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Conserved domains on  [gi|1775894724|gb|KGN66623|]
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hypothetical protein Csa_007166 [Cucumis sativus]

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 ...
 164-423 1.62e-29

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 117.44  E-value: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 164 HPGEVNRIRELPQNSRIVATHTDSpDVLIWDVEAQPNRHavlgatnsrpdlILTGHqENAEFALAMCPTEPYVLSGGKDK 243
Cdd:cd00200    50 HTGPVRDVAASADGTYLASGSSDK-TIRLWDLETGECVR------------TLTGH-TSYVSSVAFSPDGRILSSSSRDK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 244 LVVLWSIQD----HITTSATDAGASKSPGSGGSIIKkpGEANDKAS---DGPSIGPRGVYHGHEDTVEDVTFCPSNaQEF 316
Cdd:cd00200   116 TIKVWDVETgkclTTLRGHTDWVNSVAFSPDGTFVA--SSSQDGTIklwDLRTGKCVATLTGHTGEVNSVAFSPDG-EKL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 317 CSVGDDSCLILWDARTGSSpaVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAA 396
Cdd:cd00200   193 LSSSSDGTIKLWDLSTGKC--LGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRT------GECVQTLSGHTNS 263

                         250       260
                  ....*....|....*....|....*..
gi 1775894724 397 VLCVQWSPDKSSVFgSSAEDGLLNIWD 423
Cdd:cd00200   264 VTSLAWSPDGKRLA-SGSADGTIRIWD 289
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 67-135 5.69e-21

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: 86.48  E-value: 5.69e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1775894724  67 ERYTQWKSLVPVLYDWFANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVK 135
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDTSEGKNYTVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 390-518 4.65e-07

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: 51.57  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 390 FEGHKAAVLCVQWSPDkSSVFGSSAEDGLLNIWDYDKVGKKTERatrtpaappglffqhAGHRDKVVDFHWNAADPWtVV 469
Cdd:cd00200     5 LKGHTGGVTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTL---------------KGHTGPVRDVAASADGTY-LA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1775894724 470 SVSDDcdttgggGTLQIWRMSDliyrpeEEVLAELEKFKSHVIECAAKP 518
Cdd:cd00200    68 SGSSD-------KTIRLWDLET------GECVRTLTGHTSYVSSVAFSP 103
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-423 1.62e-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: 117.44  E-value: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 164 HPGEVNRIRELPQNSRIVATHTDSpDVLIWDVEAQPNRHavlgatnsrpdlILTGHqENAEFALAMCPTEPYVLSGGKDK 243
Cdd:cd00200    50 HTGPVRDVAASADGTYLASGSSDK-TIRLWDLETGECVR------------TLTGH-TSYVSSVAFSPDGRILSSSSRDK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 244 LVVLWSIQD----HITTSATDAGASKSPGSGGSIIKkpGEANDKAS---DGPSIGPRGVYHGHEDTVEDVTFCPSNaQEF 316
Cdd:cd00200   116 TIKVWDVETgkclTTLRGHTDWVNSVAFSPDGTFVA--SSSQDGTIklwDLRTGKCVATLTGHTGEVNSVAFSPDG-EKL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 317 CSVGDDSCLILWDARTGSSpaVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAA 396
Cdd:cd00200   193 LSSSSDGTIKLWDLSTGKC--LGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRT------GECVQTLSGHTNS 263

                         250       260
                  ....*....|....*....|....*..
gi 1775894724 397 VLCVQWSPDKSSVFgSSAEDGLLNIWD 423
Cdd:cd00200   264 VTSLAWSPDGKRLA-SGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
164-491 7.34e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.76  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 164 HPGEVNRIRELPQNSRIVATHTDSpDVLIWDVEaqpnrhavlgatNSRPDLILTGHQENAeFALAMCPTEPYVLSGGKDK 243
Cdd:COG2319   161 HSGAVTSVAFSPDGKLLASGSDDG-TVRLWDLA------------TGKLLRTLTGHTGAV-RSVAFSPDGKLLASGSADG 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 244 LVVLWSIQdhittsatdagaskspgsGGSIIKkpgeandkasdgpsigprgVYHGHEDTVEDVTFCPsNAQEFCSVGDDS 323
Cdd:COG2319   227 TVRLWDLA------------------TGKLLR-------------------TLTGHSGSVRSVAFSP-DGRLLASGSADG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 324 CLILWDARTGSspAVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAAVLCVQWS 403
Cdd:COG2319   269 TVRLWDLATGE--LLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAVRSVAFS 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 404 PDKSSVFgSSAEDGLLNIWDydkVGKKTERATRTpaappglffqhaGHRDKVVDFHWNAADPWtVVSVSDDcdttgggGT 483
Cdd:COG2319   340 PDGKTLA-SGSDDGTVRLWD---LATGELLRTLT------------GHTGAVTSVAFSPDGRT-LASGSAD-------GT 395


                  ....*...
gi 1775894724 484 LQIWRMSD 491
Cdd:COG2319   396 VRLWDLAT 403
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 67-135 5.69e-21

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: 86.48  E-value: 5.69e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1775894724  67 ERYTQWKSLVPVLYDWFANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVK 135
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDTSEGKNYTVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 390-518 4.65e-07

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: 51.57  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 390 FEGHKAAVLCVQWSPDkSSVFGSSAEDGLLNIWDYDKVGKKTERatrtpaappglffqhAGHRDKVVDFHWNAADPWtVV 469
Cdd:cd00200     5 LKGHTGGVTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTL---------------KGHTGPVRDVAASADGTY-LA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1775894724 470 SVSDDcdttgggGTLQIWRMSDliyrpeEEVLAELEKFKSHVIECAAKP 518
Cdd:cd00200    68 SGSSD-------KTIRLWDLET------GECVRTLTGHTSYVSSVAFSP 103
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 384-423 2.04e-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: 2.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1775894724  384 GSPIYKFEGHKAAVLCVQWSPDkSSVFGSSAEDGLLNIWD 423
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
384-423 8.74e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 8.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1775894724 384 GSPIYKFEGHKAAVLCVQWSPDKSSVFgSSAEDGLLNIWD 423
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLA-SGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 336-423 2.28e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 46.87  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 336 PAVKVeKAHNADLHCVDWNPHDDNLIITGSADNSIRLFDRR--NLTSNGVGSPIYKFEGHKAAVLCVQWSPDKSSVFGSS 413
Cdd:PTZ00420   66 PVIKL-KGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPhnDESVKEIKDPQCILKGHKKKISIIDWNPMNYYIMCSS 144

                          90
                  ....*....|
gi 1775894724 414 AEDGLLNIWD 423
Cdd:PTZ00420  145 GFDSFVNIWD 154
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-423 1.62e-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: 117.44  E-value: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 164 HPGEVNRIRELPQNSRIVATHTDSpDVLIWDVEAQPNRHavlgatnsrpdlILTGHqENAEFALAMCPTEPYVLSGGKDK 243
Cdd:cd00200    50 HTGPVRDVAASADGTYLASGSSDK-TIRLWDLETGECVR------------TLTGH-TSYVSSVAFSPDGRILSSSSRDK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 244 LVVLWSIQD----HITTSATDAGASKSPGSGGSIIKkpGEANDKAS---DGPSIGPRGVYHGHEDTVEDVTFCPSNaQEF 316
Cdd:cd00200   116 TIKVWDVETgkclTTLRGHTDWVNSVAFSPDGTFVA--SSSQDGTIklwDLRTGKCVATLTGHTGEVNSVAFSPDG-EKL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 317 CSVGDDSCLILWDARTGSSpaVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAA 396
Cdd:cd00200   193 LSSSSDGTIKLWDLSTGKC--LGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRT------GECVQTLSGHTNS 263

                         250       260
                  ....*....|....*....|....*..
gi 1775894724 397 VLCVQWSPDKSSVFgSSAEDGLLNIWD 423
Cdd:cd00200   264 VTSLAWSPDGKRLA-SGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-489 7.00e-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: 110.12  E-value: 7.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 164 HPGEVNRIRELPQNSRIVATHTDSpDVLIWDVEaqpnrhavlgatNSRPDLILTGHQENAEFALAmCPTEPYVLSGGKDK 243
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDG-TIKVWDLE------------TGELLRTLKGHTGPVRDVAA-SADGTYLASGSSDK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 244 LVVLWSIQDHITTSatdagaskspgsggsiikkpgeandkasdgpsigprgVYHGHEDTVEDVTFCPSNaQEFCSVGDDS 323
Cdd:cd00200    74 TIRLWDLETGECVR-------------------------------------TLTGHTSYVSSVAFSPDG-RILSSSSRDK 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 324 CLILWDARTGSspAVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAAVLCVQWS 403
Cdd:cd00200   116 TIKVWDVETGK--CLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRT------GKCVATLTGHTGEVNSVAFS 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 404 PDKSSVFgSSAEDGLLNIWDYDKvGKKTEratrtpaappglffQHAGHRDKV--VDFHWnaaDPWTVVSVSDDcdttggg 481
Cdd:cd00200   187 PDGEKLL-SSSSDGTIKLWDLST-GKCLG--------------TLRGHENGVnsVAFSP---DGYLLASGSED------- 240


                  ....*...
gi 1775894724 482 GTLQIWRM 489
Cdd:cd00200   241 GTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
164-491 7.34e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.76  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 164 HPGEVNRIRELPQNSRIVATHTDSpDVLIWDVEaqpnrhavlgatNSRPDLILTGHQENAeFALAMCPTEPYVLSGGKDK 243
Cdd:COG2319   161 HSGAVTSVAFSPDGKLLASGSDDG-TVRLWDLA------------TGKLLRTLTGHTGAV-RSVAFSPDGKLLASGSADG 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 244 LVVLWSIQdhittsatdagaskspgsGGSIIKkpgeandkasdgpsigprgVYHGHEDTVEDVTFCPsNAQEFCSVGDDS 323
Cdd:COG2319   227 TVRLWDLA------------------TGKLLR-------------------TLTGHSGSVRSVAFSP-DGRLLASGSADG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 324 CLILWDARTGSspAVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAAVLCVQWS 403
Cdd:COG2319   269 TVRLWDLATGE--LLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAVRSVAFS 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 404 PDKSSVFgSSAEDGLLNIWDydkVGKKTERATRTpaappglffqhaGHRDKVVDFHWNAADPWtVVSVSDDcdttgggGT 483
Cdd:COG2319   340 PDGKTLA-SGSDDGTVRLWD---LATGELLRTLT------------GHTGAVTSVAFSPDGRT-LASGSAD-------GT 395


                  ....*...
gi 1775894724 484 LQIWRMSD 491
Cdd:COG2319   396 VRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 298-491 2.27e-21

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: 94.32  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 298 GHEDTVEDVTFCPsNAQEFCSVGDDSCLILWDARTGSSpaVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFDRRN 377
Cdd:cd00200    49 GHTGPVRDVAASA-DGTYLASGSSDKTIRLWDLETGEC--VRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVET 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 378 ltsngvGSPIYKFEGHKAAVLCVQWSPDKSSVFGSSAeDGLLNIWDYdkvgkKTERATRTpaappglffqHAGHRDKV-- 455
Cdd:cd00200   125 ------GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQ-DGTIKLWDL-----RTGKCVAT----------LTGHTGEVns 182

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1775894724 456 VDFHwnaADPWTVVSVSDDcdttgggGTLQIWRMSD 491
Cdd:cd00200   183 VAFS---PDGEKLLSSSSD-------GTIKLWDLST 208
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 67-135 5.69e-21

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: 86.48  E-value: 5.69e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1775894724  67 ERYTQWKSLVPVLYDWFANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVK 135
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDTSEGKNYTVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 COG2319
WD40 repeat [General function prediction only];
191-491 2.41e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.19  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 191 LIWDVEAQPNRHAVLGATNSRPDLILTGHQENAEFALAMCPTEPYVLSGGKDKLVVLWSIQD----HITTSATDAGASKS 266
Cdd:COG2319     6 GAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAgallATLLGHTAAVLSVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 267 PGSGGSIIKKPGEAND-KASDGPSIGPRGVYHGHEDTVEDVTFCPsNAQEFCSVGDDSCLILWDARTGssPAVKVEKAHN 345
Cdd:COG2319    86 FSPDGRLLASASADGTvRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATG--KLLRTLTGHS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 346 ADLHCVDWNPhDDNLIITGSADNSIRLFDRRNltsngvGSPIYKFEGHKAAVLCVQWSPDkSSVFGSSAEDGLLNIWDYD 425
Cdd:COG2319   163 GAVTSVAFSP-DGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAVRSVAFSPD-GKLLASGSADGTVRLWDLA 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1775894724 426 kvgkkTERATRTPaappglffqhAGHRDKV--VDFHwnaADPWTVVSVSDDcdttgggGTLQIWRMSD 491
Cdd:COG2319   235 -----TGKLLRTL----------TGHSGSVrsVAFS---PDGRLLASGSAD-------GTVRLWDLAT 277
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 292-490 8.21e-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: 80.84  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 292 PRGVYHGHEDTVEDVTFCPSNaQEFCSVGDDSCLILWDARTGSspAVKVEKAHNADLHCVDWNPhDDNLIITGSADNSIR 371
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLETGE--LLRTLKGHTGPVRDVAASA-DGTYLASGSSDKTIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 372 LFDRRNltsngvGSPIYKFEGHKAAVLCVQWSPDKSSVFGSSAeDGLLNIWDydkVGKKTERATRTpaappglffqhaGH 451
Cdd:cd00200    77 LWDLET------GECVRTLTGHTSYVSSVAFSPDGRILSSSSR-DKTIKVWD---VETGKCLTTLR------------GH 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1775894724 452 RDKV--VDFHWnaaDPWTVVSVSDDcdttgggGTLQIWRMS 490
Cdd:cd00200   135 TDWVnsVAFSP---DGTFVASSSQD-------GTIKLWDLR 165
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 390-518 4.65e-07

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: 51.57  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 390 FEGHKAAVLCVQWSPDkSSVFGSSAEDGLLNIWDYDKVGKKTERatrtpaappglffqhAGHRDKVVDFHWNAADPWtVV 469
Cdd:cd00200     5 LKGHTGGVTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTL---------------KGHTGPVRDVAASADGTY-LA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1775894724 470 SVSDDcdttgggGTLQIWRMSDliyrpeEEVLAELEKFKSHVIECAAKP 518
Cdd:cd00200    68 SGSSD-------KTIRLWDLET------GECVRTLTGHTSYVSSVAFSP 103
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 384-423 2.04e-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: 2.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1775894724  384 GSPIYKFEGHKAAVLCVQWSPDkSSVFGSSAEDGLLNIWD 423
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
384-423 8.74e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 8.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1775894724 384 GSPIYKFEGHKAAVLCVQWSPDKSSVFgSSAEDGLLNIWD 423
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLA-SGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 336-423 2.28e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 46.87  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 336 PAVKVeKAHNADLHCVDWNPHDDNLIITGSADNSIRLFDRR--NLTSNGVGSPIYKFEGHKAAVLCVQWSPDKSSVFGSS 413
Cdd:PTZ00420   66 PVIKL-KGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPhnDESVKEIKDPQCILKGHKKKISIIDWNPMNYYIMCSS 144

                          90
                  ....*....|
gi 1775894724 414 AEDGLLNIWD 423
Cdd:PTZ00420  145 GFDSFVNIWD 154
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 342-374 2.88e-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: 41.14  E-value: 2.88e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1775894724  342 KAHNADLHCVDWNPhDDNLIITGSADNSIRLFD 374
Cdd:smart00320   9 KGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 351-426 1.09e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 1.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1775894724 351 VDWNPHDDNLIITGSADNSIRLFD--RRNLTSNgVGSPIYKFEGHKAAVLCVQWSPDKSSVFGSSAEDGLLNIWDYDK 426
Cdd:PTZ00421   81 VAFNPFDPQKLFTASEDGTIMGWGipEEGLTQN-ISDPIVHLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVER 157
PTZ00421 PTZ00421
coronin; Provisional
 298-379 1.09e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775894724 298 GHEDTVEDVTFCPSNAQEFCSVGDDSCLILWDARTGSspAVKVEKAHNADLHCVDWNpHDDNLIITGSADNSIRLFDRRN 377
Cdd:PTZ00421  123 GHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGK--AVEVIKCHSDQITSLEWN-LDGSLLCTTSKDKKLNIIDPRD 199


                  ..
gi 1775894724 378 LT 379
Cdd:PTZ00421  200 GT 201
WD40 pfam00400
WD domain, G-beta repeat;
338-374 1.41e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1775894724 338 VKVEKAHNADLHCVDWNPhDDNLIITGSADNSIRLFD 374
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 292-329 1.28e-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: 36.52  E-value: 1.28e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1775894724  292 PRGVYHGHEDTVEDVTFCPSNaQEFCSVGDDSCLILWD 329
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
 
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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