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Conserved domains on  [gi|1993776370|ref|NP_001380580|]
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DDB1- and CUL4-associated factor 6 isoform i [Homo sapiens]

Protein Classification

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 ...
 43-292 3.24e-22

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: 97.79  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200    78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200   147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                         250
                  ....*....|.
gi 1993776370 282 PkdDTARELKT 292
Cdd:cd00200   206 L--STGKCLGT 214
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
289-686 1.98e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14949:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 944  Bit Score: 48.57  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 443 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVL----SLhystegttts 509
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLaardSL---------- 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 510 tikLNFTDEWSSIASSSRgigshcKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQ 588
Cdd:PRK14949  623 ---LSDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLA 693

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 589 SDKFTAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAH 661
Cdd:PRK14949  694 SGSAPAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPA 766

                         410       420
                  ....*....|....*....|....*
gi 1993776370 662 EETSTRDSALQDTDDSDDDPVLIPG 686
Cdd:PRK14949  767 STTALTQTSSEVQDTELNLVLLSSG 791
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 764-823 2.10e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 47.33  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 764 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 43-292 3.24e-22

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: 97.79  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200    78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200   147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                         250
                  ....*....|.
gi 1993776370 282 PkdDTARELKT 292
Cdd:cd00200   206 L--STGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 8.17e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319   153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319   230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319   296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                         250
                  ....*....|....*
gi 1993776370 278 YLFDPkdDTARELKT 292
Cdd:COG2319   355 RLWDL--ATGELLRT 367
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 289-686 1.98e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 48.57  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 443 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVL----SLhystegttts 509
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLaardSL---------- 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 510 tikLNFTDEWSSIASSSRgigshcKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQ 588
Cdd:PRK14949  623 ---LSDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLA 693

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 589 SDKFTAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAH 661
Cdd:PRK14949  694 SGSAPAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPA 766

                         410       420
                  ....*....|....*....|....*
gi 1993776370 662 EETSTRDSALQDTDDSDDDPVLIPG 686
Cdd:PRK14949  767 STTALTQTSSEVQDTELNLVLLSSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 764-823 2.10e-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: 47.33  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 764 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 375-651 4.37e-05

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: 47.22  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 375 TSQSDISTLPTVPSS-PDLEVSETAMEVDTPAEQFLQPSTSSTmSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGH 453
Cdd:pfam05109 556 TSPTPAVTTPTPNATiPTLGKTSPTSAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQH 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 454 HTHHQSDSPSSVVNKQLGSMSLDEQQDNNNEKL----SPKPGTGEPVLSLhySTEGTTTSTIKLNFTDEWSSIASSSRGI 529
Cdd:pfam05109 635 NITSSSTSSMSLRPSSISETLSPSTSDNSTSHMplltSAHPTGGENITQV--TPASTSTHHVSTSSPAPRPGTTSQASGP 712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 530 GSHCKSEGQEESFVPQSSvqPPEGDSETKAPEESSEDV-TKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERND-- 606
Cdd:pfam05109 713 GNSSTSTKPGEVNVTKGT--PPKNATSPQAPSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTpr 790

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1993776370 607 LNLDRSCGVPEESASSEKAKEPETSDQTSTESATNENNTNPEPQF 651
Cdd:pfam05109 791 TRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRF 835
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 4.42e-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: 41.53  E-value: 4.42e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1993776370   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 pfam00400
WD domain, G-beta repeat;
42-77 3.17e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 3.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 COG2319
WD40 repeat [General function prediction only];
770-824 8.50e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776370 770 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 824
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 384-673 3.51e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 384 PTVPSSPD----LEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQ-RQSVEASGHHTHHQ 458
Cdd:NF033609  542 PVVPEQPDepgeIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSaSDSDSASDSDSASD 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 459 SDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQ 538
Cdd:NF033609  622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 539 EESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERNDLNLDRSCGVPEE 618
Cdd:NF033609  702 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 781

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776370 619 SASSEKAKEPETSDQTSTESATNENNTNPEPQFQTEATGPSAHEETSTRDSALQD 673
Cdd:NF033609  782 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 836
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 784-823 5.33e-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: 35.37  E-value: 5.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1993776370  784 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 43-292 3.24e-22

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: 97.79  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200    78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200   147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                         250
                  ....*....|.
gi 1993776370 282 PkdDTARELKT 292
Cdd:cd00200   206 L--STGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 46-275 1.80e-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: 83.92  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIFYtn 124
Cdd:cd00200    88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSP--DGTFVASSSQDGtIKLW-- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 125 veqDAETNRQCQ-FTCHYGttyEIMTVPNDP--YTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICP 201
Cdd:cd00200   163 ---DLRTGKCVAtLTGHTG---EVNSVAFSPdgEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSP 229

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993776370 202 PiPYYLAVGCSDSSVRIYDRRMLGTRATgnyagrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 275
Cdd:cd00200   230 D-GYLLASGSEDGTIRVWDLRTGECVQT---------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 8.17e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319   153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319   230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319   296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                         250
                  ....*....|....*
gi 1993776370 278 YLFDPkdDTARELKT 292
Cdd:COG2319   355 RLWDL--ATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
42-284 5.13e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 5.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI- 120
Cdd:COG2319   195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT-GHSGSVRSVAFSP--DGRLLASGSADGTVr 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 121 FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPnDPYTFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAI 199
Cdd:COG2319   272 LW-----DLATGELLRtLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 200 cPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IY 278
Cdd:COG2319   339 -SPDGKTLASGSDDGTVRLWDLA---------------TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVR 397


                  ....*.
gi 1993776370 279 LFDPKD 284
Cdd:COG2319   398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
42-299 1.18e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSP--DGKLLASGSDDGTVR 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 122 YTNVEQDAETNRqcqFTCHygtTYEIMTV---PNDPyTFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAA 194
Cdd:COG2319   188 LWDLATGKLLRT---LTGH---TGAVRSVafsPDGK-LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSV 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 195 TSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgnyagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSS 274
Cdd:COG2319   250 RSVAFSPD-GRLLASGSADGTVRLWDL---------------ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSD 308

                         250       260
                  ....*....|....*....|....*.
gi 1993776370 275 DY-IYLFDPkdDTARELKTPSAEERR 299
Cdd:COG2319   309 DGtVRLWDL--ATGKLLRTLTGHTGA 332
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 42-220 3.19e-15

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: 76.99  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:cd00200   126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSP--DGEKLLSSSSDGTIK 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 122 YTNVEQDAETnrqCQFTCHygtTYEIMTV--PNDPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAI 199
Cdd:cd00200   203 LWDLSTGKCL---GTLRGH---ENGVNSVafSPDGYLLASGSEDGTIRVWDLR-TGECVQT------LSGHTNSVTSLAW 269

                         170       180
                  ....*....|....*....|.
gi 1993776370 200 CPPIPyYLAVGCSDSSVRIYD 220
Cdd:cd00200   270 SPDGK-RLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 43-281 6.83e-15

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: 76.22  E-value: 6.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIF 121
Cdd:cd00200    43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSP--DGRILSSSSRDKtIKV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 122 YtnveqDAETNRQCQ-FTCHYGTtyeIMTVPNDPY-TFLSCG-EDGTVRWFDTRIKTSCTK-EDCKDDIlincrraaTSV 197
Cdd:cd00200   120 W-----DVETGKCLTtLRGHTDW---VNSVAFSPDgTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEV--------NSV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 198 AICpPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY- 276
Cdd:cd00200   184 AFS-PDGEKLLSSSSDGTIKLWDLS---------------TGKCLGTLRGHEN----GVNSVAFSPDGY-LLASGSEDGt 242


                  ....*
gi 1993776370 277 IYLFD 281
Cdd:cd00200   243 IRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 41-170 9.06e-13

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: 69.67  E-value: 9.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370  41 LKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI 120
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSP--DGYLLASGSEDGTI 243

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1993776370 121 -FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFD 170
Cdd:cd00200   244 rVW-----DLRTGECVQtLSGHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 289-686 1.98e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 48.57  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 443 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVL----SLhystegttts 509
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLaardSL---------- 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 510 tikLNFTDEWSSIASSSRgigshcKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQ 588
Cdd:PRK14949  623 ---LSDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLA 693

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 589 SDKFTAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAH 661
Cdd:PRK14949  694 SGSAPAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPA 766

                         410       420
                  ....*....|....*....|....*
gi 1993776370 662 EETSTRDSALQDTDDSDDDPVLIPG 686
Cdd:PRK14949  767 STTALTQTSSEVQDTELNLVLLSSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 764-823 2.10e-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: 47.33  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 764 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 375-651 4.37e-05

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: 47.22  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 375 TSQSDISTLPTVPSS-PDLEVSETAMEVDTPAEQFLQPSTSSTmSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGH 453
Cdd:pfam05109 556 TSPTPAVTTPTPNATiPTLGKTSPTSAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQH 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 454 HTHHQSDSPSSVVNKQLGSMSLDEQQDNNNEKL----SPKPGTGEPVLSLhySTEGTTTSTIKLNFTDEWSSIASSSRGI 529
Cdd:pfam05109 635 NITSSSTSSMSLRPSSISETLSPSTSDNSTSHMplltSAHPTGGENITQV--TPASTSTHHVSTSSPAPRPGTTSQASGP 712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 530 GSHCKSEGQEESFVPQSSvqPPEGDSETKAPEESSEDV-TKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERND-- 606
Cdd:pfam05109 713 GNSSTSTKPGEVNVTKGT--PPKNATSPQAPSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTpr 790

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1993776370 607 LNLDRSCGVPEESASSEKAKEPETSDQTSTESATNENNTNPEPQF 651
Cdd:pfam05109 791 TRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRF 835
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 4.42e-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: 41.53  E-value: 4.42e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1993776370   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 746-823 1.75e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 44.63  E-value: 1.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993776370 746 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:cd00200     4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 375-670 2.61e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 44.57  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 375 TSQSDISTLPTVPSSPdlevseTAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHH 454
Cdd:pfam17823 122 SPSSAAQSLPAAIAAL------PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 455 THHQSDSPSSVVNKQLGSMSldeqqdnnneklspKPGTGEPVLSLHYSTEGTTT----STIKLNFTDEWSSIASSSRGIG 530
Cdd:pfam17823 196 TTAASSAPATLTPARGISTA--------------ATATGHPAAGTALAAVGNSSpaagTVTAAVGTVTPAALATLAAAAG 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 531 SHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQ-EG----VSAENPVENHinitqsdkfTAKPLDSNSGERN 605
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQaQGpiiqVSTDQPVHNT---------AGEPTPSPSNTTL 332

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993776370 606 DLNLDRSCGVPEE---SASSEKAKEPETS------DQTSTESATNENNTNPEPQFQTEATG----PSAHEETSTRDSA 670
Cdd:pfam17823 333 EPNTPKSVASTNLavvTTTKAQAKEPSASpvpvlhTSMIPEVEATSPTTQPSPLLPTQGAAgpgiLLAPEQVATEATA 410
WD40 pfam00400
WD domain, G-beta repeat;
42-77 3.17e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 3.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1993776370  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 737-824 4.43e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.09  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 737 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 815
Cdd:cd00200   121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197


                  ....*....
gi 1993776370 816 DYDIKIWSP 824
Cdd:cd00200   198 DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
770-824 8.50e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776370 770 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 824
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
PRK08581 PRK08581
amidase domain-containing protein;
375-653 9.58e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 42.85  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 375 TSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSP--TESPHSTPLLSSPDSEQRQSVEASG 452
Cdd:PRK08581   19 TLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQdnNDKKFSTIDSSTSDSNNIIDFIYKN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 453 HHThhQSDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTT--STIKLNFTDEWSSIASSSRGIG 530
Cdd:PRK08581   99 LPQ--TNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNsdSSIKNDTDTQSSKQDKADNQKA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 531 SHCKSEGQEESFVPQSSVQP--PEGDSETKAPEESSEDVTKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERNDLN 608
Cdd:PRK08581  177 PSSNNTKPSTSNKQPNSPKPtqPNQSNSQPASDDTANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQKDYASQSKKDKT 256

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1993776370 609 LDRSCGVPEESASSEKAKepETSDQTSTESATNENNTNPEPQFQT 653
Cdd:PRK08581  257 ETSNTKNPQLPTQDELKH--KSKPAQSFENDVNQSNTRSTSLFET 299
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 766-823 9.84e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.94  E-value: 9.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1993776370 766 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:cd00200    64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
766-824 1.68e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1993776370 766 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 824
Cdd:COG2319   343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 770-824 1.75e-03

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.17  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776370 770 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 824
Cdd:cd00200   111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 384-673 3.51e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 384 PTVPSSPD----LEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQ-RQSVEASGHHTHHQ 458
Cdd:NF033609  542 PVVPEQPDepgeIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSaSDSDSASDSDSASD 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 459 SDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQ 538
Cdd:NF033609  622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776370 539 EESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERNDLNLDRSCGVPEE 618
Cdd:NF033609  702 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 781

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776370 619 SASSEKAKEPETSDQTSTESATNENNTNPEPQFQTEATGPSAHEETSTRDSALQD 673
Cdd:NF033609  782 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 836
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 766-823 3.58e-03

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 40.40  E-value: 3.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1993776370 766 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:cd00200   232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
766-824 4.71e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 4.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1993776370 766 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 824
Cdd:COG2319   301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 784-823 5.33e-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: 35.37  E-value: 5.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1993776370  784 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 823
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
770-824 9.25e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 9.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776370 770 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 824
Cdd:COG2319   221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275
 
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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