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Conserved domains on  [gi|147900490|ref|NP_001090336|]
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WD repeat domain 54 L homeolog [Xenopus laevis]

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

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
132-286 2.00e-11

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 64.55  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 132 GQYICVGTSSGLVLVFDIPAKgtniTLAEVLAEHREPITDIA--SDSATdkdsaadLVTADDSGALCVWKCGGGEEFKLL 209
Cdd:COG2319  258 GRLLASGSADGTVRLWDLATG----ELLRTLTGHSGGVNSVAfsPDGKL-------LASGSDDGTVRLWDLATGKLLRTL 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147900490 210 N--KISAYGVSCSSVKLWngvIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLS 286
Cdd:COG2319  327 TghTGAVRSVAFSPDGKT---LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 248-327 3.91e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 41.55  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 248 LNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLSRSDCGTIEVEhcHSECVTDTQICgarfcdPQGGSFAVTGYD 327
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG--HTGPVRDVAAS------ADGTYLASGSSD 72
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
132-286 2.00e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 64.55  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 132 GQYICVGTSSGLVLVFDIPAKgtniTLAEVLAEHREPITDIA--SDSATdkdsaadLVTADDSGALCVWKCGGGEEFKLL 209
Cdd:COG2319  258 GRLLASGSADGTVRLWDLATG----ELLRTLTGHSGGVNSVAfsPDGKL-------LASGSDDGTVRLWDLATGKLLRTL 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147900490 210 N--KISAYGVSCSSVKLWngvIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLS 286
Cdd:COG2319  327 TghTGAVRSVAFSPDGKT---LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 161-305 4.25e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.88  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 161 VLAEHREPITDIASDSATDKdsaadLVTADDSGALCVWKCGGGEEFKLL--NKISAYGVSCSSvklWNGVIAAAYGTGQI 238
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKL-----LATGSGDGTIKVWDLETGELLRTLkgHTGPVRDVAASA---DGTYLASGSSDKTI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147900490 239 RVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLSRSDCGTieVEHCHSECVTD 305
Cdd:cd00200   76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNS 140
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 248-327 3.91e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.55  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 248 LNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLSRSDCGTIEVEhcHSECVTDTQICgarfcdPQGGSFAVTGYD 327
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG--HTGPVRDVAAS------ADGTYLASGSSD 72
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 225-327 5.89e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 41.61  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 225 WNGVI----AAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLL-SGAEDSFIQIWQLSRS-DCGTIEvehc 298
Cdd:PLN00181 540 WNSYIksqvASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGvSIGTIK---- 615

                         90       100
                 ....*....|....*....|....*....
gi 147900490 299 hsecvTDTQICGARFCDPQGGSFAVTGYD 327
Cdd:PLN00181 616 -----TKANICCVQFPSESGRSLAFGSAD 639
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
132-286 2.00e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 64.55  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 132 GQYICVGTSSGLVLVFDIPAKgtniTLAEVLAEHREPITDIA--SDSATdkdsaadLVTADDSGALCVWKCGGGEEFKLL 209
Cdd:COG2319  258 GRLLASGSADGTVRLWDLATG----ELLRTLTGHSGGVNSVAfsPDGKL-------LASGSDDGTVRLWDLATGKLLRTL 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147900490 210 N--KISAYGVSCSSVKLWngvIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLS 286
Cdd:COG2319  327 TghTGAVRSVAFSPDGKT---LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
132-297 1.67e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 132 GQYICVGTSSGLVLVFDIPAKgtniTLAEVLAEHREPITDIA--SDSATdkdsaadLVTADDSGALCVWKCGGGEEFKLL 209
Cdd:COG2319  216 GKLLASGSADGTVRLWDLATG----KLLRTLTGHSGSVRSVAfsPDGRL-------LASGSADGTVRLWDLATGELLRTL 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 210 NKISA--YGVSCSSvklwNG-VIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLS 286
Cdd:COG2319  285 TGHSGgvNSVAFSP----DGkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360

                        170
                 ....*....|.
gi 147900490 287 RSDCGTIEVEH 297
Cdd:COG2319  361 TGELLRTLTGH 371
WD40 COG2319
WD40 repeat [General function prediction only];
128-327 1.00e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.15  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 128 APARGQYICVGTSSGLVLVFDIPAKgtniTLAEVLAEHREPITDIA--SDSATdkdsaadLVTADDSGALCVWKCGGGEE 205
Cdd:COG2319   86 FSPDGRLLASASADGTVRLWDLATG----LLLRTLTGHTGAVRSVAfsPDGKT-------LASGSADGTVRLWDLATGKL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 206 FKLLN--KISAYGVSCSSvklwNG-VIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQI 282
Cdd:COG2319  155 LRTLTghSGAVTSVAFSP----DGkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 147900490 283 WQLSRSDCGTIEVEHchsecvtDTQICGARFcDPQGGSFAVTGYD 327
Cdd:COG2319  231 WDLATGKLLRTLTGH-------SGSVRSVAF-SPDGRLLASGSAD 267
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 161-305 4.25e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.88  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 161 VLAEHREPITDIASDSATDKdsaadLVTADDSGALCVWKCGGGEEFKLL--NKISAYGVSCSSvklWNGVIAAAYGTGQI 238
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKL-----LATGSGDGTIKVWDLETGELLRTLkgHTGPVRDVAASA---DGTYLASGSSDKTI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147900490 239 RVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLSRSDCGTieVEHCHSECVTD 305
Cdd:cd00200   76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNS 140
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 132-284 5.34e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 5.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 132 GQYICVGTSSGLVLVFDIpakgTNITLAEVLAEHREPITDIASDsatdkDSAADLVTADDSGALCVWKCGGGEEFKLLnK 211
Cdd:cd00200  147 GTFVASSSQDGTIKLWDL----RTGKCVATLTGHTGEVNSVAFS-----PDGEKLLSSSSDGTIKLWDLSTGKCLGTL-R 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147900490 212 ISAYGVSCSSVKLWNGVIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQ 284
Cdd:cd00200  217 GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 100-290 1.00e-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: 52.72  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 100 SDGSIMVY-WHALDALETPPAQAVFARGIA-PARGQYICVGTSSGLVLVFDIPAKgtniTLAEVLAEHREPITDIASDSA 177
Cdd:cd00200   29 GDGTIKVWdLETGELLRTLKGHTGPVRDVAaSADGTYLASGSSDKTIRLWDLETG----ECVRTLTGHTSYVSSVAFSPD 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 178 TDKdsaadLVTADDSGALCVWKCGGGEEFKLLNKISAYgVSCSSVKLWNGVIAAAYGTGQIRVFDAATGALNVEVDAHAR 257
Cdd:cd00200  105 GRI-----LSSSSRDKTIKVWDVETGKCLTTLRGHTDW-VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTG 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 147900490 258 WIYTLDIAPESGKLLSGAEDSFIQIWQLSRSDC 290
Cdd:cd00200  179 EVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC 211
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 132-327 3.27e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.94  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 132 GQYICVGTSSGLVLVFDIPaKGTNITlaeVLAEHREPITDIASDSatDKDSaadLVTADDSGALCVWKcggGEEFKLLNK 211
Cdd:cd00200  105 GRILSSSSRDKTIKVWDVE-TGKCLT---TLRGHTDWVNSVAFSP--DGTF---VASSSQDGTIKLWD---LRTGKCVAT 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 212 ISAY--GVSCSSVKLWNGVIAAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLSRSD 289
Cdd:cd00200  173 LTGHtgEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE 252

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 147900490 290 C-GTIEvehCHSECVTDTQicgarfCDPQGGSFAVTGYD 327
Cdd:cd00200  253 CvQTLS---GHTNSVTSLA------WSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 248-327 3.91e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.55  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 248 LNVEVDAHARWIYTLDIAPESGKLLSGAEDSFIQIWQLSRSDCGTIEVEhcHSECVTDTQICgarfcdPQGGSFAVTGYD 327
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG--HTGPVRDVAAS------ADGTYLASGSSD 72
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 225-327 5.89e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 41.61  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147900490 225 WNGVI----AAAYGTGQIRVFDAATGALNVEVDAHARWIYTLDIAPESGKLL-SGAEDSFIQIWQLSRS-DCGTIEvehc 298
Cdd:PLN00181 540 WNSYIksqvASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGvSIGTIK---- 615

                         90       100
                 ....*....|....*....|....*....
gi 147900490 299 hsecvTDTQICGARFCDPQGGSFAVTGYD 327
Cdd:PLN00181 616 -----TKANICCVQFPSESGRSLAFGSAD 639
 
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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