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Conserved domains on  [gi|568974666|ref|XP_006533724|]
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dynein axonemal intermediate chain 2 isoform X1 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 166-472 6.95e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 72.37  E-value: 6.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 166 THLSWHPDGNRkLAVAYS--CLKfqrapmsmnydsyIWDLENpNRPEIALK-PLSPLVTLEYNPkDSHVLLGGCYNGQIA 242
Cdd:cd00200   13 TCVAFSPDGKL-LATGSGdgTIK-------------VWDLET-GELLRTLKgHTGPVRDVAASA-DGTYLASGSSDKTIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 243 CWDTRKGSLVAELstieFSHRDPVYGTIWLQSktGTECFSASTDGQVMWWDIRkiSEPIEVVIMDISRkeqlenalGAIS 322
Cdd:cd00200   77 LWDLETGECVRTL----TGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVE--TGKCLTTLRGHTD--------WVNS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 323 LEFestLPTKFMVGTeqgivISCNRKAK---TQAEKIVCTFYGHHGPIYALQrnpFYPKN---FLTVGDWTARIWSEDSr 396
Cdd:cd00200  141 VAF---SPDGTFVAS-----SSQDGTIKlwdLRTGKCVATLTGHTGEVNSVA---FSPDGeklLSSSSDGTIKLWDLST- 208

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568974666 397 ESSIMWTKYHMAYLSDGAWSPVRpAVFFTTKMDGTLDIWDLVFKQCDPALSLKvcDDPLFCLRVQDNGCLIACGSE 472
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFSPDG-YLLASGSEDGTIRVWDLRTGECVQTLSGH--TNSVTSLAWSPDGKRLASGSA 281
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 166-472 6.95e-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: 72.37  E-value: 6.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 166 THLSWHPDGNRkLAVAYS--CLKfqrapmsmnydsyIWDLENpNRPEIALK-PLSPLVTLEYNPkDSHVLLGGCYNGQIA 242
Cdd:cd00200   13 TCVAFSPDGKL-LATGSGdgTIK-------------VWDLET-GELLRTLKgHTGPVRDVAASA-DGTYLASGSSDKTIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 243 CWDTRKGSLVAELstieFSHRDPVYGTIWLQSktGTECFSASTDGQVMWWDIRkiSEPIEVVIMDISRkeqlenalGAIS 322
Cdd:cd00200   77 LWDLETGECVRTL----TGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVE--TGKCLTTLRGHTD--------WVNS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 323 LEFestLPTKFMVGTeqgivISCNRKAK---TQAEKIVCTFYGHHGPIYALQrnpFYPKN---FLTVGDWTARIWSEDSr 396
Cdd:cd00200  141 VAF---SPDGTFVAS-----SSQDGTIKlwdLRTGKCVATLTGHTGEVNSVA---FSPDGeklLSSSSDGTIKLWDLST- 208

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568974666 397 ESSIMWTKYHMAYLSDGAWSPVRpAVFFTTKMDGTLDIWDLVFKQCDPALSLKvcDDPLFCLRVQDNGCLIACGSE 472
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFSPDG-YLLASGSEDGTIRVWDLRTGECVQTLSGH--TNSVTSLAWSPDGKRLASGSA 281
WD40 COG2319
WD40 repeat [General function prediction only];
150-437 2.04e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.76  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 150 KTINVF--RDPQEIKRTATH------LSWHPDGNRkLAVAysclkfqrapmsmNYDS--YIWDLENPNRPEIALKPLSPL 219
Cdd:COG2319  142 GTVRLWdlATGKLLRTLTGHsgavtsVAFSPDGKL-LASG-------------SDDGtvRLWDLATGKLLRTLTGHTGAV 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 220 VTLEYNPkDSHVLLGGCYNGQIACWDTRKGSLVAELSTiefsHRDPVYGTIWlqSKTGTECFSASTDGQVMWWDIRKiSE 299
Cdd:COG2319  208 RSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTG----HSGSVRSVAF--SPDGRLLASGSADGTVRLWDLAT-GE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 300 PIEVvimdisrkeqLENALGAI-SLEFeSTLPTKFMVGTEQGIVISCNrkakTQAEKIVCTFYGHHGPIYALQrnpFYPK 378
Cdd:COG2319  280 LLRT----------LTGHSGGVnSVAF-SPDGKLLASGSDDGTVRLWD----LATGKLLRTLTGHTGAVRSVA---FSPD 341

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974666 379 -NFLTVG--DWTARIWSEDSRESSIMWTKyHMAYLSDGAWSPvRPAVFFTTKMDGTLDIWDL 437
Cdd:COG2319  342 gKTLASGsdDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSP-DGRTLASGSADGTVRLWDL 401
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 166-472 6.95e-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: 72.37  E-value: 6.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 166 THLSWHPDGNRkLAVAYS--CLKfqrapmsmnydsyIWDLENpNRPEIALK-PLSPLVTLEYNPkDSHVLLGGCYNGQIA 242
Cdd:cd00200   13 TCVAFSPDGKL-LATGSGdgTIK-------------VWDLET-GELLRTLKgHTGPVRDVAASA-DGTYLASGSSDKTIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 243 CWDTRKGSLVAELstieFSHRDPVYGTIWLQSktGTECFSASTDGQVMWWDIRkiSEPIEVVIMDISRkeqlenalGAIS 322
Cdd:cd00200   77 LWDLETGECVRTL----TGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVE--TGKCLTTLRGHTD--------WVNS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 323 LEFestLPTKFMVGTeqgivISCNRKAK---TQAEKIVCTFYGHHGPIYALQrnpFYPKN---FLTVGDWTARIWSEDSr 396
Cdd:cd00200  141 VAF---SPDGTFVAS-----SSQDGTIKlwdLRTGKCVATLTGHTGEVNSVA---FSPDGeklLSSSSDGTIKLWDLST- 208

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568974666 397 ESSIMWTKYHMAYLSDGAWSPVRpAVFFTTKMDGTLDIWDLVFKQCDPALSLKvcDDPLFCLRVQDNGCLIACGSE 472
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFSPDG-YLLASGSEDGTIRVWDLRTGECVQTLSGH--TNSVTSLAWSPDGKRLASGSA 281
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 200-392 7.37e-11

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: 63.51  E-value: 7.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 200 IWDLENpNRPEIALK-PLSPLVTLEYNPkDSHVLLGGCYNGQIACWDTRKGSLVAELStiefSHRDPVYGTIWlqSKTGT 278
Cdd:cd00200  119 VWDVET-GKCLTTLRgHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRTGKCVATLT----GHTGEVNSVAF--SPDGE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 279 ECFSASTDGQVMWWDIRKISEpievvIMDISRKEQLENALgaislefestlptkfMVGTEQGIVISC--NRKAK---TQA 353
Cdd:cd00200  191 KLLSSSSDGTIKLWDLSTGKC-----LGTLRGHENGVNSV---------------AFSPDGYLLASGseDGTIRvwdLRT 250

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568974666 354 EKIVCTFYGHHGPIYALQrnpFYP-KNFLTVGDW--TARIWS 392
Cdd:cd00200  251 GECVQTLSGHTNSVTSLA---WSPdGKRLASGSAdgTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
150-437 2.04e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.76  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 150 KTINVF--RDPQEIKRTATH------LSWHPDGNRkLAVAysclkfqrapmsmNYDS--YIWDLENPNRPEIALKPLSPL 219
Cdd:COG2319  142 GTVRLWdlATGKLLRTLTGHsgavtsVAFSPDGKL-LASG-------------SDDGtvRLWDLATGKLLRTLTGHTGAV 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 220 VTLEYNPkDSHVLLGGCYNGQIACWDTRKGSLVAELSTiefsHRDPVYGTIWlqSKTGTECFSASTDGQVMWWDIRKiSE 299
Cdd:COG2319  208 RSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTG----HSGSVRSVAF--SPDGRLLASGSADGTVRLWDLAT-GE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 300 PIEVvimdisrkeqLENALGAI-SLEFeSTLPTKFMVGTEQGIVISCNrkakTQAEKIVCTFYGHHGPIYALQrnpFYPK 378
Cdd:COG2319  280 LLRT----------LTGHSGGVnSVAF-SPDGKLLASGSDDGTVRLWD----LATGKLLRTLTGHTGAVRSVA---FSPD 341

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974666 379 -NFLTVG--DWTARIWSEDSRESSIMWTKyHMAYLSDGAWSPvRPAVFFTTKMDGTLDIWDL 437
Cdd:COG2319  342 gKTLASGsdDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSP-DGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 150-293 9.96e-07

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: 50.80  E-value: 9.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 150 KTINVFrDPQEIKRTATH---------LSWHPDGNrKLAVAysclkfqrapmSMNYDSYIWDLenpnRPEIALKPL---- 216
Cdd:cd00200  157 GTIKLW-DLRTGKCVATLtghtgevnsVAFSPDGE-KLLSS-----------SSDGTIKLWDL----STGKCLGTLrghe 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568974666 217 SPLVTLEYNPkDSHVLLGGCYNGQIACWDTRKGSLVAELStiefSHRDPVYGTIWlqSKTGTECFSASTDGQVMWWD 293
Cdd:cd00200  220 NGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS----GHTNSVTSLAW--SPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 147-296 1.15e-06

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: 50.80  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 147 PSAKTINVFRDpqeIKRTATHLSWHPDGNRklaVAYSClkfqrapmsmnYDSYI--WDLENPNRPEIALKPLSPLVTLEY 224
Cdd:cd00200  123 ETGKCLTTLRG---HTDWVNSVAFSPDGTF---VASSS-----------QDGTIklWDLRTGKCVATLTGHTGEVNSVAF 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974666 225 NPKDSHVLLGGCyNGQIACWDTRKGSLVAELStiefSHRDPVYGTIWlqSKTGTECFSASTDGQVMWWDIRK 296
Cdd:cd00200  186 SPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLR----GHENGVNSVAF--SPDGYLLASGSEDGTIRVWDLRT 250
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 322-500 2.40e-06

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: 49.64  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 322 SLEFeSTLPTKFMVGTEQGIVISCNrkakTQAEKIVCTFYGHHGPIYALQRNPFYPKnFLTVG-DWTARIWSEDSRESSI 400
Cdd:cd00200   14 CVAF-SPDGKLLATGSGDGTIKVWD----LETGELLRTLKGHTGPVRDVAASADGTY-LASGSsDKTIRLWDLETGECVR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 401 MWTKyHMAYLSDGAWSPVRPaVFFTTKMDGTLDIWDLVFKQCdpALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTL-- 478
Cdd:cd00200   88 TLTG-HTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLwd 163

                        170       180
                 ....*....|....*....|..
gi 568974666 479 LEVSSSLSTLQRNEKNIASSIF 500
Cdd:cd00200  164 LRTGKCVATLTGHTGEVNSVAF 185
WD40 COG2319
WD40 repeat [General function prediction only];
150-295 1.02e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.90  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 150 KTINVFR-DPQEIKRTATH-------LSWHPDGNRkLAVAysclkfqrapmSMNYDSYIWDLENPNRPEIALKPLSPLVT 221
Cdd:COG2319  268 GTVRLWDlATGELLRTLTGhsggvnsVAFSPDGKL-LASG-----------SDDGTVRLWDLATGKLLRTLTGHTGAVRS 335

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568974666 222 LEYNPkDSHVLLGGCYNGQIACWDTRKGSLVAELStiefSHRDPVYGTIWlqSKTGTECFSASTDGQVMWWDIR 295
Cdd:COG2319  336 VAFSP-DGKTLASGSDDGTVRLWDLATGELLRTLT----GHTGAVTSVAF--SPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 357-483 1.92e-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: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974666 357 VCTFYGHHGPIYALQRNPfyPKNFLTVG--DWTARIWseDSRESSIMWT-KYHMAYLSDGAWSPVRPaVFFTTKMDGTLD 433
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSP--DGKLLATGsgDGTIKVW--DLETGELLRTlKGHTGPVRDVAASADGT-YLASGSSDKTIR 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568974666 434 IWDLVFKQCdpALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTLLEVSS 483
Cdd:cd00200   77 LWDLETGEC--VRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET 124
 
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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