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Conserved domains on  [gi|442632382|ref|NP_001261851|]
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Doublecortin-domain-containing echinoderm-microtubule-associated protein, isoform F [Drosophila melanogaster]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 13018732)

WD40 repeat domain-containing protein similar to proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

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 ...
 224-290 6.83e-31

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: 115.73  E-value: 6.83e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632382  224 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 290
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
323-734 2.01e-25

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 323 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 402
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 403 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 481
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 482 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 559
Cdd:COG2319  155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 560 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 629
Cdd:COG2319  226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 630 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 708
Cdd:COG2319  302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                        410       420
                 ....*....|....*....|....*.
gi 442632382 709 LDWSMDGNFVQTVTIDFDLLFWDAKS 734
Cdd:COG2319  378 VAFSPDGRTLASGSADGTVRLWDLAT 403
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 75-147 1.66e-23

Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.


:

Pssm-ID: 340590  Cd Length: 69  Bit Score: 94.62  E-value: 1.66e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632382  75 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 147
Cdd:cd17070    1 KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLK-GPVRKLYTTDGKKVESLSAL---FHGPDEYVAA 69
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 622-848 2.10e-09

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: 59.66  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 622 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 700
Cdd:cd00200   14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 701 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 779
Cdd:cd00200   90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632382 780 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 848
Cdd:cd00200  142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
WD40 pfam00400
WD domain, G-beta repeat;
295-337 5.67e-03

WD domain, G-beta repeat;


:

Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 5.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 442632382  295 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 337
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 224-290 6.83e-31

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: 115.73  E-value: 6.83e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632382  224 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 290
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
323-734 2.01e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 323 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 402
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 403 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 481
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 482 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 559
Cdd:COG2319  155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 560 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 629
Cdd:COG2319  226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 630 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 708
Cdd:COG2319  302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                        410       420
                 ....*....|....*....|....*.
gi 442632382 709 LDWSMDGNFVQTVTIDFDLLFWDAKS 734
Cdd:COG2319  378 VAFSPDGRTLASGSADGTVRLWDLAT 403
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 75-147 1.66e-23

Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.


Pssm-ID: 340590  Cd Length: 69  Bit Score: 94.62  E-value: 1.66e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632382  75 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 147
Cdd:cd17070    1 KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLK-GPVRKLYTTDGKKVESLSAL---FHGPDEYVAA 69
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 296-686 1.30e-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: 95.86  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 296 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFgmGELDSGVTAVAFSqlNGGSYILAvdS 375
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG---SGDGT----IKVWDLETGELLRTL--KGHTGPVRDVAAS--ADGTYLAS--G 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 376 GRESILSVWQWQWGHLLGKVatlqeglsgaafhplddnliithgRGHlafwhrrkdgffertdivkqpsRSHVTSVQFEP 455
Cdd:cd00200   70 SSDKTIRLWDLETGECVRTL------------------------TGH----------------------TSYVSSVAFSP 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 456 DGDVITADS-DGFITIYSVDSdgaYFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqnykkiadtklpeaa 534
Cdd:cd00200  104 DGRILSSSSrDKTIKVWDVET---GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD----------------- 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 535 ggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWRKNKLIWtI 614
Cdd:cd00200  164 --LRT------------------------GKCVATLT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-L 212

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632382 615 QT----GYECVALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFR 686
Cdd:cd00200  213 GTlrghENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 622-848 2.10e-09

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: 59.66  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 622 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 700
Cdd:cd00200   14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 701 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 779
Cdd:cd00200   90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632382 780 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 848
Cdd:cd00200  142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 75-150 2.63e-06

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 46.10  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382    75 RVIRIINNLD---HSVqcRVLLNLRTSQPFEEVLEDLGQVLKIN---GAKKMYTGTGQEVRSFSQLRNefadvDTFYLAT 148
Cdd:smart00537   6 KRIRFYRNGDrffKGV--RLVVNRKRFKSFEALLQDLTEVVKLDlphGVRKLYTLDGKKVTSLDELED-----GGSYVAS 78


                   ..
gi 442632382   149 GT 150
Cdd:smart00537  79 GT 80
WD40 pfam00400
WD domain, G-beta repeat;
295-337 5.67e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 5.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 442632382  295 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 337
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 296-337 6.55e-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: 34.98  E-value: 6.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442632382   296 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWS 337
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASG---SDDGT----IKLWD 40
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 224-290 6.83e-31

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: 115.73  E-value: 6.83e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632382  224 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 290
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
323-734 2.01e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 323 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 402
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 403 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 481
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 482 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 559
Cdd:COG2319  155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 560 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 629
Cdd:COG2319  226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 630 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 708
Cdd:COG2319  302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                        410       420
                 ....*....|....*....|....*.
gi 442632382 709 LDWSMDGNFVQTVTIDFDLLFWDAKS 734
Cdd:COG2319  378 VAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
283-688 6.68e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.99  E-value: 6.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 283 AVAVLFDRDEDAQRHYTGHTEDIMCMDVHPSRELVASGQKAGRdrksqahVRIWSTESLQTLYVFGmgELDSGVTAVAFS 362
Cdd:COG2319   59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT-------VRLWDLATGLLLRTLT--GHTGAVRSVAFS 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 363 QlnGGSYILAVDSGREsiLSVWQWQWGHLLGKVATLQEGLSGAAFHPlDDNLIITHGR-GHLAFWHRRKDGFFERTdivk 441
Cdd:COG2319  130 P--DGKTLASGSADGT--VRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDdGTVRLWDLATGKLLRTL---- 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 442 QPSRSHVTSVQFEPDGDVI-TADSDGFITIYSVDSDGayfVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslq 520
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD--- 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 521 nykkiadtklpeaaggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDK 600
Cdd:COG2319  275 ----------------LAT------------------------GELLRTLT----GHSGGVNSVAFSPDGKLLASGSDDG 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 601 HVALW--RKNKLIWTIQTGYECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMG 676
Cdd:COG2319  311 TVRLWdlATGKLLRTLTGHTGAVrSVAFSPDGkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASG 390

                        410
                 ....*....|..
gi 442632382 677 SQNGSIYLFRVS 688
Cdd:COG2319  391 SADGTVRLWDLA 402
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 75-147 1.66e-23

Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.


Pssm-ID: 340590  Cd Length: 69  Bit Score: 94.62  E-value: 1.66e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632382  75 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 147
Cdd:cd17070    1 KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLK-GPVRKLYTTDGKKVESLSAL---FHGPDEYVAA 69
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 296-686 1.30e-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: 95.86  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 296 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFgmGELDSGVTAVAFSqlNGGSYILAvdS 375
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG---SGDGT----IKVWDLETGELLRTL--KGHTGPVRDVAAS--ADGTYLAS--G 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 376 GRESILSVWQWQWGHLLGKVatlqeglsgaafhplddnliithgRGHlafwhrrkdgffertdivkqpsRSHVTSVQFEP 455
Cdd:cd00200   70 SSDKTIRLWDLETGECVRTL------------------------TGH----------------------TSYVSSVAFSP 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 456 DGDVITADS-DGFITIYSVDSdgaYFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqnykkiadtklpeaa 534
Cdd:cd00200  104 DGRILSSSSrDKTIKVWDVET---GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD----------------- 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 535 ggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWRKNKLIWtI 614
Cdd:cd00200  164 --LRT------------------------GKCVATLT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-L 212

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632382 615 QT----GYECVALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFR 686
Cdd:cd00200  213 GTlrghENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 448-731 2.15e-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: 92.40  E-value: 2.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 448 VTSVQFEPDGDVI-TADSDGFITIYSVDSDgayFVRTEFEAHNKGIGCLIMLGEGT-LLSGGEkDRKIAAWDsLQNYKKI 525
Cdd:cd00200   12 VTCVAFSPDGKLLaTGSGDGTIKVWDLETG---ELLRTLKGHTGPVRDVAASADGTyLASGSS-DKTIRLWD-LETGECV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 526 adTKLPEAAGGVRTI--YPQRP----GRNDGNIYVGTTRNNilegslqrRFTQVVFGHGRQLWGLAAHPDDELYATAGHD 599
Cdd:cd00200   87 --RTLTGHTSYVSSVafSPDGRilssSSRDKTIKVWDVETG--------KCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 600 KHVALW--RKNKLIWTIQTGYECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAM 675
Cdd:cd00200  157 GTIKLWdlRTGKCVATLTGHTGEVnSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632382 676 GSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWD 731
Cdd:cd00200  237 GSEDGTIRVWDLR----TGECVQTLSGhTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
382-848 1.62e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.90  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 382 SVWQWQWGHLLGKVATLQEGLSGAAFHPLDDNLIITHGRGHLAFWHRRKDGFFERTDIVKQPSRSHVTSVQFEPDGDVI- 460
Cdd:COG2319   15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLa 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 461 TADSDGFITIYSVDSDGAyfvRTEFEAHNKGIGCLIMLGEG-TLLSGGEkDRKIAAWDslqnykkiadtklpeaaggvrt 539
Cdd:COG2319   95 SASADGTVRLWDLATGLL---LRTLTGHTGAVRSVAFSPDGkTLASGSA-DGTVRLWD---------------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 540 iypqrpgrndgniyvgttrnnILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALW--RKNKLIWTIQTG 617
Cdd:COG2319  149 ---------------------LATGKLLRTLT----GHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlATGKLLRTLTGH 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 618 YECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYK 695
Cdd:COG2319  204 TGAVrSVAFSPDGkLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA----TGE 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 696 KVNKIRG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDAKSLSPERSPIAMKDVKWltnncTVGFLVAGQWsnryysttnt 774
Cdd:COG2319  280 LLRTLTGhSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR-----SVAFSPDGKT---------- 344

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632382 775 ivatcsrsaahdmLASGDAEGYLRLFRYPCISPRAEF--HESKVYSgmlacVRFLCGDHTLITvGGTDASLMVWDI 848
Cdd:COG2319  345 -------------LASGSDDGTVRLWDLATGELLRTLtgHTGAVTS-----VAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 571-847 1.39e-13

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 71.98  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 571 TQVVFGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECVA-LAFHPFGT-LAAGSTEGHLLVINCE 646
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDleTGELLRTLKGHTGPVRdVAASADGTyLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 647 NGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFrvsrDGFSYKKVNKIRG-SQPLTHLDWSMDGNFVQTVTIDF 725
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW----DVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 726 DLLFWDAKSLSPERSPIAMKD----VKWLTNNCTVGF-----------LVAGQWSNRYYSTTNTIVAtCSRSAAHDMLAS 790
Cdd:cd00200  158 TIKLWDLRTGKCVATLTGHTGevnsVAFSPDGEKLLSsssdgtiklwdLSTGKCLGTLRGHENGVNS-VAFSPDGYLLAS 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632382 791 GDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFlCGDHTLITVGGTDASLMVWD 847
Cdd:cd00200  237 GSEDGTIRVWDLRTGECVQTLsgHTNSVT-----SLAW-SPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 291-606 6.57e-12

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: 66.97  E-value: 6.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 291 DEDAQRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFGMGEldSGVTAVAFSQLngGSYI 370
Cdd:cd00200   40 TGELLRTLKGHTGPVRDVAASADGTYLASG---SSDKT----IRLWDLETGECVRTLTGHT--SYVSSVAFSPD--GRIL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 371 LAvdSGRESILSVWQWQWGhllGKVATLQ---EGLSGAAFHPldDNLIITHGR--GHLAFWhrrkDGffeRTDIVKQPSR 445
Cdd:cd00200  109 SS--SSRDKTIKVWDVETG---KCLTTLRghtDWVNSVAFSP--DGTFVASSSqdGTIKLW----DL---RTGKCVATLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 446 SH---VTSVQFEPDG-DVITADSDGFITIYSVDSDgayFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqn 521
Cdd:cd00200  175 GHtgeVNSVAFSPDGeKLLSSSSDGTIKLWDLSTG---KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 522 ykkiadtklpeaaggvrtiypqrpgrndgniyvgttrnnilegSLQRRFTQVVFGHGRQLWGLAAHPDDELYATAGHDKH 601
Cdd:cd00200  248 -------------------------------------------LRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284


                 ....*
gi 442632382 602 VALWR 606
Cdd:cd00200  285 IRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 622-848 2.10e-09

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: 59.66  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 622 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 700
Cdd:cd00200   14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 701 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 779
Cdd:cd00200   90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632382 780 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 848
Cdd:cd00200  142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 75-150 2.63e-06

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 46.10  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382    75 RVIRIINNLD---HSVqcRVLLNLRTSQPFEEVLEDLGQVLKIN---GAKKMYTGTGQEVRSFSQLRNefadvDTFYLAT 148
Cdd:smart00537   6 KRIRFYRNGDrffKGV--RLVVNRKRFKSFEALLQDLTEVVKLDlphGVRKLYTLDGKKVTSLDELED-----GGSYVAS 78


                   ..
gi 442632382   149 GT 150
Cdd:smart00537  79 GT 80
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 75-149 3.68e-06

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340456  Cd Length: 73  Bit Score: 45.30  E-value: 3.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632382  75 RVIRIINNLD-HSVQCRVLLNLRTSQPFEEVLEDLGQVLKIN--GAKKMYTGTGQEVRSFSQLRNefadvDTFYLATG 149
Cdd:cd01617    1 KRITVFRNGDkNFKGVKVLVKPRRFRTFDQLLDELTEKLGLPtgGVRKLYTPSGKLVKSLSDLED-----GESYVVCG 73
DCX2 cd17069
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are ...
 90-150 3.75e-06

Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or as a single repeat. The first repeat of DCX domain has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK).


Pssm-ID: 340589  Cd Length: 84  Bit Score: 45.84  E-value: 3.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632382  90 RVLLNLRTSQPFEEVLEDLGQVLKIN-GA-KKMYTGTGQEVrsfSQLRNEFADvDTFYLATGT 150
Cdd:cd17069   21 RILLNKKTAHSFEQVLTDITEAIKLDsGAvRKLFTLDGRQV---TCLQDFFGD-DDVFIAYGP 79
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
411-730 2.37e-05

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 48.06  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 411 DDNLIITHGRGhLAFWHRRKDGFfERTDIVKQPSRSHVTSVQFEPDGDVITADSDGF---------ITIYSVDSDGAYFV 481
Cdd:COG3292   91 DGRLWIGTDGG-LSRYDPKTDKF-TRYPLDPGLPNNSIRSIAEDSDGNIWVGTSNGLyrydpktgkFKRFTLDGLPSNTI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 482 RTEFEAHNkgiGCLIMLGEGTLLSGGEKDRkIAAWD----SLQNYKKIADTK-LPEAAggVRTIYPQRpgrnDGNIYVGT 556
Cdd:COG3292  169 TSLAEDAD---GNLWVDSDGNLWIGTDGNG-LYRLDpntgKFEHITHDPDPNsLSSNS--IYSLFEDR----EGNLWVGT 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 557 TRN--NILEgSLQRRFTQVVFGHGRQL-----WGLAAHPDDELYAT--AGHDKHvALWRKNKLIWTIQT-------GYEC 620
Cdd:COG3292  239 YGGglNYLD-PNNSKFKSYRHNDPNGLsgnsvRSIAEDSDGNLWIRlwIGTYGG-GLFRLDPKTGKFKRynpnglpSNSV 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 621 VALAFHPFGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLN---CVAYNQVGDmIAMGSQNGsiyLFRVSRDGFSYKKV 697
Cdd:COG3292  317 YSILEDSDGNLWIGTSGGGLYRYDPKTGKFTKFSEDNGLSNNfirSILEDSDGN-LWVGTNGG---LYRLDPKTGKFTNF 392

                        330       340       350
                 ....*....|....*....|....*....|...
gi 442632382 698 NKIRGSQPLTHldwsmdgNFVQTVTIDFDLLFW 730
Cdd:COG3292  393 THDPDKNGLSS-------NYINSIFEDSDGRLW 418
DCX_DCLK3 cd16111
Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of ...
 75-149 5.30e-05

Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of doublecortin (DCX) protein family. It functions as a microtubule-associated protein (MAP). DCLK3 contains only one N-terminal doublecortin domain (DCX), unlike DCLK1 and DCLK2 which each have two conserved DCX domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK3 has a serine/threonine kinase domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases.


Pssm-ID: 340528  Cd Length: 85  Bit Score: 42.42  E-value: 5.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382  75 RVIRIINNLDHSV-QCRVLLNLRTSQPFEEVLEDLGQVL-----KINGAKKMYTGTGQEVRSFSQLrneFADVDTFyLAT 148
Cdd:cd16111    3 KVITVVRNGGQPRtKITILLNRRSVQTFEQLMADISEALgfprwKNDRVRKLYSLRGREVRSVSDF---FREDDVF-IAT 78


                 .
gi 442632382 149 G 149
Cdd:cd16111   79 G 79
DCX2_DCX cd17142
Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 90-144 8.07e-05

Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also termed doublin or lissencephalin-X (Lis-XDCX), is a microtubule-associated protein (MAP). It belongs to the doublecortin (DCX) family, has double tandem DCX repeats, and is expressed in migrating neurons. Structure studies show that the N-terminal DCX domain has a stable ubiquitin-like fold. DCX is not only a unique MAP in terms of its structure, but also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340662  Cd Length: 84  Bit Score: 41.96  E-value: 8.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632382  90 RVLLNLRTSQPFEEVLEDLGQVLKINGA--KKMYTGTGQEVrsfSQLRNEFADVDTF 144
Cdd:cd17142   21 RVLLNKKTAHSFEQVLTDITEAIKLETGvvKKLYTLDGKQV---TCLHDFFGDDDVF 74
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
526-671 1.93e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 43.91  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 526 ADTKLPEAAGGVRTIYPQRPGRNDGNIYVGTTRNNILE------GSLQRRFTqvvfgHGRQLWGLAAHPDD-ELYATAGH 598
Cdd:COG3391   56 LLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSvidlatGKVVATIP-----VGGGPRGLAVDPDGgRLYVADSG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632382 599 DKHVAL--WRKNKLIWTIQTGYECVALAFHPFGTLA-AGSTEGH-----LLVINCENGAVMLTLRVCGSPLNcVAYNQVG 670
Cdd:COG3391  131 NGRVSVidTATGKVVATIPVGAGPHGIAVDPDGKRLyVANSGSNtvsviVSVIDTATGKVVATIPVGGGPVG-VAVSPDG 209


                 .
gi 442632382 671 D 671
Cdd:COG3391  210 R 210
DCX2_DCLK1 cd17143
Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 90-144 2.20e-03

Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of doublecortin (DCX) protein family that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK1 appears to regulate cyclic AMP signaling and is involved in neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Unlike DCX, the DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340663  Cd Length: 84  Bit Score: 38.01  E-value: 2.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632382  90 RVLLNLRTSQPFEEVLEDLGQVLKIN--GAKKMYTGTGQEVRSfsqLRNEFADVDTF 144
Cdd:cd17143   21 RILLNKKTAHSFEQVLTDITDAIKLDsgVVKRLYTLDGKQVMC---LQDFFGDDDIF 74
WD40 pfam00400
WD domain, G-beta repeat;
295-337 5.67e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 5.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 442632382  295 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 337
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
DCX2_DCLK2 cd17144
Dublecortin-like domain 2 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ...
 90-144 6.45e-03

Dublecortin-like domain 2 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of doublecortin (DCX) protein family that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in double tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK2 members regulate cyclic AMP signaling. Unlike DCX, the DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340664  Cd Length: 84  Bit Score: 36.54  E-value: 6.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632382  90 RVLLNLRTSQPFEEVLEDLGQVLKINGA--KKMYTGTGQEVrsfSQLRNEFADVDTF 144
Cdd:cd17144   21 RILLNKKTAHSFEQVLTDITEAIKLDSGvvKRLCTLDGKQV---TCLQDFFGDDDVF 74
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 296-337 6.55e-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: 34.98  E-value: 6.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442632382   296 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWS 337
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASG---SDDGT----IKLWD 40
 
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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