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Conserved domains on  [gi|58865700|ref|NP_001012067|]
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glutamate-rich WD repeat-containing protein 1 [Rattus norvegicus]

Protein Classification

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

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

Gene Ontology:  GO:0005515|GO:0042393
PubMed:  10322433

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 ...
 205-383 9.86e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 122.44  E-value: 9.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 205 PIFSFAGHMGEGFALDWSPrVPGRLLTGDCQKNIHLWTPTDG---------------------------GS-------WN 250
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasGSsdktirlWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 251 VDQ----RPFVGHTRSVEDLQWSPTeDTVFASCSADASIRIWDIRaaPGKACmlTTAAAHDGDVNVISWSRREPFLLSGG 326
Cdd:cd00200  80 LETgecvRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVE--TGKCL--TTLRGHTDWVNSVAFSPDGTFVASSS 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 58865700 327 DDGTLKVWDLRqfkSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLA 383
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 2.80e-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: 2.80e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58865700    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 ...
 205-383 9.86e-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: 122.44  E-value: 9.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 205 PIFSFAGHMGEGFALDWSPrVPGRLLTGDCQKNIHLWTPTDG---------------------------GS-------WN 250
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasGSsdktirlWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 251 VDQ----RPFVGHTRSVEDLQWSPTeDTVFASCSADASIRIWDIRaaPGKACmlTTAAAHDGDVNVISWSRREPFLLSGG 326
Cdd:cd00200  80 LETgecvRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVE--TGKCL--TTLRGHTDWVNSVAFSPDGTFVASSS 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 58865700 327 DDGTLKVWDLRqfkSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:cd00200 155 QDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
138-383 3.87e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.09  E-value: 3.87e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 138 PQLELAMVPHYGGINRVRVSWLGEEPVAGvwSEKGQVEVFALR--RLLQVVDDPQA-------------LAIFLRDEQAR 202
Cdd:COG2319 110 GLLLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLAtgKLLRTLTGHSGavtsvafspdgklLASGSDDGTVR 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 203 V------KPIFSFAGHMGEGFALDWSPRvpGRLL-TGDCQKNIHLWTPTDGGSwnvdQRPFVGHTRSVEDLQWSPTEDTV 275
Cdd:COG2319 188 LwdlatgKLLRTLTGHTGAVRSVAFSPD--GKLLaSGSADGTVRLWDLATGKL----LRTLTGHSGSVRSVAFSPDGRLL 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 276 fASCSADASIRIWDirAAPGKAcmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLrqfKSGSPVATFKQHVAPV 355
Cdd:COG2319 262 -ASGSADGTVRLWD--LATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAV 333

                       250       260
                ....*....|....*....|....*...
gi 58865700 356 TSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:COG2319 334 RSVAFSP-DGKTLASGSDDGTVRLWDLA 360
PTZ00420 PTZ00420
coronin; Provisional
 258-360 1.19e-09

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 60.35  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700  258 GHTRSVEDLQWSPTEDTVFASCSADASIRIWDIR-------AAPGKACMLTtaaAHDGDVNVISWSRREPFLL-SGGDDG 329
Cdd:PTZ00420  72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPhndesvkEIKDPQCILK---GHKKKISIIDWNPMNYYIMcSSGFDS 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 58865700  330 TLKVWDLRQFKSGSPVATFKQhvapVTSVEW 360
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 2.80e-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: 2.80e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58865700    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 ...
 300-335 4.61e-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: 46.15  E-value: 4.61e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 58865700    300 LTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWD 335
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
300-335 1.40e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 1.40e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 58865700   300 LTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWD 335
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 ...
 205-383 9.86e-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: 122.44  E-value: 9.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 205 PIFSFAGHMGEGFALDWSPrVPGRLLTGDCQKNIHLWTPTDG---------------------------GS-------WN 250
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasGSsdktirlWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 251 VDQ----RPFVGHTRSVEDLQWSPTeDTVFASCSADASIRIWDIRaaPGKACmlTTAAAHDGDVNVISWSRREPFLLSGG 326
Cdd:cd00200  80 LETgecvRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVE--TGKCL--TTLRGHTDWVNSVAFSPDGTFVASSS 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 58865700 327 DDGTLKVWDLRqfkSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:cd00200 155 QDGTIKLWDLR---TGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLS 207
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 197-381 3.85e-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: 115.51  E-value: 3.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 197 RDEQARV------KPIFSFAGHMGEGFALDWSPrvPGRLLTGDCQ-KNIHLWtptDGGSWNVDQRpFVGHTRSVEDLQWS 269
Cdd:cd00200 113 RDKTIKVwdvetgKCLTTLRGHTDWVNSVAFSP--DGTFVASSSQdGTIKLW---DLRTGKCVAT-LTGHTGEVNSVAFS 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 270 PTEDTvFASCSADASIRIWDIRAapgKACmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLRqfkSGSPVATFK 349
Cdd:cd00200 187 PDGEK-LLSSSSDGTIKLWDLST---GKC-LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR---TGECVQTLS 258

                       170       180       190
                ....*....|....*....|....*....|..
gi 58865700 350 QHVAPVTSVEWHPqDSGVFAASGADNQITQWD 381
Cdd:cd00200 259 GHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
138-383 3.87e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.09  E-value: 3.87e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 138 PQLELAMVPHYGGINRVRVSWLGEEPVAGvwSEKGQVEVFALR--RLLQVVDDPQA-------------LAIFLRDEQAR 202
Cdd:COG2319 110 GLLLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLAtgKLLRTLTGHSGavtsvafspdgklLASGSDDGTVR 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 203 V------KPIFSFAGHMGEGFALDWSPRvpGRLL-TGDCQKNIHLWTPTDGGSwnvdQRPFVGHTRSVEDLQWSPTEDTV 275
Cdd:COG2319 188 LwdlatgKLLRTLTGHTGAVRSVAFSPD--GKLLaSGSADGTVRLWDLATGKL----LRTLTGHSGSVRSVAFSPDGRLL 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 276 fASCSADASIRIWDirAAPGKAcmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLrqfKSGSPVATFKQHVAPV 355
Cdd:COG2319 262 -ASGSADGTVRLWD--LATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAV 333

                       250       260
                ....*....|....*....|....*...
gi 58865700 356 TSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:COG2319 334 RSVAFSP-DGKTLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 204-382 5.05e-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: 115.12  E-value: 5.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 204 KPIFSFAGHMGEGFALDWSPRvpGRLLTGD-CQKNIHLWTPTDGGSwnvdQRPFVGHTRSVEDLQWSPTEDTVfASCSAD 282
Cdd:cd00200  84 ECVRTLTGHTSYVSSVAFSPD--GRILSSSsRDKTIKVWDVETGKC----LTTLRGHTDWVNSVAFSPDGTFV-ASSSQD 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 283 ASIRIWDIRAAPGKAcmltTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLRqfkSGSPVATFKQHVAPVTSVEWHP 362
Cdd:cd00200 157 GTIKLWDLRTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS---TGKCLGTLRGHENGVNSVAFSP 229

                       170       180
                ....*....|....*....|
gi 58865700 363 qDSGVFAASGADNQITQWDL 382
Cdd:cd00200 230 -DGYLLASGSEDGTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
188-383 1.93e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.08  E-value: 1.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 188 DPQALAIFLRDEQARV------KPIFSFAGHMGEGFALDWSPRvpGRLL-TGDCQKNIHLWTPTDGGSWnvdqRPFVGHT 260
Cdd:COG2319 215 DGKLLASGSADGTVRLwdlatgKLLRTLTGHSGSVRSVAFSPD--GRLLaSGSADGTVRLWDLATGELL----RTLTGHS 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 261 RSVEDLQWSPTEDTVfASCSADASIRIWDIraAPGKAcmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLRqfk 340
Cdd:COG2319 289 GGVNSVAFSPDGKLL-ASGSDDGTVRLWDL--ATGKL--LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA--- 360

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 58865700 341 SGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:COG2319 361 TGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
188-383 4.47e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.93  E-value: 4.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 188 DPQALAIFLRDEQARV------KPIFSFAGHMGEGFALDWSPRvpG-RLLTGDCQKNIHLWTPTDGGSwnvdQRPFVGHT 260
Cdd:COG2319  89 DGRLLASASADGTVRLwdlatgLLLRTLTGHTGAVRSVAFSPD--GkTLASGSADGTVRLWDLATGKL----LRTLTGHS 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 261 RSVEDLQWSPTEDTVfASCSADASIRIWDIRAapGKAcmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLRqfk 340
Cdd:COG2319 163 GAVTSVAFSPDGKLL-ASGSDDGTVRLWDLAT--GKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA--- 234

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 58865700 341 SGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:COG2319 235 TGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLA 276
WD40 COG2319
WD40 repeat [General function prediction only];
147-337 8.46e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.96  E-value: 8.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 147 HYGGINRVRVS----WL---GEEPVAGVWSEKGQVEVFALRRLLQVVD------DPQALAIFLRDEQARV------KPIF 207
Cdd:COG2319 203 HTGAVRSVAFSpdgkLLasgSADGTVRLWDLATGKLLRTLTGHSGSVRsvafspDGRLLASGSADGTVRLwdlatgELLR 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 208 SFAGHMGEGFALDWSPRvpGRLL-TGDCQKNIHLWTPTDGGSwnvdQRPFVGHTRSVEDLQWSPTEDTVfASCSADASIR 286
Cdd:COG2319 283 TLTGHSGGVNSVAFSPD--GKLLaSGSDDGTVRLWDLATGKL----LRTLTGHTGAVRSVAFSPDGKTL-ASGSDDGTVR 355

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 58865700 287 IWDIRAAPGkacmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLR 337
Cdd:COG2319 356 LWDLATGEL----LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 188-335 2.32e-17

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: 82.00  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 188 DPQALAIFLRDEQARV------KPIFSFAGHMGEGFALDWSPRvPGRLLTGDCQKNIHLWTPTDGgsWNVDQrpFVGHTR 261
Cdd:cd00200 146 DGTFVASSSQDGTIKLwdlrtgKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDGTIKLWDLSTG--KCLGT--LRGHEN 220

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865700 262 SVEDLQWSPTEDtVFASCSADASIRIWDIRAapgKACMlTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWD 335
Cdd:cd00200 221 GVNSVAFSPDGY-LLASGSEDGTIRVWDLRT---GECV-QTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
240-383 4.73e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 64.16  E-value: 4.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700 240 LWTPTDGGSWNVDQRPFVGHTRSVEDLQWSPTEDTVFASCSADASIRIWDIRAAPgkacmLTTAAAHDGDVNVISWSRRE 319
Cdd:COG2319  16 LALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLSVAFSPDG 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865700 320 PFLLSGGDDGTLKVWDLrqfKSGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLA 383
Cdd:COG2319  91 RLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLA 150
PTZ00420 PTZ00420
coronin; Provisional
 258-360 1.19e-09

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 60.35  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700  258 GHTRSVEDLQWSPTEDTVFASCSADASIRIWDIR-------AAPGKACMLTtaaAHDGDVNVISWSRREPFLL-SGGDDG 329
Cdd:PTZ00420  72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPhndesvkEIKDPQCILK---GHKKKISIIDWNPMNYYIMcSSGFDS 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 58865700  330 TLKVWDLRQFKSGSPVATFKQhvapVTSVEW 360
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 2.80e-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: 2.80e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58865700    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 ...
 300-335 4.61e-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: 46.15  E-value: 4.61e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 58865700    300 LTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWD 335
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
300-335 1.40e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 1.40e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 58865700   300 LTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWD 335
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 256-289 1.54e-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: 1.54e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 58865700    256 FVGHTRSVEDLQWSPTeDTVFASCSADASIRIWD 289
Cdd:smart00320   8 LKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 341-381 3.15e-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: 3.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 58865700    341 SGSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWD 381
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
256-289 1.25e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 58865700   256 FVGHTRSVEDLQWSPTeDTVFASCSADASIRIWD 289
Cdd:pfam00400   7 LEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 268-395 2.12e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.00  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700  268 WSPTEDTVFASCSADASIRIWDIraapGKACMLTTAAAHDGDVNVISWSRREPFLL-SGGDDGTLKVWDLR--------- 337
Cdd:PLN00181 540 WNSYIKSQVASSNFEGVVQVWDV----ARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINqgvsigtik 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700  338 --------QFKSGS-----------------------PVATFKQHVAPVTSVEWhpQDSGVFAASGADNQITQWDLAVEr 386
Cdd:PLN00181 616 tkaniccvQFPSESgrslafgsadhkvyyydlrnpklPLCTMIGHSKTVSYVRF--VDSSTLVSSSTDNTLKLWDLSMS- 692


                 ....*....
gi 58865700  387 dpESGETET 395
Cdd:PLN00181 693 --ISGINET 699
WD40 pfam00400
WD domain, G-beta repeat;
342-381 8.85e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 8.85e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 58865700   342 GSPVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWD 381
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 193-351 3.69e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.57  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700  193 AIFLRDEQARVK---PIFsfAGHMGEGFALDWSPRVPGRLLTGDCQKNIHLW-TPTDGGSWNVDQrPFV---GHTRSVED 265
Cdd:PTZ00421  54 AVLKHTDYGKLAsnpPIL--LGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWgIPEEGLTQNISD-PIVhlqGHTKKVGI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700  266 LQWSPTEDTVFASCSADASIRIWDIRAapGKAcmLTTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLRqfkSGSPV 345
Cdd:PTZ00421 131 VSFHPSAMNVLASAGADMVVNVWDVER--GKA--VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPR---DGTIV 203


                 ....*.
gi 58865700  346 ATFKQH 351
Cdd:PTZ00421 204 SSVEAH 209
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 344-397 2.41e-03

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: 39.63  E-value: 2.41e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 58865700 344 PVATFKQHVAPVTSVEWHPqDSGVFAASGADNQITQWDLAVERDPESGETETDP 397
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGP 53
PTZ00421 PTZ00421
coronin; Provisional
 319-386 2.51e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.26  E-value: 2.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58865700  319 EPF----LLSGGDDGTLKVWD-----LRQFKSgSPVATFKQHVAPVTSVEWHPQDSGVFAASGADNQITQWDlaVER 386
Cdd:PTZ00421  84 NPFdpqkLFTASEDGTIMGWGipeegLTQNIS-DPIVHLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWD--VER 157
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 266-360 5.50e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.10  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865700   266 LQWSPTEDTVfASCSADASI--------RIWDIraapgkacmltTAAAHDGDVNVISWSRREPFLLSGGDDGTLKVWDLr 337
Cdd:pfam12894   1 MSWCPTMDLI-ALATEDGELllhrlnwqRVWTL-----------SPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDA- 67

                          90       100
                  ....*....|....*....|...
gi 58865700   338 qfKSGSPVATFKQHVAPVTSVEW 360
Cdd:pfam12894  68 --ENGKIVHHFSAGSDLITCLGW 88
 
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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