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Conserved domains on  [gi|1168720145|ref|NP_001336702|]
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DDB1- and CUL4-associated factor 6 isoform e [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 1.68e-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: 98.56  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200    78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200   147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                         250
                  ....*....|.
gi 1168720145 282 PkdDTARELKT 292
Cdd:cd00200   206 L--STGKCLGT 214
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 807-866 1.74e-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: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 807 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
394-743 1.29e-04

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: 45.87  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 394 VSETAMEVDTPAEQFLQPSTSSTM-----------SAQAHSTSSPTESPHSTPLLSSPDSEQR-QSVEASGHHTHHQSEF 461
Cdd:PRK14949  367 QVDDPAEISLPEGQTPSALAAAVQaphanepqfvnAAPAEKKTALTEQTTAQQQVQAANAEAVaEADASAEPADTVEQAL 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 462 lrGPEIALLrKRL---QQLRLKKAEQQ----------RQQELAAHTQQQPSTS------------DQSSHEGSSQDPHAS 516
Cdd:PRK14949  447 --DDESELL-AALnaeQAVILSQAQSQgfeasssldaDNSAVPEQIDSTAEQSvvnpsvtdtqvdDTSASNNSAADNTVD 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 517 DSPS---SVVNKQLGSM-------SLDEQQDNNNEKLSPKPGTGEPvLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI 586
Cdd:PRK14949  524 DNYSaedTLESNGLDEGdyaqdsaPLDAYQDDYVAFSSESYNALSD-DEQHSANVQSAQSAAEAQPSSQSLSPISAVTTA 602

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 587 -------------------------------GSHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAEN 635
Cdd:PRK14949  603 aasladddildavlaardsllsdldalspkeGDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELA 682

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 636 PVENHINI-TQSDKFTAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQ 707
Cdd:PRK14949  683 THQSVPEAaLASGSAPAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQ 755

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1168720145 708 FQTEATGPSAHEETSTRDSALQDTDDSDDDPVLIPG 743
Cdd:PRK14949  756 PQVQAEAQSPASTTALTQTSSEVQDTELNLVLLSSG 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 ...
 43-292 1.68e-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: 98.56  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200    78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200   147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                         250
                  ....*....|.
gi 1168720145 282 PkdDTARELKT 292
Cdd:cd00200   206 L--STGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 8.74e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 8.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319   153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319   230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319   296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                         250
                  ....*....|....*
gi 1168720145 278 YLFDPkdDTARELKT 292
Cdd:COG2319   355 RLWDL--ATGELLRT 367
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 807-866 1.74e-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: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 807 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 3.73e-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: 3.73e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1168720145   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 394-743 1.29e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 45.87  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 394 VSETAMEVDTPAEQFLQPSTSSTM-----------SAQAHSTSSPTESPHSTPLLSSPDSEQR-QSVEASGHHTHHQSEF 461
Cdd:PRK14949  367 QVDDPAEISLPEGQTPSALAAAVQaphanepqfvnAAPAEKKTALTEQTTAQQQVQAANAEAVaEADASAEPADTVEQAL 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 462 lrGPEIALLrKRL---QQLRLKKAEQQ----------RQQELAAHTQQQPSTS------------DQSSHEGSSQDPHAS 516
Cdd:PRK14949  447 --DDESELL-AALnaeQAVILSQAQSQgfeasssldaDNSAVPEQIDSTAEQSvvnpsvtdtqvdDTSASNNSAADNTVD 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 517 DSPS---SVVNKQLGSM-------SLDEQQDNNNEKLSPKPGTGEPvLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI 586
Cdd:PRK14949  524 DNYSaedTLESNGLDEGdyaqdsaPLDAYQDDYVAFSSESYNALSD-DEQHSANVQSAQSAAEAQPSSQSLSPISAVTTA 602

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 587 -------------------------------GSHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAEN 635
Cdd:PRK14949  603 aasladddildavlaardsllsdldalspkeGDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELA 682

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 636 PVENHINI-TQSDKFTAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQ 707
Cdd:PRK14949  683 THQSVPEAaLASGSAPAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQ 755

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1168720145 708 FQTEATGPSAHEETSTRDSALQDTDDSDDDPVLIPG 743
Cdd:PRK14949  756 PQVQAEAQSPASTTALTQTSSEVQDTELNLVLLSSG 791
WD40 pfam00400
WD domain, G-beta repeat;
42-77 2.67e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 2.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1168720145  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 COG2319
WD40 repeat [General function prediction only];
813-867 8.99e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720145 813 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 827-866 4.72e-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: 4.72e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1168720145  827 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
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 1.68e-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: 98.56  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200    78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200   147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                         250
                  ....*....|.
gi 1168720145 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 9.77e-18

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: 84.69  E-value: 9.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIFYtn 124
Cdd:cd00200    88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSP--DGTFVASSSQDGtIKLW-- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 125 veqDAETNRQCQ-FTCHYGttyEIMTVPNDP--YTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICP 201
Cdd:cd00200   163 ---DLRTGKCVAtLTGHTG---EVNSVAFSPdgEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSP 229

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168720145 202 PiPYYLAVGCSDSSVRIYDRRMLGTRATgnyagrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 275
Cdd:cd00200   230 D-GYLLASGSEDGTIRVWDLRTGECVQT---------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 8.74e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 8.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319   153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319   230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319   296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                         250
                  ....*....|....*
gi 1168720145 278 YLFDPkdDTARELKT 292
Cdd:COG2319   355 RLWDL--ATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
42-284 5.48e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 5.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI- 120
Cdd:COG2319   195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT-GHSGSVRSVAFSP--DGRLLASGSADGTVr 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 121 FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPnDPYTFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAI 199
Cdd:COG2319   272 LW-----DLATGELLRtLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 200 cPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IY 278
Cdd:COG2319   339 -SPDGKTLASGSDDGTVRLWDLA---------------TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVR 397


                  ....*.
gi 1168720145 279 LFDPKD 284
Cdd:COG2319   398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
42-299 1.26e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSP--DGKLLASGSDDGTVR 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 122 YTNVEQDAETNRqcqFTCHygtTYEIMTV---PNDPyTFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAA 194
Cdd:COG2319   188 LWDLATGKLLRT---LTGH---TGAVRSVafsPDGK-LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSV 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 195 TSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgnyagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSS 274
Cdd:COG2319   250 RSVAFSPD-GRLLASGSADGTVRLWDL---------------ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSD 308

                         250       260
                  ....*....|....*....|....*.
gi 1168720145 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 2.09e-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: 77.76  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:cd00200   126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSP--DGEKLLSSSSDGTIK 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 122 YTNVEQDAETnrqCQFTCHygtTYEIMTV--PNDPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAI 199
Cdd:cd00200   203 LWDLSTGKCL---GTLRGH---ENGVNSVafSPDGYLLASGSEDGTIRVWDLR-TGECVQT------LSGHTNSVTSLAW 269

                         170       180
                  ....*....|....*....|.
gi 1168720145 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 ...
 43-292 3.61e-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: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIF 121
Cdd:cd00200    43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSP--DGRILSSSSRDKtIKV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 122 YtnveqDAETNRQCQ-FTCHYGTtyeIMTVPNDPY-TFLSCG-EDGTVRWFDTRIKTSCTK-EDCKDDIlincrraaTSV 197
Cdd:cd00200   120 W-----DVETGKCLTtLRGHTDW---VNSVAFSPDgTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEV--------NSV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 198 AICpPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY- 276
Cdd:cd00200   184 AFS-PDGEKLLSSSSDGTIKLWDLS---------------TGKCLGTLRGHEN----GVNSVAFSPDGY-LLASGSEDGt 242

                         250
                  ....*....|....*.
gi 1168720145 277 IYLFDpkDDTARELKT 292
Cdd:cd00200   243 IRVWD--LRTGECVQT 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 41-170 6.64e-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: 70.44  E-value: 6.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145  41 LKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI 120
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSP--DGYLLASGSEDGTI 243

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1168720145 121 -FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFD 170
Cdd:cd00200   244 rVW-----DLRTGECVQtLSGHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 807-866 1.74e-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: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 807 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 3.73e-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: 3.73e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1168720145   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 394-743 1.29e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 45.87  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 394 VSETAMEVDTPAEQFLQPSTSSTM-----------SAQAHSTSSPTESPHSTPLLSSPDSEQR-QSVEASGHHTHHQSEF 461
Cdd:PRK14949  367 QVDDPAEISLPEGQTPSALAAAVQaphanepqfvnAAPAEKKTALTEQTTAQQQVQAANAEAVaEADASAEPADTVEQAL 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 462 lrGPEIALLrKRL---QQLRLKKAEQQ----------RQQELAAHTQQQPSTS------------DQSSHEGSSQDPHAS 516
Cdd:PRK14949  447 --DDESELL-AALnaeQAVILSQAQSQgfeasssldaDNSAVPEQIDSTAEQSvvnpsvtdtqvdDTSASNNSAADNTVD 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 517 DSPS---SVVNKQLGSM-------SLDEQQDNNNEKLSPKPGTGEPvLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI 586
Cdd:PRK14949  524 DNYSaedTLESNGLDEGdyaqdsaPLDAYQDDYVAFSSESYNALSD-DEQHSANVQSAQSAAEAQPSSQSLSPISAVTTA 602

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 587 -------------------------------GSHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAEN 635
Cdd:PRK14949  603 aasladddildavlaardsllsdldalspkeGDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELA 682

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 636 PVENHINI-TQSDKFTAKPLDSNsgerndlNLDRSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQ 707
Cdd:PRK14949  683 THQSVPEAaLASGSAPAPPPVPD-------PYDRPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQ 755

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1168720145 708 FQTEATGPSAHEETSTRDSALQDTDDSDDDPVLIPG 743
Cdd:PRK14949  756 PQVQAEAQSPASTTALTQTSSEVQDTELNLVLLSSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 789-866 1.48e-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: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720145 789 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200     4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 pfam00400
WD domain, G-beta repeat;
42-77 2.67e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 2.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1168720145  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 ...
 780-867 3.96e-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: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720145 780 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 858
Cdd:cd00200   121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197


                  ....*....
gi 1168720145 859 DYDIKIWSP 867
Cdd:cd00200   198 DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
813-867 8.99e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720145 813 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 809-866 9.02e-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: 42.32  E-value: 9.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720145 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200    64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 813-867 1.53e-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: 41.55  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720145 813 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:cd00200   111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 COG2319
WD40 repeat [General function prediction only];
809-867 1.78e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720145 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319   343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 809-866 3.28e-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: 3.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720145 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200   232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 827-866 4.72e-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: 4.72e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1168720145  827 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
809-867 4.98e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 4.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720145 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319   301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
 
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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