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Conserved domains on  [gi|163937861|ref|NP_700468|]
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glutamate-rich WD repeat-containing protein 1 [Mus musculus]

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 ...
 206-384 5.88e-30

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: 117.82  E-value: 5.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 206 PIFSFAGHMGEGFALDWSPrVPGRLLTGDCQKNVHLWTPTEG---------------------------GS-------WN 251
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasGSsdktirlWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 252 VDQ----RPFVGHTRSVEDLQWSPTeDTVFASCSADASIRIWDIRaaPGKACmlTTATAHDGDVNVISWSRREPFLLSGG 327
Cdd:cd00200   80 LETgecvRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVE--TGKCL--TTLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 163937861 328 DDGALKVWDLRqfkSGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:cd00200  155 QDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP-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 2.81e-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: 2.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163937861   44 GEELVMDEEAYVLY---HRAQTGAPCLSFDIVRDHLGDNrtELPLSLYLCaGTQAESAQSNRLMMLRMHNLH 112
Cdd:pfam12265   1 EEYLIWKKNAPFLYdmlHTHALEWPSLSFDWFPDTSEGK--NYTVQRLLL-GTQTSGAEQNYLYVAKVSLPS 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 ...
 206-384 5.88e-30

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: 117.82  E-value: 5.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 206 PIFSFAGHMGEGFALDWSPrVPGRLLTGDCQKNVHLWTPTEG---------------------------GS-------WN 251
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasGSsdktirlWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 252 VDQ----RPFVGHTRSVEDLQWSPTeDTVFASCSADASIRIWDIRaaPGKACmlTTATAHDGDVNVISWSRREPFLLSGG 327
Cdd:cd00200   80 LETgecvRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVE--TGKCL--TTLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 163937861 328 DDGALKVWDLRqfkSGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:cd00200  155 QDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
139-384 4.63e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 115.01  E-value: 4.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 139 PQLELAMVPHYGGINRVRVSWLGEEPVAGvwSEKGQVEVFALR--RLLQVVDDPQA-------------LAIFLRDEQAR 203
Cdd:COG2319  110 GLLLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLAtgKLLRTLTGHSGavtsvafspdgklLASGSDDGTVR 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 204 I------KPIFSFAGHMGEGFALDWSPRvpGRLL-TGDCQKNVHLWTPTEGGSwnvdQRPFVGHTRSVEDLQWSPTEDTV 276
Cdd:COG2319  188 LwdlatgKLLRTLTGHTGAVRSVAFSPD--GKLLaSGSADGTVRLWDLATGKL----LRTLTGHSGSVRSVAFSPDGRLL 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 277 fASCSADASIRIWDirAAPGKAcmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLrqfKSGSPVATFKQHMAPV 356
Cdd:COG2319  262 -ASGSADGTVRLWD--LATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAV 333

                        250       260
                 ....*....|....*....|....*...
gi 163937861 357 TSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:COG2319  334 RSVAFSP-DGKTLASGSDDGTVRLWDLA 360
PTZ00420 PTZ00420
coronin; Provisional
 259-361 1.28e-09

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 60.35  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 259 GHTRSVEDLQWSPTEDTVFASCSADASIRIWDIR-------AAPGKACMLttaTAHDGDVNVISWSRREPFLL-SGGDDG 330
Cdd:PTZ00420  72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPhndesvkEIKDPQCIL---KGHKKKISIIDWNPMNYYIMcSSGFDS 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 163937861 331 ALKVWDLRQFKSGSPVATFKQhmapVTSVEW 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 2.81e-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: 2.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163937861   44 GEELVMDEEAYVLY---HRAQTGAPCLSFDIVRDHLGDNrtELPLSLYLCaGTQAESAQSNRLMMLRMHNLH 112
Cdd:pfam12265   1 EEYLIWKKNAPFLYdmlHTHALEWPSLSFDWFPDTSEGK--NYTVQRLLL-GTQTSGAEQNYLYVAKVSLPS 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 257-290 1.51e-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: 1.51e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 163937861   257 FVGHTRSVEDLQWSPTeDTVFASCSADASIRIWD 290
Cdd:smart00320   8 LKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
301-336 7.25e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 7.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 163937861  301 LTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWD 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 ...
 206-384 5.88e-30

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: 117.82  E-value: 5.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 206 PIFSFAGHMGEGFALDWSPrVPGRLLTGDCQKNVHLWTPTEG---------------------------GS-------WN 251
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasGSsdktirlWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 252 VDQ----RPFVGHTRSVEDLQWSPTeDTVFASCSADASIRIWDIRaaPGKACmlTTATAHDGDVNVISWSRREPFLLSGG 327
Cdd:cd00200   80 LETgecvRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVE--TGKCL--TTLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 163937861 328 DDGALKVWDLRqfkSGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:cd00200  155 QDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
139-384 4.63e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 115.01  E-value: 4.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 139 PQLELAMVPHYGGINRVRVSWLGEEPVAGvwSEKGQVEVFALR--RLLQVVDDPQA-------------LAIFLRDEQAR 203
Cdd:COG2319  110 GLLLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLAtgKLLRTLTGHSGavtsvafspdgklLASGSDDGTVR 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 204 I------KPIFSFAGHMGEGFALDWSPRvpGRLL-TGDCQKNVHLWTPTEGGSwnvdQRPFVGHTRSVEDLQWSPTEDTV 276
Cdd:COG2319  188 LwdlatgKLLRTLTGHTGAVRSVAFSPD--GKLLaSGSADGTVRLWDLATGKL----LRTLTGHSGSVRSVAFSPDGRLL 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 277 fASCSADASIRIWDirAAPGKAcmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLrqfKSGSPVATFKQHMAPV 356
Cdd:COG2319  262 -ASGSADGTVRLWD--LATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAV 333

                        250       260
                 ....*....|....*....|....*...
gi 163937861 357 TSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:COG2319  334 RSVAFSP-DGKTLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 205-383 1.02e-27

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: 111.66  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 205 KPIFSFAGHMGEGFALDWSPRvpGRLLTGD-CQKNVHLWTPTEGGSwnvdQRPFVGHTRSVEDLQWSPTEDTVfASCSAD 283
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSPD--GRILSSSsRDKTIKVWDVETGKC----LTTLRGHTDWVNSVAFSPDGTFV-ASSSQD 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 284 ASIRIWDIRAAPGKAcmltTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLRqfkSGSPVATFKQHMAPVTSVEWHP 363
Cdd:cd00200  157 GTIKLWDLRTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS---TGKCLGTLRGHENGVNSVAFSP 229

                        170       180
                 ....*....|....*....|
gi 163937861 364 qDSGVFAASGADNQITQWDL 383
Cdd:cd00200  230 -DGYLLASGSEDGTIRVWDL 248
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 198-382 1.58e-27

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: 110.89  E-value: 1.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 198 RDEQARI------KPIFSFAGHMGEGFALDWSPrvPGRLLTGDCQ-KNVHLWtptEGGSWNVDQRpFVGHTRSVEDLQWS 270
Cdd:cd00200  113 RDKTIKVwdvetgKCLTTLRGHTDWVNSVAFSP--DGTFVASSSQdGTIKLW---DLRTGKCVAT-LTGHTGEVNSVAFS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 271 PTEDTvFASCSADASIRIWDIRAapgKACmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLRqfkSGSPVATFK 350
Cdd:cd00200  187 PDGEK-LLSSSSDGTIKLWDLST---GKC-LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR---TGECVQTLS 258

                        170       180       190
                 ....*....|....*....|....*....|..
gi 163937861 351 QHMAPVTSVEWHPqDSGVFAASGADNQITQWD 382
Cdd:cd00200  259 GHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
189-384 1.60e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.39  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 189 DPQALAIFLRDEQARI------KPIFSFAGHMGEGFALDWSPRvpGRLL-TGDCQKNVHLWTPTEGGSWnvdqRPFVGHT 261
Cdd:COG2319  215 DGKLLASGSADGTVRLwdlatgKLLRTLTGHSGSVRSVAFSPD--GRLLaSGSADGTVRLWDLATGELL----RTLTGHS 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 262 RSVEDLQWSPTEDTVfASCSADASIRIWDIraAPGKAcmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLRqfk 341
Cdd:COG2319  289 GGVNSVAFSPDGKLL-ASGSDDGTVRLWDL--ATGKL--LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA--- 360

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 163937861 342 SGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:COG2319  361 TGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
189-384 3.09e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 3.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 189 DPQALAIFLRDEQARI------KPIFSFAGHMGEGFALDWSPRvpG-RLLTGDCQKNVHLWTPTEGGSwnvdQRPFVGHT 261
Cdd:COG2319   89 DGRLLASASADGTVRLwdlatgLLLRTLTGHTGAVRSVAFSPD--GkTLASGSADGTVRLWDLATGKL----LRTLTGHS 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 262 RSVEDLQWSPTEDTVfASCSADASIRIWDIRAapGKAcmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLRqfk 341
Cdd:COG2319  163 GAVTSVAFSPDGKLL-ASGSDDGTVRLWDLAT--GKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA--- 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 163937861 342 SGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:COG2319  235 TGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLA 276
WD40 COG2319
WD40 repeat [General function prediction only];
148-338 2.30e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.42  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 148 HYGGINRVRVS----WL---GEEPVAGVWSEKGQVEVFALRRLLQVVD------DPQALAIFLRDEQARI------KPIF 208
Cdd:COG2319  203 HTGAVRSVAFSpdgkLLasgSADGTVRLWDLATGKLLRTLTGHSGSVRsvafspDGRLLASGSADGTVRLwdlatgELLR 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 209 SFAGHMGEGFALDWSPRvpGRLL-TGDCQKNVHLWTPTEGGSwnvdQRPFVGHTRSVEDLQWSPTEDTVfASCSADASIR 287
Cdd:COG2319  283 TLTGHSGGVNSVAFSPD--GKLLaSGSDDGTVRLWDLATGKL----LRTLTGHTGAVRSVAFSPDGKTL-ASGSDDGTVR 355

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 163937861 288 IWDIRAAPGkacmLTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLR 338
Cdd:COG2319  356 LWDLATGEL----LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
254-384 1.48e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 254 QRPFVGHTRSVEDLQWSPTEDTVFASCSADASIRIWDIRAAPgkacmLTTATAHDGDVNVISWSRREPFLLSGGDDGALK 333
Cdd:COG2319   29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLSVAFSPDGRLLASASADGTVR 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 163937861 334 VWDLrqfKSGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLA 384
Cdd:COG2319  104 LWDL---ATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLA 150
PTZ00420 PTZ00420
coronin; Provisional
 259-361 1.28e-09

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 60.35  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 259 GHTRSVEDLQWSPTEDTVFASCSADASIRIWDIR-------AAPGKACMLttaTAHDGDVNVISWSRREPFLL-SGGDDG 330
Cdd:PTZ00420  72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPhndesvkEIKDPQCIL---KGHKKKISIIDWNPMNYYIMcSSGFDS 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 163937861 331 ALKVWDLRQFKSGSPVATFKQhmapVTSVEW 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 2.81e-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: 2.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163937861   44 GEELVMDEEAYVLY---HRAQTGAPCLSFDIVRDHLGDNrtELPLSLYLCaGTQAESAQSNRLMMLRMHNLH 112
Cdd:pfam12265   1 EEYLIWKKNAPFLYdmlHTHALEWPSLSFDWFPDTSEGK--NYTVQRLLL-GTQTSGAEQNYLYVAKVSLPS 69
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 269-390 3.50e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.78  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 269 WSPTEDTVFASCSADASIRIWDIraapGKACMLTTATAHDGDVNVISWSRREPFLL-SGGDDGALKVWDLRQfksGSPVA 347
Cdd:PLN00181 540 WNSYIKSQVASSNFEGVVQVWDV----ARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQ---GVSIG 612

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 163937861 348 TFKQHmAPVTSVEWhPQDSGVFAASG-ADNQITQWDLaveRDPE 390
Cdd:PLN00181 613 TIKTK-ANICCVQF-PSESGRSLAFGsADHKVYYYDL---RNPK 651
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 257-290 1.51e-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: 1.51e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 163937861   257 FVGHTRSVEDLQWSPTeDTVFASCSADASIRIWD 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 2.95e-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: 2.95e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 163937861   301 LTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWD 336
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 342-382 3.52e-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: 43.46  E-value: 3.52e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 163937861   342 SGSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWD 382
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
301-336 7.25e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 7.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 163937861  301 LTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWD 336
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
257-290 1.21e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 163937861  257 FVGHTRSVEDLQWSPTeDTVFASCSADASIRIWD 290
Cdd:pfam00400   7 LEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
343-382 9.22e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 9.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 163937861  343 GSPVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWD 382
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 212-416 5.53e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.19  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 212 GHMGEGFALDWSPRVPGRLLTGDCQKNVHLW-TPTEGGSWNVDQrPFV---GHTRSVEDLQWSPTEDTVFASCSADASIR 287
Cdd:PTZ00421  73 GQEGPIIDVAFNPFDPQKLFTASEDGTIMGWgIPEEGLTQNISD-PIVhlqGHTKKVGIVSFHPSAMNVLASAGADMVVN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 288 IWDIRAAPGKACM-----------------LTTATAHDGDVNVIS----------------------WSRREPFLLSGGD 328
Cdd:PTZ00421 152 VWDVERGKAVEVIkchsdqitslewnldgsLLCTTSKDKKLNIIDprdgtivssveahasaksqrclWAKRKDLIITLGC 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163937861 329 DGA----LKVWDLRqfKSGSPVATFKQHMAPVTSVEWHPQDSGVF-AASGADNQITQWDLAVER-DPESGETETDP--GL 400
Cdd:PTZ00421 232 SKSqqrqIMLWDTR--KMASPYSTVDLDQSSALFIPFFDEDTNLLyIGSKGEGNIRCFELMNERlTFCSSYSSVEPhkGL 309

                        250
                 ....*....|....*.
gi 163937861 401 AALPQQLLFVHQGETD 416
Cdd:PTZ00421 310 CMMPKWSLDTRKCEIA 325
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 345-398 6.75e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.55  E-value: 6.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163937861 345 PVATFKQHMAPVTSVEWHPqDSGVFAASGADNQITQWDLAVERDPESGETETDP 398
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGP 53
 
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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