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Conserved domains on  [gi|1907132192|ref|XP_036017433|]
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echinoderm microtubule-associated protein-like 3 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 218-286 3.06e-32

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


:

Pssm-ID: 460922  Cd Length: 72  Bit Score: 119.58  E-value: 3.06e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132192 218 KMFLRGRPITMYIPSGIRSLEELPS--GPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYR 286
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQkkEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
WD40 COG2319
WD40 repeat [General function prediction only];
506-870 2.33e-28

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.48  E-value: 2.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 506 TIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPgLVALQEAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRG 584
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAfSPDGKTLASGSADGTVRLW 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 585 DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEGHALAWSMDLKETGL-CADFHPSGAVVVVGLNTGR 662
Cdd:COG2319   148 DLATGkLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVrSVAFSPDGKLLASGSADGT 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 663 WLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFI 742
Cdd:COG2319   228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLT---GHSGGVNSVAFSPDGKLL 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 743 MSNSGDYEILYWDVAGGcKLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLF 822
Cdd:COG2319   304 ASGSDDGTVRLWDLATG-KLLR---------------TLTGHTGAVR----------SVAFSPDGKTLASGSDDGTVRLW 357

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1907132192 823 QypcARAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 870
Cdd:COG2319   358 D---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
300-626 8.47e-24

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.99  E-value: 8.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 300 RHYRGHTDCVRCLAVHPDGVRVASGqtaGVDKdgkplqpVVHIWDSETLLKLQEigLGAFERGVGALAFSAadQGAFLcv 379
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASG---SADG-------TVRLWDLATGKLLRT--LTGHSGAVTSVAFSP--DGKLL-- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 380 VDDSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 458
Cdd:COG2319   178 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGK------LLRTLTG------ 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 459 KPKFIPCFVFLPDGDIL-TGDSEGNILTWGRsvsdsktpgrggakETYTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 537
Cdd:COG2319   245 HSGSVRSVAFSPDGRLLaSGSADGTVRLWDL--------------ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 538 RLVQWGPGLVALQeAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 615
Cdd:COG2319   311 TVRLWDLATGKLL-RTLTGHTGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGeLLRTLTGHTGAVTSVAFSPDGRTLAS 389

                         330
                  ....*....|.
gi 1907132192 616 CGHDRQLCLWD 626
Cdd:COG2319   390 GSADGTVRLWD 400
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 6-34 7.60e-07

trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.


:

Pssm-ID: 409270  Cd Length: 48  Bit Score: 46.55  E-value: 7.60e-07
                          10        20
                  ....*....|....*....|....*....
gi 1907132192   6 GPGEGPAHETLQTLSQRLRVQEEEMELVK 34
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLK 29
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 218-286 3.06e-32

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


Pssm-ID: 460922  Cd Length: 72  Bit Score: 119.58  E-value: 3.06e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132192 218 KMFLRGRPITMYIPSGIRSLEELPS--GPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYR 286
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQkkEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
WD40 COG2319
WD40 repeat [General function prediction only];
506-870 2.33e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.48  E-value: 2.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 506 TIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPgLVALQEAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRG 584
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAfSPDGKTLASGSADGTVRLW 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 585 DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEGHALAWSMDLKETGL-CADFHPSGAVVVVGLNTGR 662
Cdd:COG2319   148 DLATGkLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVrSVAFSPDGKLLASGSADGT 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 663 WLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFI 742
Cdd:COG2319   228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLT---GHSGGVNSVAFSPDGKLL 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 743 MSNSGDYEILYWDVAGGcKLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLF 822
Cdd:COG2319   304 ASGSDDGTVRLWDLATG-KLLR---------------TLTGHTGAVR----------SVAFSPDGKTLASGSDDGTVRLW 357

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1907132192 823 QypcARAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 870
Cdd:COG2319   358 D---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 552-869 4.30e-27

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: 112.04  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 552 AEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQGFSP-VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEG 629
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVwDLETGELLrTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 630 HALAWSMDL-KETGLCADFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIY 708
Cdd:cd00200    83 GECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 709 SVSSCgtksSRFGRCMGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGcKLLrnryesrdrewatytCVLGFHVYGV 788
Cdd:cd00200   163 DLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCL---------------GTLRGHENGV 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 789 WpdgsdgtdinSLCRSHNERVVAVADDFCKVHLFQYpcaRAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 868
Cdd:cd00200   223 N----------SVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIW 288


                  .
gi 1907132192 869 R 869
Cdd:cd00200   289 D 289
WD40 COG2319
WD40 repeat [General function prediction only];
300-626 8.47e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.99  E-value: 8.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 300 RHYRGHTDCVRCLAVHPDGVRVASGqtaGVDKdgkplqpVVHIWDSETLLKLQEigLGAFERGVGALAFSAadQGAFLcv 379
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASG---SADG-------TVRLWDLATGKLLRT--LTGHSGAVTSVAFSP--DGKLL-- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 380 VDDSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 458
Cdd:COG2319   178 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGK------LLRTLTG------ 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 459 KPKFIPCFVFLPDGDIL-TGDSEGNILTWGRsvsdsktpgrggakETYTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 537
Cdd:COG2319   245 HSGSVRSVAFSPDGRLLaSGSADGTVRLWDL--------------ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 538 RLVQWGPGLVALQeAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 615
Cdd:COG2319   311 TVRLWDLATGKLL-RTLTGHTGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGeLLRTLTGHTGAVTSVAFSPDGRTLAS 389

                         330
                  ....*....|.
gi 1907132192 616 CGHDRQLCLWD 626
Cdd:COG2319   390 GSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 300-626 3.75e-20

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: 91.63  E-value: 3.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 300 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWDSETllKLQEIGLGAFERGVGALAFSAADQGAFLCv 379
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLET--GELLRTLKGHTGPVRDVAASADGTYLASG- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 380 vddSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 458
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGK------CLTTLRG------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 459 KPKFIPCFVFLPDGDILT-GDSEGNILTWgrsvsDSKTPgrggaketyTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 537
Cdd:cd00200   134 HTDWVNSVAFSPDGTFVAsSSQDGTIKLW-----DLRTG---------KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 538 RLVQWGPGLVALQeAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 615
Cdd:cd00200   200 TIKLWDLSTGKCL-GTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVwDLRTGeCVQTLSGHTNSVTSLAWSPDGKRLAS 278

                         330
                  ....*....|.
gi 1907132192 616 CGHDRQLCLWD 626
Cdd:cd00200   279 GSADGTIRIWD 289
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 6-34 7.60e-07

trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.


Pssm-ID: 409270  Cd Length: 48  Bit Score: 46.55  E-value: 7.60e-07
                          10        20
                  ....*....|....*....|....*....
gi 1907132192   6 GPGEGPAHETLQTLSQRLRVQEEEMELVK 34
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLK 29
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 593-626 3.11e-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: 41.91  E-value: 3.11e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907132192  593 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 626
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
593-626 2.82e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907132192 593 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 626
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 300-344 9.25e-04

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: 37.68  E-value: 9.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907132192  300 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 344
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
299-344 2.41e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907132192 299 QRHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 344
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASG-----SDDGT-----VKVWD 39
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 218-286 3.06e-32

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


Pssm-ID: 460922  Cd Length: 72  Bit Score: 119.58  E-value: 3.06e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132192 218 KMFLRGRPITMYIPSGIRSLEELPS--GPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYR 286
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQkkEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
WD40 COG2319
WD40 repeat [General function prediction only];
506-870 2.33e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.48  E-value: 2.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 506 TIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPgLVALQEAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRG 584
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAfSPDGKTLASGSADGTVRLW 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 585 DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEGHALAWSMDLKETGL-CADFHPSGAVVVVGLNTGR 662
Cdd:COG2319   148 DLATGkLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVrSVAFSPDGKLLASGSADGT 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 663 WLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFI 742
Cdd:COG2319   228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLT---GHSGGVNSVAFSPDGKLL 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 743 MSNSGDYEILYWDVAGGcKLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLF 822
Cdd:COG2319   304 ASGSDDGTVRLWDLATG-KLLR---------------TLTGHTGAVR----------SVAFSPDGKTLASGSDDGTVRLW 357

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1907132192 823 QypcARAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 870
Cdd:COG2319   358 D---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
312-758 1.35e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 116.16  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 312 LAVHPDGVRVASGQTAGVDKDGKPLQPVVHIWDSETLLKLQEigLGAFERGVGALAFSAADQGaflcVVDDSNEHMLSVW 391
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT--LLGHTAAVLSVAFSPDGRL----LASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 392 DCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkykKPKFIPCFVFLP 470
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGK------LLRTLTG------HSGAVTSVAFSP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 471 DGDIL-TGDSEGNILTWgrsvsDSKTPgrggaKETYTIvaqaHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWgpglval 549
Cdd:COG2319   173 DGKLLaSGSDDGTVRLW-----DLATG-----KLLRTL----TGHTGAVRSVAFSPDGKLLASGSADGTVRLW------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 550 qeaeipehfgavraiaeglgsellvgttknallrgDLAQGFSP-VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGE 628
Cdd:COG2319   232 -----------------------------------DLATGKLLrTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 629 GHALAWSMDLKETGLCA-DFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYI 707
Cdd:COG2319   277 TGELLRTLTGHSGGVNSvAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907132192 708 YSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAG 758
Cdd:COG2319   357 WDLAT-GELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 552-869 4.30e-27

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: 112.04  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 552 AEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQGFSP-VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEG 629
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVwDLETGELLrTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 630 HALAWSMDL-KETGLCADFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIY 708
Cdd:cd00200    83 GECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 709 SVSSCgtksSRFGRCMGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGcKLLrnryesrdrewatytCVLGFHVYGV 788
Cdd:cd00200   163 DLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCL---------------GTLRGHENGV 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 789 WpdgsdgtdinSLCRSHNERVVAVADDFCKVHLFQYpcaRAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 868
Cdd:cd00200   223 N----------SVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIW 288


                  .
gi 1907132192 869 R 869
Cdd:cd00200   289 D 289
WD40 COG2319
WD40 repeat [General function prediction only];
523-870 4.08e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 523 LRRDGTVLSGGGRDRRLVQWGPGLVALQEAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDEL 601
Cdd:COG2319     2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 602 WGLCTHPSQNRFLTCGHDRQLCLWDGE-GHALAWSMDLKETGLCADFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDG 680
Cdd:COG2319    82 LSVAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 681 NEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGc 760
Cdd:COG2319   162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLLRTLT---GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 761 KLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLFQypcARAKAPSRMYSGHG 840
Cdd:COG2319   237 KLLR---------------TLTGHSGSVR----------SVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHS 288

                         330       340       350
                  ....*....|....*....|....*....|
gi 1907132192 841 SHVTSVRFTHDDSYLVSlGGKDASIFQWRV 870
Cdd:COG2319   289 GGVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
WD40 COG2319
WD40 repeat [General function prediction only];
300-626 8.47e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.99  E-value: 8.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 300 RHYRGHTDCVRCLAVHPDGVRVASGqtaGVDKdgkplqpVVHIWDSETLLKLQEigLGAFERGVGALAFSAadQGAFLcv 379
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASG---SADG-------TVRLWDLATGKLLRT--LTGHSGAVTSVAFSP--DGKLL-- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 380 VDDSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 458
Cdd:COG2319   178 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGK------LLRTLTG------ 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 459 KPKFIPCFVFLPDGDIL-TGDSEGNILTWGRsvsdsktpgrggakETYTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 537
Cdd:COG2319   245 HSGSVRSVAFSPDGRLLaSGSADGTVRLWDL--------------ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 538 RLVQWGPGLVALQeAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 615
Cdd:COG2319   311 TVRLWDLATGKLL-RTLTGHTGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGeLLRTLTGHTGAVTSVAFSPDGRTLAS 389

                         330
                  ....*....|.
gi 1907132192 616 CGHDRQLCLWD 626
Cdd:COG2319   390 GSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 399-709 5.30e-21

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: 94.32  E-value: 5.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 399 LAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkykKPKFIPCFVFLPDGD-ILT 476
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSP-DGKLLATGSGDGtIKVWDLETGE------LLRTLKG------HTGPVRDVAASADGTyLAS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 477 GDSEGNILTWgrsvsDSKTPgrggaKETYTIvaqaHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWgPGLVALQEAEIPE 556
Cdd:cd00200    69 GSSDKTIRLW-----DLETG-----ECVRTL----TGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-DVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 557 HFGAVRAIAEGLGSELLVGTTKNALLR-GDLAQGfSPV--IQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD-GEGHAL 632
Cdd:cd00200   134 HTDWVNSVAFSPDGTFVASSSQDGTIKlWDLRTG-KCVatLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDlSTGKCL 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132192 633 AwSMDLKETGLCA-DFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYS 709
Cdd:cd00200   213 G-TLRGHENGVNSvAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 300-626 3.75e-20

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: 91.63  E-value: 3.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 300 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWDSETllKLQEIGLGAFERGVGALAFSAADQGAFLCv 379
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLET--GELLRTLKGHTGPVRDVAASADGTYLASG- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 380 vddSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 458
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGK------CLTTLRG------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 459 KPKFIPCFVFLPDGDILT-GDSEGNILTWgrsvsDSKTPgrggaketyTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 537
Cdd:cd00200   134 HTDWVNSVAFSPDGTFVAsSSQDGTIKLW-----DLRTG---------KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 538 RLVQWGPGLVALQeAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 615
Cdd:cd00200   200 TIKLWDLSTGKCL-GTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVwDLRTGeCVQTLSGHTNSVTSLAWSPDGKRLAS 278

                         330
                  ....*....|.
gi 1907132192 616 CGHDRQLCLWD 626
Cdd:cd00200   279 GSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 725-870 1.49e-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: 53.88  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132192 725 GHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGCKLLRNRyesrdrewatytcvlgfhvygvwpdGSDGTDINSLCRS 804
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK-------------------------GHTGPVRDVAASA 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132192 805 HNERVVAVADDFCkVHLFQYpcaRAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 870
Cdd:cd00200    62 DGTYLASGSSDKT-IRLWDL---ETGECVRTLTGHTSYVSSVAFSPDGRILSS-SSRDKTIKVWDV 122
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 6-34 7.60e-07

trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.


Pssm-ID: 409270  Cd Length: 48  Bit Score: 46.55  E-value: 7.60e-07
                          10        20
                  ....*....|....*....|....*....
gi 1907132192   6 GPGEGPAHETLQTLSQRLRVQEEEMELVK 34
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLK 29
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 593-626 3.11e-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: 41.91  E-value: 3.11e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907132192  593 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 626
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
593-626 2.82e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907132192 593 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 626
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 723-755 7.16e-04

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: 38.06  E-value: 7.16e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907132192  723 CMGHSSFITHLDWSKDGNFIMSNSGDYEILYWD 755
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 300-344 9.25e-04

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: 37.68  E-value: 9.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907132192  300 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 344
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
299-344 2.41e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907132192 299 QRHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 344
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASG-----SDDGT-----VKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 832-868 2.43e-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: 36.52  E-value: 2.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907132192  832 PSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 868
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
725-755 4.03e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 4.03e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907132192 725 GHSSFITHLDWSKDGNFIMSNSGDYEILYWD 755
Cdd:pfam00400   9 GHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
832-868 6.40e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 6.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907132192 832 PSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 868
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLAS-GSDDGTVKVW 38
 
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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