NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|221510715|ref|NP_610064|]
View 

outer segment 5 [Drosophila melanogaster]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 12822048)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
94-305 2.25e-23

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  94 TLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARWA 171
Cdd:COG2319  134 TLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 172 PNSNSIVFC-QGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAITS 249
Cdd:COG2319  214 PDGKLLASGsADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAtGELLRTLTGHSGGVNS 293

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221510715 250 VAFNPEKDYLLVGTF-NLLKLchsngWSYNT---ARFSSPRVGSIFNLSWSADGTQ-ATCG 305
Cdd:COG2319  294 VAFSPDGKLLASGSDdGTVRL-----WDLATgklLRTLTGHTGAVRSVAFSPDGKTlASGS 349
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 28-149 3.73e-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: 46.17  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  28 NCPLSCVDWSSNEEIYFV-SDDHQIFKWSDVSRDSVEVAKLPDDFVpTDMHWLLlggrssgggkgsDTLLI--CSNDGRF 104
Cdd:cd00200  177 TGEVNSVAFSPDGEKLLSsSSDGTIKLWDLSTGKCLGTLRGHENGV-NSVAFSP------------DGYLLasGSEDGTI 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 221510715 105 VILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:cd00200  244 RVWDlRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 588-753 1.28e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 588 FEESVLTFRSAGALLPVNVNMYCEILHRALLEGQWQQALKICRM-----GQHSSLWATLAAVATRKHQLQISEEAYSAAL 662
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERllklgPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 663 QIDKvsylqhlkaltpssaeQMAENSLMLGRMLEAEtillhgKKIEQAVGLalrmhnWRRALEISQKHKGEQPELVpRVL 742
Cdd:COG2956  172 KLDP----------------DCARALLLLAELYLEQ------GDYEEAIAA------LERALEQDPDYLPALPRLA-ELY 222

                        170
                 ....*....|.
gi 221510715 743 QERRKYLKALQ 753
Cdd:COG2956  223 EKLGDPEEALE 233
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
94-305 2.25e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  94 TLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARWA 171
Cdd:COG2319  134 TLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 172 PNSNSIVFC-QGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAITS 249
Cdd:COG2319  214 PDGKLLASGsADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAtGELLRTLTGHSGGVNS 293

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221510715 250 VAFNPEKDYLLVGTF-NLLKLchsngWSYNT---ARFSSPRVGSIFNLSWSADGTQ-ATCG 305
Cdd:COG2319  294 VAFSPDGKLLASGSDdGTVRL-----WDLATgklLRTLTGHTGAVRSVAFSPDGKTlASGS 349
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 115-313 6.92e-19

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: 87.78  E-value: 6.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 115 RSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWSRSGM-LRSTVVQNEESIRCARWAPNSNSIVFCQGGH-ISIKPLAA 192
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGeLLRTLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 193 NSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWD-AQGANLFTSAAEEYAITSVAFNPEKDYLLVGTFN-LLKLc 270
Cdd:cd00200   83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDvETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKL- 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 221510715 271 hsngWSYNTARFS---SPRVGSIFNLSWSADGTQATCGTSTGQLIV 313
Cdd:cd00200  162 ----WDLRTGKCVatlTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 110-149 7.58e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 7.58e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 221510715   110 SARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 28-149 3.73e-05

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 46.17  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  28 NCPLSCVDWSSNEEIYFV-SDDHQIFKWSDVSRDSVEVAKLPDDFVpTDMHWLLlggrssgggkgsDTLLI--CSNDGRF 104
Cdd:cd00200  177 TGEVNSVAFSPDGEKLLSsSSDGTIKLWDLSTGKCLGTLRGHENGV-NSVAFSP------------DGYLLasGSEDGTI 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 221510715 105 VILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:cd00200  244 RVWDlRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 pfam00400
WD domain, G-beta repeat;
115-149 1.70e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 221510715  115 RSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 588-753 1.28e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 588 FEESVLTFRSAGALLPVNVNMYCEILHRALLEGQWQQALKICRM-----GQHSSLWATLAAVATRKHQLQISEEAYSAAL 662
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERllklgPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 663 QIDKvsylqhlkaltpssaeQMAENSLMLGRMLEAEtillhgKKIEQAVGLalrmhnWRRALEISQKHKGEQPELVpRVL 742
Cdd:COG2956  172 KLDP----------------DCARALLLLAELYLEQ------GDYEEAIAA------LERALEQDPDYLPALPRLA-ELY 222

                        170
                 ....*....|.
gi 221510715 743 QERRKYLKALQ 753
Cdd:COG2956  223 EKLGDPEEALE 233
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
94-305 2.25e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  94 TLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARWA 171
Cdd:COG2319  134 TLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 172 PNSNSIVFC-QGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAITS 249
Cdd:COG2319  214 PDGKLLASGsADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAtGELLRTLTGHSGGVNS 293

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221510715 250 VAFNPEKDYLLVGTF-NLLKLchsngWSYNT---ARFSSPRVGSIFNLSWSADGTQ-ATCG 305
Cdd:COG2319  294 VAFSPDGKLLASGSDdGTVRL-----WDLATgklLRTLTGHTGAVRSVAFSPDGKTlASGS 349
WD40 COG2319
WD40 repeat [General function prediction only];
93-346 3.63e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 102.68  E-value: 3.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  93 DTLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARW 170
Cdd:COG2319   91 RLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAF 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 171 APNSNSIVF-CQGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAIT 248
Cdd:COG2319  171 SPDGKLLASgSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAtGKLLRTLTGHSGSVR 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 249 SVAFNPEKDYLLVGTF-NLLKLchsngWSYNT---ARFSSPRVGSIFNLSWSADGTQ-ATCG---------TSTGQLIVA 314
Cdd:COG2319  251 SVAFSPDGRLLASGSAdGTVRL-----WDLATgelLRTLTGHSGGVNSVAFSPDGKLlASGSddgtvrlwdLATGKLLRT 325

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 221510715 315 YAIEQQLVS-------GNLKATSKSRKSITLKDIATGTQ 346
Cdd:COG2319  326 LTGHTGAVRsvafspdGKTLASGSDDGTVRLWDLATGEL 364
WD40 COG2319
WD40 repeat [General function prediction only];
94-262 1.58e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.59  E-value: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  94 TLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARWA 171
Cdd:COG2319  218 LLASGSADGTVRLWDlATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDlATGELLRTLTGHSGGVNSVAFS 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 172 PNSNSIVF-CQGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAITS 249
Cdd:COG2319  298 PDGKLLASgSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAtGELLRTLTGHTGAVTS 377

                        170
                 ....*....|...
gi 221510715 250 VAFNPEKDYLLVG 262
Cdd:COG2319  378 VAFSPDGRTLASG 390
WD40 COG2319
WD40 repeat [General function prediction only];
99-346 2.54e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.13  E-value: 2.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  99 SNDGRFVILNKSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARWAPNSNSI 177
Cdd:COG2319   56 GDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 178 VF-CQGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAITSVAFNPE 255
Cdd:COG2319  136 ASgSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFSPD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 256 KDYLLVGTF-NLLKLchsngWSYNTARFSSPRVG---SIFNLSWSADGTQ-ATCG---------TSTGQLIVAYAIEQQL 321
Cdd:COG2319  216 GKLLASGSAdGTVRL-----WDLATGKLLRTLTGhsgSVRSVAFSPDGRLlASGSadgtvrlwdLATGELLRTLTGHSGG 290

                        250       260       270
                 ....*....|....*....|....*....|..
gi 221510715 322 VS-------GNLKATSKSRKSITLKDIATGTQ 346
Cdd:COG2319  291 VNsvafspdGKLLASGSDDGTVRLWDLATGKL 322
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 115-313 6.92e-19

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: 87.78  E-value: 6.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 115 RSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWSRSGM-LRSTVVQNEESIRCARWAPNSNSIVFCQGGH-ISIKPLAA 192
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGeLLRTLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 193 NSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWD-AQGANLFTSAAEEYAITSVAFNPEKDYLLVGTFN-LLKLc 270
Cdd:cd00200   83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDvETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKL- 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 221510715 271 hsngWSYNTARFS---SPRVGSIFNLSWSADGTQATCGTSTGQLIV 313
Cdd:cd00200  162 ----WDLRTGKCVatlTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
WD40 COG2319
WD40 repeat [General function prediction only];
94-234 4.13e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.19  E-value: 4.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  94 TLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARWA 171
Cdd:COG2319  260 LLASGSADGTVRLWDlATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHTGAVRSVAFS 339

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221510715 172 PNSNSIVF-CQGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQG 234
Cdd:COG2319  340 PDGKTLASgSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 18-265 1.22e-16

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: 81.23  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  18 KVEESSKSTTNC----PLSCVDWSSN-EEIYFVSDDHQIFKWSDVSRDSVE-----------VAKLPDDFVptdmhwlll 81
Cdd:cd00200   37 DLETGELLRTLKghtgPVRDVAASADgTYLASGSSDKTIRLWDLETGECVRtltghtsyvssVAFSPDGRI--------- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  82 ggrssgggkgsdtLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVV 159
Cdd:cd00200  108 -------------LSSSSRDKTIKVWDvETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDlRTGKCVATLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 160 QNEESIRCARWAPNSNSIVFCqgghisikplAANSKIIRW-----------RAHDGLVLSLSWSTQSNIIASGGEDFRFK 228
Cdd:cd00200  175 GHTGEVNSVAFSPDGEKLLSS----------SSDGTIKLWdlstgkclgtlRGHENGVNSVAFSPDGYLLASGSEDGTIR 244

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 221510715 229 IWDAQ-GANLFTSAAEEYAITSVAFNPEKDYLLVGTFN 265
Cdd:cd00200  245 VWDLRtGECVQTLSGHTNSVTSLAWSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 93-231 6.42e-16

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: 78.92  E-value: 6.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  93 DTLLICSNDGrFVIL--NKSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCAR 169
Cdd:cd00200  148 TFVASSSQDG-TIKLwdLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDlSTGKCLGTLRGHENGVNSVA 226

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221510715 170 WAPNSNSIVFC-QGGHISIKPLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWD 231
Cdd:cd00200  227 FSPDGYLLASGsEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 93-313 1.17e-14

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.06  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  93 DTLLICSNDGRFVILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS-RSGMLRSTVVQNEESIRCARW 170
Cdd:cd00200   22 KLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDlETGECVRTLTGHTSYVSSVAF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 171 APNsNSIVFCQGGHISIK--PLAANSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWDAQGANLF-TSAAEEYAI 247
Cdd:cd00200  102 SPD-GRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVaTLTGHTGEV 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 248 TSVAFNPEKDYLLVGTF-NLLKLchsngWSYNTARFSSPRVG---SIFNLSWSADGTQATCGTSTGQLIV 313
Cdd:cd00200  181 NSVAFSPDGEKLLSSSSdGTIKL-----WDLSTGKCLGTLRGhenGVNSVAFSPDGYLLASGSEDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
128-346 1.93e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.15  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 128 RWSPDGAGLLTAGEDGVIKIW--SRSGMLRSTVVQNEESIRCARWAPNSNSIVFCQGGHISIKPLAANSKIIRWRAHDGL 205
Cdd:COG2319    1 ALSADGAALAAASADLALALLaaALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 206 VLSLSWSTQSNIIASGGEDFRFKIWDAQ-GANLFTSAAEEYAITSVAFNPEKDYLLVGTF-NLLKLchsngWSYNT---- 279
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAdGTVRL-----WDLATgkll 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 280 ARFSSPRvGSIFNLSWSADGTQ-ATCG---------TSTGQLIVAYAIEQQLVS-------GNLKATSKSRKSITLKDIA 342
Cdd:COG2319  156 RTLTGHS-GAVTSVAFSPDGKLlASGSddgtvrlwdLATGKLLRTLTGHTGAVRsvafspdGKLLASGSADGTVRLWDLA 234


                 ....
gi 221510715 343 TGTQ 346
Cdd:COG2319  235 TGKL 238
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 110-149 7.58e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 7.58e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 221510715   110 SARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 194-231 3.54e-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: 3.54e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 221510715   194 SKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWD 231
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 28-149 3.73e-05

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 46.17  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715  28 NCPLSCVDWSSNEEIYFV-SDDHQIFKWSDVSRDSVEVAKLPDDFVpTDMHWLLlggrssgggkgsDTLLI--CSNDGRF 104
Cdd:cd00200  177 TGEVNSVAFSPDGEKLLSsSSDGTIKLWDLSTGKCLGTLRGHENGV-NSVAFSP------------DGYLLasGSEDGTI 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 221510715 105 VILN-KSARVERSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:cd00200  244 RVWDlRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 pfam00400
WD domain, G-beta repeat;
115-149 1.70e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 221510715  115 RSISAHAAAISSGRWSPDGAGLLTAGEDGVIKIWS 149
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
193-231 2.13e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 2.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 221510715  193 NSKIIRWRAHDGLVLSLSWSTQSNIIASGGEDFRFKIWD 231
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 588-753 1.28e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 588 FEESVLTFRSAGALLPVNVNMYCEILHRALLEGQWQQALKICRM-----GQHSSLWATLAAVATRKHQLQISEEAYSAAL 662
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERllklgPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 663 QIDKvsylqhlkaltpssaeQMAENSLMLGRMLEAEtillhgKKIEQAVGLalrmhnWRRALEISQKHKGEQPELVpRVL 742
Cdd:COG2956  172 KLDP----------------DCARALLLLAELYLEQ------GDYEEAIAA------LERALEQDPDYLPALPRLA-ELY 222

                        170
                 ....*....|.
gi 221510715 743 QERRKYLKALQ 753
Cdd:COG2956  223 EKLGDPEEALE 233
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 588-763 8.44e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 8.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 588 FEESVLTFRSAGALLPVNVNMYCEILHRALLEGQWQQALKICRM-----GQHSSLWATLAAVATRKHQLQISEEAYSAAL 662
Cdd:COG3914   94 YEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRalalnPDFAEAYLNLGEALRRLGRLEEAIAALRRAL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221510715 663 QIDKvsylQHLKALtpssaeqmaensLMLGRMLEAEtillhgKKIEQAVGLAlrmhnwRRALEISQKHKGEQPELVP--- 739
Cdd:COG3914  174 ELDP----DNAEAL------------NNLGNALQDL------GRLEEAIAAY------RRALELDPDNADAHSNLLFalr 225

                        170       180       190
                 ....*....|....*....|....*....|.
gi 221510715 740 -----RVLQERRKYLKALQR--EEWDPLYLP 763
Cdd:COG3914  226 qacdwEVYDRFEELLAALARgpSELSPFALL 256
 
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