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Conserved domains on  [gi|1443040548|ref|XP_015621921|]
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WD-40 repeat-containing protein MSI4 isoform X2 [Oryza sativa Japonica Group]

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 ...
 224-487 4.45e-26

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: 107.81  E-value: 4.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 224 LRGHKDIAeFALAMCPAEPYVLSGGKDKSVVWWSIQD---------HISALGDSSKTESSPG-ASGSKGKTANDKDSPKV 293
Cdd:cd00200     5 LKGHTGGV-TCVAFSPDGKLLATGSGDGTIKVWDLETgellrtlkgHTGPVRDVAASADGTYlASGSSDKTIRLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 294 DPRGIFLGHDSTVEDVQFCPSSaQEFCSVGDDSCLILWDARsgTGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSV 373
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVE--TGKCLTTLRGHTDWVNSVAFS-PDGTFVASSSQDGTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 374 RMWDrrnlgsGGAGIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDGFLNVWDHEKVGNKKnpnapaglffQHAGHRDKI 453
Cdd:cd00200   160 KLWD------LRTGKCVATLTGHTGEVNSVAFSPDGEKLL-SSSSDGTIKLWDLSTGKCLG----------TLRGHENGV 222

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1443040548 454 VDFHWNSSDPWtIVSVSDDgestgggGTLQIWRM 487
Cdd:cd00200   223 NSVAFSPDGYL-LASGSED-------GTIRVWDL 248
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 75-143 1.12e-19

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: 83.01  E-value: 1.12e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040548  75 ERYAQWKSLIPVLYDWFANHNLVWPSLSCRWGPQFEKATYKNRQRLYLSEQTDGTVPNTLVIANCEVVK 143
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDTSEGKNYTVQRLLLGTQTSGAEQNYLYVAKVSLPS 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 ...
 224-487 4.45e-26

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: 107.81  E-value: 4.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 224 LRGHKDIAeFALAMCPAEPYVLSGGKDKSVVWWSIQD---------HISALGDSSKTESSPG-ASGSKGKTANDKDSPKV 293
Cdd:cd00200     5 LKGHTGGV-TCVAFSPDGKLLATGSGDGTIKVWDLETgellrtlkgHTGPVRDVAASADGTYlASGSSDKTIRLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 294 DPRGIFLGHDSTVEDVQFCPSSaQEFCSVGDDSCLILWDARsgTGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSV 373
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVE--TGKCLTTLRGHTDWVNSVAFS-PDGTFVASSSQDGTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 374 RMWDrrnlgsGGAGIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDGFLNVWDHEKVGNKKnpnapaglffQHAGHRDKI 453
Cdd:cd00200   160 KLWD------LRTGKCVATLTGHTGEVNSVAFSPDGEKLL-SSSSDGTIKLWDLSTGKCLG----------TLRGHENGV 222

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1443040548 454 VDFHWNSSDPWtIVSVSDDgestgggGTLQIWRM 487
Cdd:cd00200   223 NSVAFSPDGYL-LASGSED-------GTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
172-489 1.58e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 172 HPGEVNRIRELPqNSKIIATHTDSPDVLIWDVEAQPNRQaqlaqmesrpdlILRGHKDIAeFALAMCPAEPYVLSGGKDK 251
Cdd:COG2319   119 HTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLR------------TLTGHSGAV-TSVAFSPDGKLLASGSDDG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 252 SVVWWSIQD--HISAL-GDSSKTES---SPG----ASGSKGKTAN--DKDSPKvdPRGIFLGHDSTVEDVQFCPSSaQEF 319
Cdd:COG2319   185 TVRLWDLATgkLLRTLtGHTGAVRSvafSPDgkllASGSADGTVRlwDLATGK--LLRTLTGHSGSVRSVAFSPDG-RLL 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 320 CSVGDDSCLILWDARsgTGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSVRMWDRRNlgsggaGIPVHKFEGHKAA 399
Cdd:COG2319   262 ASGSADGTVRLWDLA--TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGA 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 400 VLCVQWSPDKASVFgSSAEDGFLNVWDhekvgnkknpNAPAGLFFQHAGHRDKIVDfhwnssdpwtiVSVSDDGE---ST 476
Cdd:COG2319   333 VRSVAFSPDGKTLA-SGSDDGTVRLWD----------LATGELLRTLTGHTGAVTS-----------VAFSPDGRtlaSG 390

                         330
                  ....*....|...
gi 1443040548 477 GGGGTLQIWRMSD 489
Cdd:COG2319   391 SADGTVRLWDLAT 403
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 75-143 1.12e-19

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: 83.01  E-value: 1.12e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040548  75 ERYAQWKSLIPVLYDWFANHNLVWPSLSCRWGPQFEKATYKNRQRLYLSEQTDGTVPNTLVIANCEVVK 143
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDTSEGKNYTVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 337-377 4.72e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 4.72e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1443040548  337 TGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSVRMWD 377
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFS-PDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
387-426 4.23e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 4.23e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1443040548 387 GIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDGFLNVWD 426
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLA-SGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 301-380 8.24e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.27  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 301 GHDSTVEDVQFCPSSAQEFCSVGDDSCLILWDARSGTgpAVKVEKAHGGDVHCVDWNLhDVNYILTGSADNSVRMWDRRN 380
Cdd:PTZ00421  123 GHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGK--AVEVIKCHSDQITSLEWNL-DGSLLCTTSKDKKLNIIDPRD 199
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 224-487 4.45e-26

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: 107.81  E-value: 4.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 224 LRGHKDIAeFALAMCPAEPYVLSGGKDKSVVWWSIQD---------HISALGDSSKTESSPG-ASGSKGKTANDKDSPKV 293
Cdd:cd00200     5 LKGHTGGV-TCVAFSPDGKLLATGSGDGTIKVWDLETgellrtlkgHTGPVRDVAASADGTYlASGSSDKTIRLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 294 DPRGIFLGHDSTVEDVQFCPSSaQEFCSVGDDSCLILWDARsgTGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSV 373
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVE--TGKCLTTLRGHTDWVNSVAFS-PDGTFVASSSQDGTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 374 RMWDrrnlgsGGAGIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDGFLNVWDHEKVGNKKnpnapaglffQHAGHRDKI 453
Cdd:cd00200   160 KLWD------LRTGKCVATLTGHTGEVNSVAFSPDGEKLL-SSSSDGTIKLWDLSTGKCLG----------TLRGHENGV 222

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1443040548 454 VDFHWNSSDPWtIVSVSDDgestgggGTLQIWRM 487
Cdd:cd00200   223 NSVAFSPDGYL-LASGSED-------GTIRVWDL 248
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 172-426 1.56e-25

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 106.27  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 172 HPGEVNRIRELPQNSKIIATHTDSpDVLIWDVEAQPNRQaqlaqmesrpdlILRGHKDiAEFALAMCPAEPYVLSGGKDK 251
Cdd:cd00200    50 HTGPVRDVAASADGTYLASGSSDK-TIRLWDLETGECVR------------TLTGHTS-YVSSVAFSPDGRILSSSSRDK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 252 SVVWW---------SIQDHISALGDSSKTESSP-GASGSKGKTAN--DKDSPKvdPRGIFLGHDSTVEDVQFCPSSaQEF 319
Cdd:cd00200   116 TIKVWdvetgkcltTLRGHTDWVNSVAFSPDGTfVASSSQDGTIKlwDLRTGK--CVATLTGHTGEVNSVAFSPDG-EKL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 320 CSVGDDSCLILWDARSGTgpAVKVEKAHGGDVHCVDWNLHDvNYILTGSADNSVRMWDRRNlgsggaGIPVHKFEGHKAA 399
Cdd:cd00200   193 LSSSSDGTIKLWDLSTGK--CLGTLRGHENGVNSVAFSPDG-YLLASGSEDGTIRVWDLRT------GECVQTLSGHTNS 263

                         250       260
                  ....*....|....*....|....*..
gi 1443040548 400 VLCVQWSPDKASVFgSSAEDGFLNVWD 426
Cdd:cd00200   264 VTSLAWSPDGKRLA-SGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 172-486 1.09e-23

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: 100.87  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 172 HPGEVNRIRELPQNSKIIATHTDSpDVLIWDVEaqpnrqaqlaqmESRPDLILRGHKDIAEFALAmCPAEPYVLSGGKDK 251
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDG-TIKVWDLE------------TGELLRTLKGHTGPVRDVAA-SADGTYLASGSSDK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 252 SV-VWWSIQDH-ISALGDSSKTESS----PG----ASGSKGKTANDKDSPKVDPRGIFLGHDSTVEDVQFCPSSAQEFCS 321
Cdd:cd00200    74 TIrLWDLETGEcVRTLTGHTSYVSSvafsPDgrilSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 322 vGDDSCLILWDARSGTgpAVKVEKAHGGDVHCVDWnLHDVNYILTGSADNSVRMWDRRnlgsggAGIPVHKFEGHKAAVL 401
Cdd:cd00200   154 -SQDGTIKLWDLRTGK--CVATLTGHTGEVNSVAF-SPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLRGHENGVN 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 402 CVQWSPDKASVFgSSAEDGFLNVWDHEKVGNKKnpnapaglffQHAGHRDKIVDFHWnSSDPWTIVSVSDDgestgggGT 481
Cdd:cd00200   224 SVAFSPDGYLLA-SGSEDGTIRVWDLRTGECVQ----------TLSGHTNSVTSLAW-SPDGKRLASGSAD-------GT 284


                  ....*
gi 1443040548 482 LQIWR 486
Cdd:cd00200   285 IRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
172-489 1.58e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 172 HPGEVNRIRELPqNSKIIATHTDSPDVLIWDVEAQPNRQaqlaqmesrpdlILRGHKDIAeFALAMCPAEPYVLSGGKDK 251
Cdd:COG2319   119 HTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLR------------TLTGHSGAV-TSVAFSPDGKLLASGSDDG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 252 SVVWWSIQD--HISAL-GDSSKTES---SPG----ASGSKGKTAN--DKDSPKvdPRGIFLGHDSTVEDVQFCPSSaQEF 319
Cdd:COG2319   185 TVRLWDLATgkLLRTLtGHTGAVRSvafSPDgkllASGSADGTVRlwDLATGK--LLRTLTGHSGSVRSVAFSPDG-RLL 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 320 CSVGDDSCLILWDARsgTGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSVRMWDRRNlgsggaGIPVHKFEGHKAA 399
Cdd:COG2319   262 ASGSADGTVRLWDLA--TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGA 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 400 VLCVQWSPDKASVFgSSAEDGFLNVWDhekvgnkknpNAPAGLFFQHAGHRDKIVDfhwnssdpwtiVSVSDDGE---ST 476
Cdd:COG2319   333 VRSVAFSPDGKTLA-SGSDDGTVRLWD----------LATGELLRTLTGHTGAVTS-----------VAFSPDGRtlaSG 390

                         330
                  ....*....|...
gi 1443040548 477 GGGGTLQIWRMSD 489
Cdd:COG2319   391 SADGTVRLWDLAT 403
CAF1C_H4-bd pfam12265
Histone-binding protein RBBP4 or subunit C of CAF1 complex; The CAF-1 complex is a conserved ...
 75-143 1.12e-19

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: 83.01  E-value: 1.12e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040548  75 ERYAQWKSLIPVLYDWFANHNLVWPSLSCRWGPQFEKATYKNRQRLYLSEQTDGTVPNTLVIANCEVVK 143
Cdd:pfam12265   1 EEYLIWKKNAPFLYDMLHTHALEWPSLSFDWFPDTSEGKNYTVQRLLLGTQTSGAEQNYLYVAKVSLPS 69
WD40 COG2319
WD40 repeat [General function prediction only];
195-489 2.44e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 195 SPDVLIWDVEAQPNRQAQLAQMESRPDLILRGHKDIAEFALAMCPAEPYVLSGGKDKSVVWWSIQDHISAL------GDS 268
Cdd:COG2319     3 SADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATllghtaAVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 269 SKTESSPG---ASGSKGKTANDKDSPKVDPRGIFLGHDSTVEDVQFCPSS---AqefcSVGDDSCLILWDARsgTGPAVK 342
Cdd:COG2319    83 SVAFSPDGrllASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGktlA----SGSADGTVRLWDLA--TGKLLR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 343 VEKAHGGDVHCVDWNlHDVNYILTGSADNSVRMWDRRNlgsggaGIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDGFL 422
Cdd:COG2319   157 TLTGHSGAVTSVAFS-PDGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAVRSVAFSPDGKLLA-SGSADGTV 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040548 423 NVWDhekVGNKKnpnapagLFFQHAGHRDKIVDFHWnSSDPWTIVSVSDDgestgggGTLQIWRMSD 489
Cdd:COG2319   229 RLWD---LATGK-------LLRTLTGHSGSVRSVAF-SPDGRLLASGSAD-------GTVRLWDLAT 277
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 341-485 1.41e-14

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: 74.29  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 341 VKVEKAHGGDVHCVDWNLhDVNYILTGSADNSVRMWDRRNlgsggaGIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDG 420
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLET------GELLRTLKGHTGPVRDVAASADGTYLA-SGSSDK 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040548 421 FLNVWDhekVGNKKnpnapagLFFQHAGHRDKIVDFHWNSSDPWtIVSVSDDgestgggGTLQIW 485
Cdd:cd00200    74 TIRLWD---LETGE-------CVRTLTGHTSYVSSVAFSPDGRI-LSSSSRD-------KTIKVW 120
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 337-377 4.72e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 4.72e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1443040548  337 TGPAVKVEKAHGGDVHCVDWNlHDVNYILTGSADNSVRMWD 377
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFS-PDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 387-426 1.05e-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: 42.30  E-value: 1.05e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1443040548  387 GIPVHKFEGHKAAVLCVQWSPDKaSVFGSSAEDGFLNVWD 426
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 389-513 1.32e-05

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: 46.94  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 389 PVHKFEGHKAAVLCVQWSPDKaSVFGSSAEDGFLNVWDHEkvgnkknpnaPAGLFFQHAGHRDKIVDFHWNSSDPWtIVS 468
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLE----------TGELLRTLKGHTGPVRDVAASADGTY-LAS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1443040548 469 VSDDgestgggGTLQIWRMSDliyrpeDEVLAELENFKTHLASCA 513
Cdd:cd00200    69 GSSD-------KTIRLWDLET------GECVRTLTGHTSYVSSVA 100
WD40 pfam00400
WD domain, G-beta repeat;
387-426 4.23e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 4.23e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1443040548 387 GIPVHKFEGHKAAVLCVQWSPDKASVFgSSAEDGFLNVWD 426
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLA-SGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
341-377 6.03e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 6.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1443040548 341 VKVEKAHGGDVHCVDWNlHDVNYILTGSADNSVRMWD 377
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFS-PDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 301-380 8.24e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.27  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 301 GHDSTVEDVQFCPSSAQEFCSVGDDSCLILWDARSGTgpAVKVEKAHGGDVHCVDWNLhDVNYILTGSADNSVRMWDRRN 380
Cdd:PTZ00421  123 GHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGK--AVEVIKCHSDQITSLEWNL-DGSLLCTTSKDKKLNIIDPRD 199
PTZ00420 PTZ00420
coronin; Provisional
 339-428 8.43e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.86  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 339 PAVKVeKAHGGDVHCVDWNLHDVNYILTGSADNSVRMWDRRNLGSGGAGI--PVHKFEGHKAAVLCVQWSPDKASVFGSS 416
Cdd:PTZ00420   66 PVIKL-KGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVKEIkdPQCILKGHKKKISIIDWNPMNYYIMCSS 144

                          90
                  ....*....|..
gi 1443040548 417 AEDGFLNVWDHE 428
Cdd:PTZ00420  145 GFDSFVNIWDIE 156
PTZ00420 PTZ00420
coronin; Provisional
 301-380 4.62e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 39.55  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040548 301 GHDSTVEDVQFCPSSAQEFCSVGDDSCLILWDARSGTGPAVKVE------KAHGGDVHCVDWNlhDVNYILTGSA--DNS 372
Cdd:PTZ00420   72 GHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVKEIKdpqcilKGHKKKISIIDWN--PMNYYIMCSSgfDSF 149


                  ....*...
gi 1443040548 373 VRMWDRRN 380
Cdd:PTZ00420  150 VNIWDIEN 157
 
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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