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Conserved domains on  [gi|23093438|gb|AAF49697|]
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Doublecortin-domain-containing echinoderm-microtubule-associated protein, isoform D [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 ...
 192-258 6.43e-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: 6.43e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23093438   192 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 258
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
291-702 3.35e-25

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 291 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 370
Cdd:COG2319   2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 371 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 449
Cdd:COG2319  82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 450 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 527
Cdd:COG2319 155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 528 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 597
Cdd:COG2319 226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 598 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 676
Cdd:COG2319 302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                       410       420
                ....*....|....*....|....*.
gi 23093438 677 LDWSMDGNFVQTVTIDFDLLFWDAKS 702
Cdd:COG2319 378 VAFSPDGRTLASGSADGTVRLWDLAT 403
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 43-115 1.59e-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: 1.59e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23093438  43 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 115
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 ...
 590-816 2.07e-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: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 590 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 668
Cdd:cd00200  14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 669 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 747
Cdd:cd00200  90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23093438 748 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 816
Cdd:cd00200 142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
WD40 pfam00400
WD domain, G-beta repeat;
263-305 5.57e-03

WD domain, G-beta repeat;


:

Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 5.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 23093438   263 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 305
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 ...
 192-258 6.43e-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: 6.43e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23093438   192 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 258
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
291-702 3.35e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 291 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 370
Cdd:COG2319   2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 371 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 449
Cdd:COG2319  82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 450 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 527
Cdd:COG2319 155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 528 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 597
Cdd:COG2319 226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 598 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 676
Cdd:COG2319 302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                       410       420
                ....*....|....*....|....*.
gi 23093438 677 LDWSMDGNFVQTVTIDFDLLFWDAKS 702
Cdd:COG2319 378 VAFSPDGRTLASGSADGTVRLWDLAT 403
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 43-115 1.59e-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: 1.59e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23093438  43 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 115
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 ...
 264-654 1.46e-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: 1.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 264 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFgmGELDSGVTAVAFSqlNGGSYILAvdS 343
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATG---SGDGT----IKVWDLETGELLRTL--KGHTGPVRDVAAS--ADGTYLAS--G 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 344 GRESILSVWQWQWGHLLGKVatlqeglsgaafhplddnliithgRGHlafwhrrkdgffertdivkqpsRSHVTSVQFEP 423
Cdd:cd00200  70 SSDKTIRLWDLETGECVRTL------------------------TGH----------------------TSYVSSVAFSP 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 424 DGDVITADS-DGFITIYSVDSdgaYFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqnykkiadtklpeaa 502
Cdd:cd00200 104 DGRILSSSSrDKTIKVWDVET---GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD----------------- 163

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 503 ggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWRKNKLIWtI 582
Cdd:cd00200 164 --LRT------------------------GKCVATLT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-L 212

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23093438 583 QT----GYECVALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFR 654
Cdd:cd00200 213 GTlrghENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 590-816 2.07e-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: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 590 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 668
Cdd:cd00200  14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 669 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 747
Cdd:cd00200  90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23093438 748 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 816
Cdd:cd00200 142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 43-118 2.53e-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: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438     43 RVIRIINNLD---HSVqcRVLLNLRTSQPFEEVLEDLGQVLKIN---GAKKMYTGTGQEVRSFSQLRNefadvDTFYLAT 116
Cdd:smart00537   6 KRIRFYRNGDrffKGV--RLVVNRKRFKSFEALLQDLTEVVKLDlphGVRKLYTLDGKKVTSLDELED-----GGSYVAS 78


                   ..
gi 23093438    117 GT 118
Cdd:smart00537  79 GT 80
WD40 pfam00400
WD domain, G-beta repeat;
263-305 5.57e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 5.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 23093438   263 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 305
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 264-305 6.43e-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: 34.98  E-value: 6.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 23093438    264 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWS 305
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 ...
 192-258 6.43e-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: 6.43e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23093438   192 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 258
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
291-702 3.35e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 291 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 370
Cdd:COG2319   2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 371 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 449
Cdd:COG2319  82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 450 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 527
Cdd:COG2319 155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 528 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 597
Cdd:COG2319 226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 598 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 676
Cdd:COG2319 302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                       410       420
                ....*....|....*....|....*.
gi 23093438 677 LDWSMDGNFVQTVTIDFDLLFWDAKS 702
Cdd:COG2319 378 VAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
251-656 1.18e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 1.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 251 AVAVLFDRDEDAQRHYTGHTEDIMCMDVHPSRELVASGQKAGRdrksqahVRIWSTESLQTLYVFGmgELDSGVTAVAFS 330
Cdd:COG2319  59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT-------VRLWDLATGLLLRTLT--GHTGAVRSVAFS 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 331 QlnGGSYILAVDSGREsiLSVWQWQWGHLLGKVATLQEGLSGAAFHPlDDNLIITHGR-GHLAFWHRRKDGFFERTdivk 409
Cdd:COG2319 130 P--DGKTLASGSADGT--VRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDdGTVRLWDLATGKLLRTL---- 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 410 QPSRSHVTSVQFEPDGDVI-TADSDGFITIYSVDSDGayfVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslq 488
Cdd:COG2319 201 TGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD--- 274

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 489 nykkiadtklpeaaggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDK 568
Cdd:COG2319 275 ----------------LAT------------------------GELLRTLT----GHSGGVNSVAFSPDGKLLASGSDDG 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 569 HVALW--RKNKLIWTIQTGYECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMG 644
Cdd:COG2319 311 TVRLWdlATGKLLRTLTGHTGAVrSVAFSPDGkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASG 390

                       410
                ....*....|..
gi 23093438 645 SQNGSIYLFRVS 656
Cdd:COG2319 391 SADGTVRLWDLA 402
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 43-115 1.59e-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: 1.59e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23093438  43 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 115
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 ...
 264-654 1.46e-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: 1.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 264 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFgmGELDSGVTAVAFSqlNGGSYILAvdS 343
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATG---SGDGT----IKVWDLETGELLRTL--KGHTGPVRDVAAS--ADGTYLAS--G 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 344 GRESILSVWQWQWGHLLGKVatlqeglsgaafhplddnliithgRGHlafwhrrkdgffertdivkqpsRSHVTSVQFEP 423
Cdd:cd00200  70 SSDKTIRLWDLETGECVRTL------------------------TGH----------------------TSYVSSVAFSP 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 424 DGDVITADS-DGFITIYSVDSdgaYFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqnykkiadtklpeaa 502
Cdd:cd00200 104 DGRILSSSSrDKTIKVWDVET---GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD----------------- 163

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 503 ggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWRKNKLIWtI 582
Cdd:cd00200 164 --LRT------------------------GKCVATLT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-L 212

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23093438 583 QT----GYECVALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFR 654
Cdd:cd00200 213 GTlrghENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 416-699 2.29e-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: 2.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 416 VTSVQFEPDGDVI-TADSDGFITIYSVDSDgayFVRTEFEAHNKGIGCLIMLGEGT-LLSGGEkDRKIAAWDsLQNYKKI 493
Cdd:cd00200  12 VTCVAFSPDGKLLaTGSGDGTIKVWDLETG---ELLRTLKGHTGPVRDVAASADGTyLASGSS-DKTIRLWD-LETGECV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 494 adTKLPEAAGGVRTI--YPQRP----GRNDGNIYVGTTRNNilegslqrRFTQVVFGHGRQLWGLAAHPDDELYATAGHD 567
Cdd:cd00200  87 --RTLTGHTSYVSSVafSPDGRilssSSRDKTIKVWDVETG--------KCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 568 KHVALW--RKNKLIWTIQTGYECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAM 643
Cdd:cd00200 157 GTIKLWdlRTGKCVATLTGHTGEVnSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23093438 644 GSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWD 699
Cdd:cd00200 237 GSEDGTIRVWDLR----TGECVQTLSGhTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
350-816 2.79e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.13  E-value: 2.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 350 SVWQWQWGHLLGKVATLQEGLSGAAFHPLDDNLIITHGRGHLAFWHRRKDGFFERTDIVKQPSRSHVTSVQFEPDGDVI- 428
Cdd:COG2319  15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLa 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 429 TADSDGFITIYSVDSDGAyfvRTEFEAHNKGIGCLIMLGEG-TLLSGGEkDRKIAAWDslqnykkiadtklpeaaggvrt 507
Cdd:COG2319  95 SASADGTVRLWDLATGLL---LRTLTGHTGAVRSVAFSPDGkTLASGSA-DGTVRLWD---------------------- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 508 iypqrpgrndgniyvgttrnnILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALW--RKNKLIWTIQTG 585
Cdd:COG2319 149 ---------------------LATGKLLRTLT----GHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlATGKLLRTLTGH 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 586 YECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYK 663
Cdd:COG2319 204 TGAVrSVAFSPDGkLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA----TGE 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 664 KVNKIRG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDAKSLSPERSPIAMKDVKWltnncTVGFLVAGQWsnryysttnt 742
Cdd:COG2319 280 LLRTLTGhSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR-----SVAFSPDGKT---------- 344

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23093438 743 ivatcsrsaahdmLASGDAEGYLRLFRYPCISPRAEF--HESKVYSgmlacVRFLCGDHTLITvGGTDASLMVWDI 816
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 ...
 539-815 1.40e-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: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 539 TQVVFGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECVA-LAFHPFGT-LAAGSTEGHLLVINCE 614
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDleTGELLRTLKGHTGPVRdVAASADGTyLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 615 NGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFrvsrDGFSYKKVNKIRG-SQPLTHLDWSMDGNFVQTVTIDF 693
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW----DVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 694 DLLFWDAKSLSPERSPIAMKD----VKWLTNNCTVGF-----------LVAGQWSNRYYSTTNTIVAtCSRSAAHDMLAS 758
Cdd:cd00200 158 TIKLWDLRTGKCVATLTGHTGevnsVAFSPDGEKLLSsssdgtiklwdLSTGKCLGTLRGHENGVNS-VAFSPDGYLLAS 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23093438 759 GDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFlCGDHTLITVGGTDASLMVWD 815
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 ...
 259-574 7.11e-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: 7.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 259 DEDAQRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFGMGEldSGVTAVAFSQLngGSYI 338
Cdd:cd00200  40 TGELLRTLKGHTGPVRDVAASADGTYLASG---SSDKT----IRLWDLETGECVRTLTGHT--SYVSSVAFSPD--GRIL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 339 LAvdSGRESILSVWQWQWGhllGKVATLQ---EGLSGAAFHPldDNLIITHGR--GHLAFWhrrkDGffeRTDIVKQPSR 413
Cdd:cd00200 109 SS--SSRDKTIKVWDVETG---KCLTTLRghtDWVNSVAFSP--DGTFVASSSqdGTIKLW----DL---RTGKCVATLT 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 414 SH---VTSVQFEPDG-DVITADSDGFITIYSVDSDgayFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqn 489
Cdd:cd00200 175 GHtgeVNSVAFSPDGeKLLSSSSDGTIKLWDLSTG---KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 490 ykkiadtklpeaaggvrtiypqrpgrndgniyvgttrnnilegSLQRRFTQVVFGHGRQLWGLAAHPDDELYATAGHDKH 569
Cdd:cd00200 248 -------------------------------------------LRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284


                ....*
gi 23093438 570 VALWR 574
Cdd:cd00200 285 IRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 590-816 2.07e-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: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 590 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 668
Cdd:cd00200  14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 669 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 747
Cdd:cd00200  90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23093438 748 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 816
Cdd:cd00200 142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 43-118 2.53e-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: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438     43 RVIRIINNLD---HSVqcRVLLNLRTSQPFEEVLEDLGQVLKIN---GAKKMYTGTGQEVRSFSQLRNefadvDTFYLAT 116
Cdd:smart00537   6 KRIRFYRNGDrffKGV--RLVVNRKRFKSFEALLQDLTEVVKLDlphGVRKLYTLDGKKVTSLDELED-----GGSYVAS 78


                   ..
gi 23093438    117 GT 118
Cdd:smart00537  79 GT 80
DCX2 cd17069
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are ...
 58-118 3.60e-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: 3.60e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23093438  58 RVLLNLRTSQPFEEVLEDLGQVLKIN-GA-KKMYTGTGQEVrsfSQLRNEFADvDTFYLATGT 118
Cdd:cd17069  21 RILLNKKTAHSFEQVLTDITEAIKLDsGAvRKLFTLDGRQV---TCLQDFFGD-DDVFIAYGP 79
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 43-117 3.94e-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: 3.94e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23093438  43 RVIRIINNLD-HSVQCRVLLNLRTSQPFEEVLEDLGQVLKIN--GAKKMYTGTGQEVRSFSQLRNefadvDTFYLATG 117
Cdd:cd01617   1 KRITVFRNGDkNFKGVKVLVKPRRFRTFDQLLDELTEKLGLPtgGVRKLYTPSGKLVKSLSDLED-----GESYVVCG 73
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
379-698 3.04e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 3.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 379 DDNLIITHGRGhLAFWHRRKDGFfERTDIVKQPSRSHVTSVQFEPDGDVITADSDGF---------ITIYSVDSDGAYFV 449
Cdd:COG3292  91 DGRLWIGTDGG-LSRYDPKTDKF-TRYPLDPGLPNNSIRSIAEDSDGNIWVGTSNGLyrydpktgkFKRFTLDGLPSNTI 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 450 RTEFEAHNkgiGCLIMLGEGTLLSGGEKDRkIAAWD----SLQNYKKIADTK-LPEAAggVRTIYPQRpgrnDGNIYVGT 524
Cdd:COG3292 169 TSLAEDAD---GNLWVDSDGNLWIGTDGNG-LYRLDpntgKFEHITHDPDPNsLSSNS--IYSLFEDR----EGNLWVGT 238

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 525 TRN--NILEgSLQRRFTQVVFGHGRQL-----WGLAAHPDDELYAT--AGHDKHvALWRKNKLIWTIQT-------GYEC 588
Cdd:COG3292 239 YGGglNYLD-PNNSKFKSYRHNDPNGLsgnsvRSIAEDSDGNLWIRlwIGTYGG-GLFRLDPKTGKFKRynpnglpSNSV 316

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 589 VALAFHPFGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLN---CVAYNQVGDmIAMGSQNGsiyLFRVSRDGFSYKKV 665
Cdd:COG3292 317 YSILEDSDGNLWIGTSGGGLYRYDPKTGKFTKFSEDNGLSNNfirSILEDSDGN-LWVGTNGG---LYRLDPKTGKFTNF 392

                       330       340       350
                ....*....|....*....|....*....|...
gi 23093438 666 NKIRGSQPLTHldwsmdgNFVQTVTIDFDLLFW 698
Cdd:COG3292 393 THDPDKNGLSS-------NYINSIFEDSDGRLW 418
DCX_DCLK3 cd16111
Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of ...
 43-117 5.35e-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: 5.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438  43 RVIRIINNLDHSV-QCRVLLNLRTSQPFEEVLEDLGQVL-----KINGAKKMYTGTGQEVRSFSQLrneFADVDTFyLAT 116
Cdd:cd16111   3 KVITVVRNGGQPRtKITILLNRRSVQTFEQLMADISEALgfprwKNDRVRKLYSLRGREVRSVSDF---FREDDVF-IAT 78


                .
gi 23093438 117 G 117
Cdd:cd16111  79 G 79
DCX2_DCX cd17142
Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 58-112 7.76e-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: 7.76e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23093438  58 RVLLNLRTSQPFEEVLEDLGQVLKINGA--KKMYTGTGQEVrsfSQLRNEFADVDTF 112
Cdd:cd17142  21 RVLLNKKTAHSFEQVLTDITEAIKLETGvvKKLYTLDGKQV---TCLHDFFGDDDVF 74
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
494-639 2.30e-04

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 43.53  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 494 ADTKLPEAAGGVRTIYPQRPGRNDGNIYVGTTRNNILE------GSLQRRFTqvvfgHGRQLWGLAAHPDD-ELYATAGH 566
Cdd:COG3391  56 LLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSvidlatGKVVATIP-----VGGGPRGLAVDPDGgRLYVADSG 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093438 567 DKHVAL--WRKNKLIWTIQTGYECVALAFHPFGTLA-AGSTEGH-----LLVINCENGAVMLTLRVCGSPLNcVAYNQVG 638
Cdd:COG3391 131 NGRVSVidTATGKVVATIPVGAGPHGIAVDPDGKRLyVANSGSNtvsviVSVIDTATGKVVATIPVGGGPVG-VAVSPDG 209


                .
gi 23093438 639 D 639
Cdd:COG3391 210 R 210
DCX2_DCLK1 cd17143
Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 58-112 2.17e-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: 2.17e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23093438  58 RVLLNLRTSQPFEEVLEDLGQVLKIN--GAKKMYTGTGQEVRSfsqLRNEFADVDTF 112
Cdd:cd17143  21 RILLNKKTAHSFEQVLTDITDAIKLDsgVVKRLYTLDGKQVMC---LQDFFGDDDIF 74
WD40 pfam00400
WD domain, G-beta repeat;
263-305 5.57e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 5.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 23093438   263 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 305
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 ...
 58-112 6.20e-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: 6.20e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23093438  58 RVLLNLRTSQPFEEVLEDLGQVLKINGA--KKMYTGTGQEVrsfSQLRNEFADVDTF 112
Cdd:cd17144  21 RILLNKKTAHSFEQVLTDITEAIKLDSGvvKRLCTLDGKQV---TCLQDFFGDDDVF 74
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 264-305 6.43e-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: 34.98  E-value: 6.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 23093438    264 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWS 305
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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