKGHTKEGYGLSWNPNkEGLILSASDDQTVCHWDinanqnvAGELQAKDVFKGHESVVEDVAWHVLh 234
Cdd:COG2319  19 ALLAAALGALLLLLLGLAAAVASLAASPD-GARLAAGAGDLTLLLLD-------AAAGALLATLLGHTAAVLSVAFSPD- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 235 DGVFGSVGDDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPySEFILATGSADKTVALWDLRNLRmKLHSFESHRDEIFQ 314
Cdd:COG2319  90 GRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGK-LLRTLTGHSGAVTS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 315 VQWSPhNETILASSGTDKRLHVWDLSKigedqsaedaedgpPELLFIHGGHTAKISDFSWNPNEPWVVcSVSEDNILQVW 394
Cdd:COG2319 168 VAFSP-DGKLLASGSDDGTVRLWDLAT--------------GKLLRTLTGHTGAVRSVAFSPDGKLLA-SGSADGTVRLW 231

                ....
gi 17508127 395 QMAD 398
Cdd:COG2319 232 DLAT 235
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
215-397 9.69e-25

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: 102.80  E-value: 9.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 215 KDVFKGHESVVEDVAWHVLHDgVFGSVGDDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPYSEFiLATGSADKTVALWD 294
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGK-LLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTY-LASGSSDKTIRLWD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 295 LRNLRMkLHSFESHRDEIFQVQWSPHNeTILASSGTDKRLHVWDLSKigedqsaedaedgpPELLFIHGGHTAKISDFSW 374
Cdd:cd00200  80 LETGEC-VRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVET--------------GKCLTTLRGHTDWVNSVAF 143
                       170       180
                ....*....|....*....|...
gi 17508127 375 NPNePWVVCSVSEDNILQVWQMA 397
Cdd:cd00200 144 SPD-GTFVASSSQDGTIKLWDLR 165
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
259-399 7.45e-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: 88.93  E-value: 7.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127 259 HCIDAHSAEVNCLAFNPYSEFiLATGSADKTVALWDLRNLRmKLHSFESHRDEIFQVQWSPHNETiLASSGTDKRLHVWD 338
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKL-LATGSGDGTIKVWDLETGE-LLRTLKGHTGPVRDVAASADGTY-LASGSSDKTIRLWD 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17508127 339 LSKigedqsaedaedgpPELLFIHGGHTAKISDFSWNPNEPWVVCSvSEDNILQVWQMADN 399
Cdd:cd00200  80 LET--------------GECVRTLTGHTSYVSSVAFSPDGRILSSS-SRDKTIKVWDVETG 125
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
164-340 1.93e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 68.96  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  164 PLIRLKGHTKEGyGLSWNPNKEGLILSASDDQTVCHWDINANQNVAGelqakdvFKGHESVVEDVAWHVLHDGVFGSVGD 243
Cdd:PLN00181 525 PVVELASRSKLS-GICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE-------MKEHEKRVWSIDYSSADPTLLASGSD 596
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  244 DKKLLIWDVRTSTPGHCIDAhSAEVNCLAFNPYSEFILATGSADKTVALWDLRNLRMKLHSFESHRDEIFQVQWSphNET 323
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKT-KANICCVQFPSESGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFV--DSS 673
                        170
                 ....*....|....*..
gi 17508127  324 ILASSGTDKRLHVWDLS 340
Cdd:PLN00181 674 TLVSSSTDNTLKLWDLS 690
PTZ00421 PTZ00421
coronin; Provisional
113-298 8.96e-09

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 57.21  E-value: 8.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  113 PDIRINHEGEVNRARYMPQKSNIIATKSphADVYIFDYlkhsAVPRD----NTFNPLIRLKGHTKEGYGLSWNPNKEGLI 188
Cdd:PTZ00421  68 PPILLGQEGPIIDVAFNPFDPQKLFTAS--EDGTIMGW----GIPEEgltqNISDPIVHLQGHTKKVGIVSFHPSAMNVL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  189 LSASDDQTVCHWDINANqnvagelQAKDVFKGHESVVEDVAWHvLHDGVFGSVGDDKKLLIWDVRTSTPGHCIDAH-SAE 267
Cdd:PTZ00421 142 ASAGADMVVNVWDVERG-------KAVEVIKCHSDQITSLEWN-LDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHaSAK 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 17508127  268 VNCLAFNPYSEFILATG---SADKTVALWDLRNL 298
Cdd:PTZ00421 214 SQRCLWAKRKDLIITLGcskSQQRQIMLWDTRKM 247
PTZ00420 PTZ00420
coronin; Provisional
305-403 3.95e-08

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 55.34  E-value: 3.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  305 FESHRDEIFQVQWSPHNETILASSGTDKRLHVWDLSKigEDQSAEDAEDGppelLFIHGGHTAKISDFSWNPNEPWVVCS 384
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPH--NDESVKEIKDP----QCILKGHKKKISIIDWNPMNYYIMCS 143
                         90
                 ....*....|....*....
gi 17508127  385 VSEDNILQVWqmadNIYNE 403
Cdd:PTZ00420 144 SGFDSFVNIW----DIENE 158
PTZ00420 PTZ00420
coronin; Provisional
164-252 8.33e-08

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 54.19  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  164 PLIRLKGHTKEGYGLSWNPNKEGLILSASDDQTVCHWDINANQNVAGELqaKD---VFKGHESVVEDVAWHVLHDGVFGS 240
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVKEI--KDpqcILKGHKKKISIIDWNPMNYYIMCS 143
                         90
                 ....*....|..
gi 17508127  241 VGDDKKLLIWDV 252
Cdd:PTZ00420 144 SGFDSFVNIWDI 155
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
254-294 1.72e-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: 44.23  E-value: 1.72e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 17508127    254 TSTPGHCIDAHSAEVNCLAFNPYSEFiLATGSADKTVALWD 294
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKY-LASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
255-294 8.66e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 8.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 17508127   255 STPGHCIDAHSAEVNCLAFNPYSEFiLATGSADKTVALWD 294
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKL-LASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
302-338 3.99e-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: 3.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 17508127    302 LHSFESHRDEIFQVQWSPHNeTILASSGTDKRLHVWD 338
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
161-201 7.55e-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: 39.60  E-value: 7.55e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 17508127    161 TFNPLIRLKGHTKEGYGLSWNPNKEgLILSASDDQTVCHWD 201
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGK-YLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
271-393 3.20e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.96  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  271 LAFNPYSEFILATGSADKTVALWDL------RNLRMKLHSFESHRDEIFQVQWSPHNETILASSGTDKRLHVWDLSK--I 342
Cdd:PTZ00421  81 VAFNPFDPQKLFTASEDGTIMGWGIpeegltQNISDPIVHLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERgkA 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17508127  343 GEDQSAedaedgppellfihggHTAKISDFSWNPNEPwVVCSVSEDNILQV 393
Cdd:PTZ00421 161 VEVIKC----------------HSDQITSLEWNLDGS-LLCTTSKDKKLNI 194
WD40 pfam00400
WD domain, G-beta repeat;
302-338 4.41e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 4.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17508127   302 LHSFESHRDEIFQVQWSPhNETILASSGTDKRLHVWD 338
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
113-297 1.09e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.09  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  113 PDIRI-NHEGEVNRARYMPQKSNIIATKSPHADVYIFDyLKHSAVPRDNTFNPLIRLKGHTKEGYGLSWNPNKEGLILSA 191
Cdd:PTZ00420  66 PVIKLkGHTSSILDLQFNPCFSEILASGSEDLTIRVWE-IPHNDESVKEIKDPQCILKGHKKKISIIDWNPMNYYIMCSS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508127  192 SDDQTVCHWDINaNQNVAGELQAKdvfKGHESVVEDVAWHVLHDGVFGS---VGDDKK------LLIWDVRTSTPGHCID 262
Cdd:PTZ00420 145 GFDSFVNIWDIE-NEKRAFQINMP---KKLSSLKWNIKGNLLSGTCVGKhmhIIDPRKqeiassFHIHDGGKNTKNIWID 220
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 17508127  263 AHSAEVNClafnpysefILATGSAD---KTVALWDLRN 297
Cdd:PTZ00420 221 GLGGDDNY---------ILSTGFSKnnmREMKLWDLKN 249
WD40 pfam00400
WD domain, G-beta repeat;
162-201 1.32e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 17508127   162 FNPLIRLKGHTKEGYGLSWNPNKEgLILSASDDQTVCHWD 201
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
355-394 5.10e-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: 34.60  E-value: 5.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 17508127    355 PPELLFIHGGHTAKISDFSWNPNEPWVVcSVSEDNILQVW 394
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLA-SGSDDGTIKLW 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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