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Conserved domains on  [gi|2501356900|ref|NP_001407901|]
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zinc finger protein 106 isoform 2 [Mus musculus]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 1000017)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  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 ...
 1530-1727 2.21e-31

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: 125.53  E-value: 2.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1530 GSFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLvthTSGKSSVLYTGSSDHTIRCYN 1607
Cdd:cd00200      3 RTLKGHTGGVTCVAFSpdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVA---ASADGTYLASGSSDKTIRLWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1608 IKTRECMEQLQL-EDRVLCL--HNRWRTLYAGLANGTVVTFDIKNNKRQEIFECHgPRAVSCLATAQEGarKLLVVGSYD 1684
Cdd:cd00200     80 LETGECVRTLTGhTSYVSSVafSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-TDWVNSVAFSPDG--TFVASSSQD 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2501356900 1685 CTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSV 1727
Cdd:cd00200    157 GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTI 201
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 530-681 4.11e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.21  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900  530 PRVLKENKTVSGTQKEPDEK---LNSTSQKAQDTVLQCPKTLQNPLPTTPKRTENDA---KESSVEESAKDSLSIESQPH 603
Cdd:pfam05109  572 PTLGKTSPTSAVTTPTPNATsptVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAvttGQHNITSSSTSSMSLRPSSI 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900  604 SAGNSAMTSDAEN---------HGIKSEGVASLTTevVSCSTHTVDKEQGSQIPGTPENLSAsPCNSTVLQKEAEVQVSA 674
Cdd:pfam05109  652 SETLSPSTSDNSTshmplltsaHPTGGENITQVTP--ASTSTHHVSTSSPAPRPGTTSQASG-PGNSSTSTKPGEVNVTK 728


                   ....*..
gi 2501356900  675 ATSPHSG 681
Cdd:pfam05109  729 GTPPKNA 735
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1530-1727 2.21e-31

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: 125.53  E-value: 2.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1530 GSFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLvthTSGKSSVLYTGSSDHTIRCYN 1607
Cdd:cd00200      3 RTLKGHTGGVTCVAFSpdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVA---ASADGTYLASGSSDKTIRLWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1608 IKTRECMEQLQL-EDRVLCL--HNRWRTLYAGLANGTVVTFDIKNNKRQEIFECHgPRAVSCLATAQEGarKLLVVGSYD 1684
Cdd:cd00200     80 LETGECVRTLTGhTSYVSSVafSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-TDWVNSVAFSPDG--TFVASSSQD 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2501356900 1685 CTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSV 1727
Cdd:cd00200    157 GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTI 201
WD40 COG2319
WD40 repeat [General function prediction only];
1531-1728 3.85e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 116.16  E-value: 3.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1531 SFEGHQAAVNAIQiF---GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYN 1607
Cdd:COG2319    199 TLTGHTGAVRSVA-FspdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF---SPDGRLLASGSADGTVRLWD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1608 IKTRECMEQLQ-LEDRVLCLhnRW----RTLYAGLANGTVVTFDIKNNKRQEIFECHGpRAVSCLATAQEGarKLLVVGS 1682
Cdd:COG2319    275 LATGELLRTLTgHSGGVNSV--AFspdgKLLASGSDDGTVRLWDLATGKLLRTLTGHT-GAVRSVAFSPDG--KTLASGS 349

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2501356900 1683 YDCTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSVH 1728
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDgrTLASGSADGTVR 397
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1565-1607 9.10e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 44.23  E-value: 9.10e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2501356900  1565 SRKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYN 1607
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAF---SPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1566-1607 8.66e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.18  E-value: 8.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2501356900 1566 RKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYN 1607
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAF---SPDGKLLASGSDDGTVKVWD 39
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 530-681 4.11e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.21  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900  530 PRVLKENKTVSGTQKEPDEK---LNSTSQKAQDTVLQCPKTLQNPLPTTPKRTENDA---KESSVEESAKDSLSIESQPH 603
Cdd:pfam05109  572 PTLGKTSPTSAVTTPTPNATsptVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAvttGQHNITSSSTSSMSLRPSSI 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900  604 SAGNSAMTSDAEN---------HGIKSEGVASLTTevVSCSTHTVDKEQGSQIPGTPENLSAsPCNSTVLQKEAEVQVSA 674
Cdd:pfam05109  652 SETLSPSTSDNSTshmplltsaHPTGGENITQVTP--ASTSTHHVSTSSPAPRPGTTSQASG-PGNSSTSTKPGEVNVTK 728


                   ....*..
gi 2501356900  675 ATSPHSG 681
Cdd:pfam05109  729 GTPPKNA 735
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1530-1727 2.21e-31

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: 125.53  E-value: 2.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1530 GSFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLvthTSGKSSVLYTGSSDHTIRCYN 1607
Cdd:cd00200      3 RTLKGHTGGVTCVAFSpdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVA---ASADGTYLASGSSDKTIRLWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1608 IKTRECMEQLQL-EDRVLCL--HNRWRTLYAGLANGTVVTFDIKNNKRQEIFECHgPRAVSCLATAQEGarKLLVVGSYD 1684
Cdd:cd00200     80 LETGECVRTLTGhTSYVSSVafSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-TDWVNSVAFSPDG--TFVASSSQD 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2501356900 1685 CTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSV 1727
Cdd:cd00200    157 GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTI 201
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1531-1727 3.70e-31

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: 125.14  E-value: 3.70e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1531 SFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVTHTSGkssVLYTGSSDHTIRCYNI 1608
Cdd:cd00200     88 TLTGHTSYVSSVAFSpdGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT---FVASSSQDGTIKLWDL 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1609 KTRECMEQLQL-EDRV--LCLHNRWRTLYAGLANGTVVTFDIKNNKRQEIFECHgPRAVSCLATAQEgaRKLLVVGSYDC 1685
Cdd:cd00200    165 RTGKCVATLTGhTGEVnsVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-ENGVNSVAFSPD--GYLLASGSEDG 241

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2501356900 1686 TISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSV 1727
Cdd:cd00200    242 TIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgkRLASGSADGTI 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1531-1727 2.79e-28

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: 116.67  E-value: 2.79e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1531 SFEGHQAAVNAIQI--FGNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVTHtsgKSSVLYTGSSDHTIRCYNI 1608
Cdd:cd00200     46 TLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP---DGRILSSSSRDKTIKVWDV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1609 KTRECMEQLQL-EDRVLCLhnRW----RTLYAGLANGTVVTFDIKNNKRQEIFECHgPRAVSCLATAQEGARklLVVGSY 1683
Cdd:cd00200    123 ETGKCLTTLRGhTDWVNSV--AFspdgTFVASSSQDGTIKLWDLRTGKCVATLTGH-TGEVNSVAFSPDGEK--LLSSSS 197

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2501356900 1684 DCTISVRDARNGLLLRTLEGHSKTVLCMKV--VNDLVFSGSSDQSV 1727
Cdd:cd00200    198 DGTIKLWDLSTGKCLGTLRGHENGVNSVAFspDGYLLASGSEDGTI 243
WD40 COG2319
WD40 repeat [General function prediction only];
1531-1728 3.85e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 116.16  E-value: 3.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1531 SFEGHQAAVNAIQiF---GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYN 1607
Cdd:COG2319    199 TLTGHTGAVRSVA-FspdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF---SPDGRLLASGSADGTVRLWD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1608 IKTRECMEQLQ-LEDRVLCLhnRW----RTLYAGLANGTVVTFDIKNNKRQEIFECHGpRAVSCLATAQEGarKLLVVGS 1682
Cdd:COG2319    275 LATGELLRTLTgHSGGVNSV--AFspdgKLLASGSDDGTVRLWDLATGKLLRTLTGHT-GAVRSVAFSPDG--KTLASGS 349

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2501356900 1683 YDCTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSVH 1728
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDgrTLASGSADGTVR 397
WD40 COG2319
WD40 repeat [General function prediction only];
1532-1728 8.31e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 115.01  E-value: 8.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1532 FEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYNIK 1609
Cdd:COG2319    116 LTGHTGAVRSVAFSpdGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF---SPDGKLLASGSDDGTVRLWDLA 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1610 TRECMEQLQL-EDRVLCLhnRW----RTLYAGLANGTVVTFDIKNNKRQEIFECHGPRaVSCLATAQEGarKLLVVGSYD 1684
Cdd:COG2319    193 TGKLLRTLTGhTGAVRSV--AFspdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGS-VRSVAFSPDG--RLLASGSAD 267

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2501356900 1685 CTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSVH 1728
Cdd:COG2319    268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDgkLLASGSDDGTVR 313
WD40 COG2319
WD40 repeat [General function prediction only];
1531-1728 1.77e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 101.91  E-value: 1.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1531 SFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVTHtSGKssVLYTGSSDHTIRCYNI 1608
Cdd:COG2319     73 TLLGHTAAVLSVAFSpdGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGK--TLASGSADGTVRLWDL 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1609 KTRECMEQLQL-EDRVLCLhnRW----RTLYAGLANGTVVTFDIKNNKRQEIFECHgPRAVSCLATAQEGarKLLVVGSY 1683
Cdd:COG2319    150 ATGKLLRTLTGhSGAVTSV--AFspdgKLLASGSDDGTVRLWDLATGKLLRTLTGH-TGAVRSVAFSPDG--KLLASGSA 224

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2501356900 1684 DCTISVRDARNGLLLRTLEGHSKTVLCMKVVND--LVFSGSSDQSVH 1728
Cdd:COG2319    225 DGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDgrLLASGSADGTVR 271
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1568-1728 5.08e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 92.40  E-value: 5.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1568 CVGVFEGHTSKVNCLlvtHTSGKSSVLYTGSSDHTIRCYNIKTRECMEQLQLE----DRVLCLHNRwRTLYAGLANGTVV 1643
Cdd:cd00200      1 LRRTLKGHTGGVTCV---AFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHtgpvRDVAASADG-TYLASGSSDKTIR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1644 TFDIKNNKRQEIFECHgPRAVSCLATAQEGarKLLVVGSYDCTISVRDARNGLLLRTLEGHSKTVLCMKV--VNDLVFSG 1721
Cdd:cd00200     77 LWDLETGECVRTLTGH-TSYVSSVAFSPDG--RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFspDGTFVASS 153


                   ....*..
gi 2501356900 1722 SSDQSVH 1728
Cdd:cd00200    154 SQDGTIK 160
WD40 COG2319
WD40 repeat [General function prediction only];
1531-1694 5.54e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 85.35  E-value: 5.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1531 SFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYNI 1608
Cdd:COG2319    241 TLTGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF---SPDGKLLASGSDDGTVRLWDL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900 1609 KTRECMEQLQ-LEDRVLCLhnRW----RTLYAGLANGTVVTFDIKNNKRQEIFECHGpRAVSCLATAQEGarKLLVVGSY 1683
Cdd:COG2319    318 ATGKLLRTLTgHTGAVRSV--AFspdgKTLASGSDDGTVRLWDLATGELLRTLTGHT-GAVTSVAFSPDG--RTLASGSA 392

                          170
                   ....*....|.
gi 2501356900 1684 DCTISVRDARN 1694
Cdd:COG2319    393 DGTVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1565-1607 9.10e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 44.23  E-value: 9.10e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2501356900  1565 SRKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYN 1607
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAF---SPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1566-1607 8.66e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.18  E-value: 8.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2501356900 1566 RKCVGVFEGHTSKVNCLLVthtSGKSSVLYTGSSDHTIRCYN 1607
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAF---SPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1531-1562 5.70e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.22  E-value: 5.70e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2501356900  1531 SFEGHQAAVNAIQIF--GNFLYTCSADTTVRVYN 1562
Cdd:smart00320    7 TLKGHTGPVTSVAFSpdGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1530-1562 1.11e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 1.11e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2501356900 1530 GSFEGHQAAVNAIQI--FGNFLYTCSADTTVRVYN 1562
Cdd:pfam00400    5 KTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 530-681 4.11e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.21  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900  530 PRVLKENKTVSGTQKEPDEK---LNSTSQKAQDTVLQCPKTLQNPLPTTPKRTENDA---KESSVEESAKDSLSIESQPH 603
Cdd:pfam05109  572 PTLGKTSPTSAVTTPTPNATsptVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAvttGQHNITSSSTSSMSLRPSSI 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501356900  604 SAGNSAMTSDAEN---------HGIKSEGVASLTTevVSCSTHTVDKEQGSQIPGTPENLSAsPCNSTVLQKEAEVQVSA 674
Cdd:pfam05109  652 SETLSPSTSDNSTshmplltsaHPTGGENITQVTP--ASTSTHHVSTSSPAPRPGTTSQASG-PGNSSTSTKPGEVNVTK 728


                   ....*..
gi 2501356900  675 ATSPHSG 681
Cdd:pfam05109  729 GTPPKNA 735
 
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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