NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1168720165|ref|NP_001336705|]
View 

DDB1- and CUL4-associated factor 6 isoform f [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 5-145 5.25e-08

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: 55.03  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   5 NDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPPiPYYLAVGCSDSSVRIYDrrmlgtratgn 84
Cdd:cd00200   103 PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD-GTFVASSSQDGTIKLWD----------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168720165  85 yagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFDPkdDTARELKT 145
Cdd:cd00200   164 ----LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWDL--STGKCLGT 214
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 603-662 1.16e-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: 47.71  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 603 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
142-539 7.27e-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: 46.26  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 142 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 216
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 217 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 295
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 296 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVLSLHYSTegtttstikL 366
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLAARDSL---------L 623

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 367 NFTDEWSSIASSSRgigshcKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKF 445
Cdd:PRK14949  624 SDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSA 697

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 446 TAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETS 518
Cdd:PRK14949  698 PAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTA 770

                         410       420
                  ....*....|....*....|.
gi 1168720165 519 TRDSALQDTDDSDDDPVLIPG 539
Cdd:PRK14949  771 LTQTSSEVQDTELNLVLLSSG 791
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-145 5.25e-08

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: 55.03  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   5 NDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPPiPYYLAVGCSDSSVRIYDrrmlgtratgn 84
Cdd:cd00200   103 PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD-GTFVASSSQDGTIKLWD----------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168720165  85 yagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFDPkdDTARELKT 145
Cdd:cd00200   164 ----LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWDL--STGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 603-662 1.16e-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: 47.71  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 603 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 142-539 7.27e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 46.26  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 142 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 216
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 217 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 295
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 296 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVLSLHYSTegtttstikL 366
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLAARDSL---------L 623

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 367 NFTDEWSSIASSSRgigshcKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKF 445
Cdd:PRK14949  624 SDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSA 697

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 446 TAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETS 518
Cdd:PRK14949  698 PAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTA 770

                         410       420
                  ....*....|....*....|.
gi 1168720165 519 TRDSALQDTDDSDDDPVLIPG 539
Cdd:PRK14949  771 LTQTSSEVQDTELNLVLLSSG 791
WD40 COG2319
WD40 repeat [General function prediction only];
9-152 1.18e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   9 TFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgn 84
Cdd:COG2319   218 LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSVRSVAFSPD-GRLLASGSADGTVRLWDL---------- 275

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720165  85 yagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSSDY-IYLFDPkdDTARELKTPSAEERR 152
Cdd:COG2319   276 -----ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSDDGtVRLWDL--ATGKLLRTLTGHTGA 332
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 228-504 1.76e-04

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: 44.91  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 228 TSQSDISTLPTVPSS-PDLEVSETAMEVDTPAEQFLQPSTSSTmSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGH 306
Cdd:pfam05109 556 TSPTPAVTTPTPNATiPTLGKTSPTSAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQH 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 307 HTHHQSDSPSSVVNKQLGSMSLDEQQDNNNEKL----SPKPGTGEPVLSLhySTEGTTTSTIKLNFTDEWSSIASSSRGI 382
Cdd:pfam05109 635 NITSSSTSSMSLRPSSISETLSPSTSDNSTSHMplltSAHPTGGENITQV--TPASTSTHHVSTSSPAPRPGTTSQASGP 712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 383 GSHCKSEGQEESFVPQSSvqPPEGDSETKAPEESSEDV-TKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERND-- 459
Cdd:pfam05109 713 GNSSTSTKPGEVNVTKGT--PPKNATSPQAPSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTpr 790

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1168720165 460 LNLDRSCGVPEESASSEKAKEPETSDQTSTESATNENNTNPEPQF 504
Cdd:pfam05109 791 TRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRF 835
WD40 COG2319
WD40 repeat [General function prediction only];
609-663 6.66e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 6.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720165 609 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 663
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 623-662 3.09e-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: 35.75  E-value: 3.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1168720165  623 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
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 ...
 5-145 5.25e-08

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: 55.03  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   5 NDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPPiPYYLAVGCSDSSVRIYDrrmlgtratgn 84
Cdd:cd00200   103 PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD-GTFVASSSQDGTIKLWD----------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168720165  85 yagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFDPkdDTARELKT 145
Cdd:cd00200   164 ----LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWDL--STGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 6-128 1.03e-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: 48.10  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   6 DPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRRMLGTRATgny 85
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSPD-GYLLASGSEDGTIRVWDLRTGECVQT--- 256

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1168720165  86 agrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 128
Cdd:cd00200   257 ------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 603-662 1.16e-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: 47.71  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 603 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 142-539 7.27e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 46.26  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 142 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 216
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 217 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 295
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 296 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVLSLHYSTegtttstikL 366
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLAARDSL---------L 623

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 367 NFTDEWSSIASSSRgigshcKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKF 445
Cdd:PRK14949  624 SDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSA 697

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 446 TAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETS 518
Cdd:PRK14949  698 PAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTA 770

                         410       420
                  ....*....|....*....|.
gi 1168720165 519 TRDSALQDTDDSDDDPVLIPG 539
Cdd:PRK14949  771 LTQTSSEVQDTELNLVLLSSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 585-662 9.69e-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: 45.02  E-value: 9.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720165 585 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:cd00200     4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 COG2319
WD40 repeat [General function prediction only];
9-152 1.18e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   9 TFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgn 84
Cdd:COG2319   218 LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSVRSVAFSPD-GRLLASGSADGTVRLWDL---------- 275

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720165  85 yagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSSDY-IYLFDPkdDTARELKTPSAEERR 152
Cdd:COG2319   276 -----ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSDDGtVRLWDL--ATGKLLRTLTGHTGA 332
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 228-504 1.76e-04

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: 44.91  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 228 TSQSDISTLPTVPSS-PDLEVSETAMEVDTPAEQFLQPSTSSTmSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGH 306
Cdd:pfam05109 556 TSPTPAVTTPTPNATiPTLGKTSPTSAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQH 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 307 HTHHQSDSPSSVVNKQLGSMSLDEQQDNNNEKL----SPKPGTGEPVLSLhySTEGTTTSTIKLNFTDEWSSIASSSRGI 382
Cdd:pfam05109 635 NITSSSTSSMSLRPSSISETLSPSTSDNSTSHMplltSAHPTGGENITQV--TPASTSTHHVSTSSPAPRPGTTSQASGP 712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 383 GSHCKSEGQEESFVPQSSvqPPEGDSETKAPEESSEDV-TKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERND-- 459
Cdd:pfam05109 713 GNSSTSTKPGEVNVTKGT--PPKNATSPQAPSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTpr 790

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1168720165 460 LNLDRSCGVPEESASSEKAKEPETSDQTSTESATNENNTNPEPQF 504
Cdd:pfam05109 791 TRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRF 835
WD40 COG2319
WD40 repeat [General function prediction only];
9-145 2.10e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.52  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   9 TFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagr 88
Cdd:COG2319   260 LLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLA------------- 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720165  89 gtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YIYLFDPkdDTARELKT 145
Cdd:COG2319   319 --TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTVRLWDL--ATGELLRT 367
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 576-663 2.60e-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: 43.48  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 576 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 654
Cdd:cd00200   121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197


                  ....*....
gi 1168720165 655 DYDIKIWSP 663
Cdd:cd00200   198 DGTIKLWDL 206
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 605-662 5.73e-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: 42.71  E-value: 5.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720165 605 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:cd00200    64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
9-152 6.11e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   9 TFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAATSVAICPpipyYLAVGCSDSSVRIYDRRmlgtratgn 84
Cdd:COG2319   176 LLASGSDDGTVRLWDLAtgklLRT-----------LTGHTGAVRSVAFSPdg-kLLASGSADGTVRLWDLA--------- 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720165  85 yagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YIYLFDPkdDTARELKTPSAEERR 152
Cdd:COG2319   235 ------TGKLLRTLTGHSG----SVRSVAFSPDGR-LLASGSADgTVRLWDL--ATGELLRTLTGHSGG 290
WD40 COG2319
WD40 repeat [General function prediction only];
609-663 6.66e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 6.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720165 609 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 663
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 609-663 9.76e-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: 9.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720165 609 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 663
Cdd:cd00200   111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 COG2319
WD40 repeat [General function prediction only];
605-663 1.32e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720165 605 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 663
Cdd:COG2319   343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
PRK08581 PRK08581
amidase domain-containing protein;
228-506 1.97e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 41.31  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 228 TSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSP--TESPHSTPLLSSPDSEQRQSVEASG 305
Cdd:PRK08581   19 TLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQdnNDKKFSTIDSSTSDSNNIIDFIYKN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 306 HHThhQSDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTT--STIKLNFTDEWSSIASSSRGIG 383
Cdd:PRK08581   99 LPQ--TNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNsdSSIKNDTDTQSSKQDKADNQKA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 384 SHCKSEGQEESFVPQSSVQP--PEGDSETKAPEESSEDVTKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERNDLN 461
Cdd:PRK08581  177 PSSNNTKPSTSNKQPNSPKPtqPNQSNSQPASDDTANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQKDYASQSKKDKT 256

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1168720165 462 LDRSCGVPEESASSEKAKepETSDQTSTESATNENNTNPEPQFQT 506
Cdd:PRK08581  257 ETSNTKNPQLPTQDELKH--KSKPAQSFENDVNQSNTRSTSLFET 299
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 605-662 2.18e-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: 40.78  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720165 605 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:cd00200   232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 228-523 2.74e-03

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: 41.10  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 228 TSQSDISTLPTVPSSPdlevseTAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHH 307
Cdd:pfam17823 122 SPSSAAQSLPAAIAAL------PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 308 THHQSDSPSSVVNKQLGSMSldeqqdnnneklspKPGTGEPVLSLHYSTEGTTT----STIKLNFTDEWSSIASSSRGIG 383
Cdd:pfam17823 196 TTAASSAPATLTPARGISTA--------------ATATGHPAAGTALAAVGNSSpaagTVTAAVGTVTPAALATLAAAAG 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165 384 SHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQ-EG----VSAENPVENHinitqsdkfTAKPLDSNSGERN 458
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQaQGpiiqVSTDQPVHNT---------AGEPTPSPSNTTL 332

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720165 459 DLNLDRSCGVPEE---SASSEKAKEPETS------DQTSTESATNENNTNPEPQFQTEATG----PSAHEETSTRDSA 523
Cdd:pfam17823 333 EPNTPKSVASTNLavvTTTKAQAKEPSASpvpvlhTSMIPEVEATSPTTQPSPLLPTQGAAgpgiLLAPEQVATEATA 410
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 623-662 3.09e-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: 35.75  E-value: 3.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1168720165  623 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 662
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
605-663 3.71e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 3.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720165 605 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 663
Cdd:COG2319   301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
9-137 6.35e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720165   9 TFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAIcPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagr 88
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF-SPDGKTLASGSDDGTVRLWDLA------------- 360

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1168720165  89 gtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IYLFDPKD 137
Cdd:COG2319   361 --TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
609-663 7.29e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 7.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720165 609 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 663
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH