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Conserved domains on  [gi|442632378|ref|NP_001261850|]
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Doublecortin-domain-containing echinoderm-microtubule-associated protein, isoform G [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 166-253 7.87e-33

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: 121.98  E-value: 7.87e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378    166 SYWKARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLLDKISP--KMDLPRGARYVFSMDGDRKYHLDELEDGAFYVVSS 243
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKR-FKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKKVTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 442632378    244 FKAFKPASYG 253
Cdd:smart00537   80 TEAFKKVDYG 89
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 449-515 2.34e-30

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: 114.57  E-value: 2.34e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632378   449 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 515
Cdd:pfam03451    1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
548-959 2.72e-25

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  548 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 627
Cdd:COG2319     2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  628 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 706
Cdd:COG2319    82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  707 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 784
Cdd:COG2319   155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  785 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 854
Cdd:COG2319   226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  855 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 933
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                         410       420
                  ....*....|....*....|....*.
gi 442632378  934 LDWSMDGNFVQTVTIDFDLLFWDAKS 959
Cdd:COG2319   378 VAFSPDGRTLASGSADGTVRLWDLAT 403
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 300-372 2.19e-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: 2.19e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632378  300 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 372
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 ...
 847-1073 1.55e-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: 60.43  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  847 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 925
Cdd:cd00200    14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  926 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 1004
Cdd:cd00200    90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632378 1005 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 1073
Cdd:cd00200   142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
WD40 pfam00400
WD domain, G-beta repeat;
520-562 6.82e-03

WD domain, G-beta repeat;


:

Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 6.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 442632378   520 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 562
Cdd:pfam00400    4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
 
Name Accession Description Interval E-value
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 166-253 7.87e-33

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: 121.98  E-value: 7.87e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378    166 SYWKARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLLDKISP--KMDLPRGARYVFSMDGDRKYHLDELEDGAFYVVSS 243
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKR-FKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKKVTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 442632378    244 FKAFKPASYG 253
Cdd:smart00537   80 TEAFKKVDYG 89
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 449-515 2.34e-30

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: 114.57  E-value: 2.34e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632378   449 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 515
Cdd:pfam03451    1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
548-959 2.72e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  548 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 627
Cdd:COG2319     2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  628 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 706
Cdd:COG2319    82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  707 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 784
Cdd:COG2319   155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  785 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 854
Cdd:COG2319   226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  855 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 933
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                         410       420
                  ....*....|....*....|....*.
gi 442632378  934 LDWSMDGNFVQTVTIDFDLLFWDAKS 959
Cdd:COG2319   378 VAFSPDGRTLASGSADGTVRLWDLAT 403
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 300-372 2.19e-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: 2.19e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632378  300 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 372
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 ...
 521-911 4.96e-22

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: 97.79  E-value: 4.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  521 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFgmGELDSGVTAVAFSqlNGGSYILAvdS 600
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG---SGDGT----IKVWDLETGELLRTL--KGHTGPVRDVAAS--ADGTYLAS--G 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  601 GRESILSVWQWQWGHLLGKVatlqeglsgaafhplddnliithgRGHlafwhrrkdgffertdivkqpsRSHVTSVQFEP 680
Cdd:cd00200    70 SSDKTIRLWDLETGECVRTL------------------------TGH----------------------TSYVSSVAFSP 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  681 DGDVITADS-DGFITIYSVDSdgaYFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqnykkiadtklpeaa 759
Cdd:cd00200   104 DGRILSSSSrDKTIKVWDVET---GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD----------------- 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  760 ggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWRKNKLIWtI 839
Cdd:cd00200   164 --LRT------------------------GKCVATLT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-L 212

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  840 QT----GYECVALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFR 911
Cdd:cd00200   213 GTlrghENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
DCX1 cd16109
Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are ...
 169-249 1.37e-19

Dublecortin-like domain 1; Members of the 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 single repeats. The family represents the first repeat of the DCX domain which 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: 340526  Cd Length: 85  Bit Score: 84.27  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  169 KARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLLDK----ISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSS 243
Cdd:cd16109     1 KAKKVRFYRNGDRFFKGIVYAVSSER-FRSFEALLADltrsLSDNVNLPQGVRTIFTIDGSRKItSLDELEDGESYVCAS 79


                  ....*.
gi 442632378  244 FKAFKP 249
Cdd:cd16109    80 TDAFKK 85
DCX pfam03607
Doublecortin;
192-247 4.68e-11

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 59.00  E-value: 4.68e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632378   192 PGRDVTSLDNLLDKISPKMD-LPRGA-RYVFSMDGDRKYHLDELEDGAFYVVSSFKAF 247
Cdd:pfam03607    3 NKRRFRSFDALLDELTEKVVkLPFGAvRKLYTLDGKRVTSLDELEDGGVYVAAGREKF 60
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 847-1073 1.55e-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: 60.43  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  847 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 925
Cdd:cd00200    14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  926 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 1004
Cdd:cd00200    90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632378 1005 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 1073
Cdd:cd00200   142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 300-375 3.93e-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: 3.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378    300 RVIRIINNLD---HSVqcRVLLNLRTSQPFEEVLEDLGQVLKIN---GAKKMYTGTGQEVRSFSQLRNefadvDTFYLAT 373
Cdd:smart00537    6 KRIRFYRNGDrffKGV--RLVVNRKRFKSFEALLQDLTEVVKLDlphGVRKLYTLDGKKVTSLDELED-----GGSYVAS 78


                    ..
gi 442632378    374 GT 375
Cdd:smart00537   79 GT 80
WD40 pfam00400
WD domain, G-beta repeat;
520-562 6.82e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 6.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 442632378   520 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 562
Cdd:pfam00400    4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 521-562 7.57e-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: 35.37  E-value: 7.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 442632378    521 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWS 562
Cdd:smart00320    6 KTLKGHTGPVTSVAFSPDGKYLASG---SDDGT----IKLWD 40
 
Name Accession Description Interval E-value
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 166-253 7.87e-33

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: 121.98  E-value: 7.87e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378    166 SYWKARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLLDKISP--KMDLPRGARYVFSMDGDRKYHLDELEDGAFYVVSS 243
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKR-FKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKKVTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 442632378    244 FKAFKPASYG 253
Cdd:smart00537   80 TEAFKKVDYG 89
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 449-515 2.34e-30

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: 114.57  E-value: 2.34e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632378   449 KVTIRGLRRTFYPPVHHAPADNS-----PPDKKLQLQWVHGYRGIDARRNLWVLPSGELLYYVAAVAVLFDR 515
Cdd:pfam03451    1 KMAIRGRPGAVYPPSNYYPKDDLdqkkePPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
548-959 2.72e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  548 AGRDRKSQAHVRIWSTESLQTLYVFGMGELDSGVTAVAFSQLNGGSYILAVDSGRESILSVWQWQWGHLLGKVATLQEGL 627
Cdd:COG2319     2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  628 SGAAFHPLDDNLIITHGRGHLAFWhRRKDGFFERTDivkQPSRSHVTSVQFEPDGD-VITADSDGFITIYSVDSDGayfV 706
Cdd:COG2319    82 LSVAFSPDGRLLASASADGTVRLW-DLATGLLLRTL---TGHTGAVRSVAFSPDGKtLASGSADGTVRLWDLATGK---L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  707 RTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDsLQNYKKIAdtKLPEAAGGVRTIY--PqrpgrnDGNIYVGTTRN 784
Cdd:COG2319   155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLR--TLTGHTGAVRSVAfsP------DGKLLASGSAD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  785 ------NILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECV-ALAFHPFG- 854
Cdd:COG2319   226 gtvrlwDLATGKLLRTLT----GHSGSVRSVAFSPDGRLLASGSADGTVRLWDlaTGELLRTLTGHSGGVnSVAFSPDGk 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  855 TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTH 933
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA----TGELLRTLTGhTGAVTS 377

                         410       420
                  ....*....|....*....|....*.
gi 442632378  934 LDWSMDGNFVQTVTIDFDLLFWDAKS 959
Cdd:COG2319   378 VAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
508-913 8.96e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.38  E-value: 8.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  508 AVAVLFDRDEDAQRHYTGHTEDIMCMDVHPSRELVASGQKAGRdrksqahVRIWSTESLQTLYVFGmgELDSGVTAVAFS 587
Cdd:COG2319    59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT-------VRLWDLATGLLLRTLT--GHTGAVRSVAFS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  588 QlnGGSYILAVDSGREsiLSVWQWQWGHLLGKVATLQEGLSGAAFHPlDDNLIITHGR-GHLAFWHRRKDGFFERTdivk 666
Cdd:COG2319   130 P--DGKTLASGSADGT--VRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDdGTVRLWDLATGKLLRTL---- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  667 QPSRSHVTSVQFEPDGDVI-TADSDGFITIYSVDSDGayfVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslq 745
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD--- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  746 nykkiadtklpeaaggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDK 825
Cdd:COG2319   275 ----------------LAT------------------------GELLRTLT----GHSGGVNSVAFSPDGKLLASGSDDG 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  826 HVALW--RKNKLIWTIQTGYECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMG 901
Cdd:COG2319   311 TVRLWdlATGKLLRTLTGHTGAVrSVAFSPDGkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASG 390

                         410
                  ....*....|..
gi 442632378  902 SQNGSIYLFRVS 913
Cdd:COG2319   391 SADGTVRLWDLA 402
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 300-372 2.19e-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: 2.19e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632378  300 RVIRIINNLDHSVQCRVLLNLRTSQPFEEVLEDLGQVLKiNGAKKMYTGTGQEVRSFSQLrneFADVDTFYLA 372
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 ...
 521-911 4.96e-22

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: 97.79  E-value: 4.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  521 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFgmGELDSGVTAVAFSqlNGGSYILAvdS 600
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG---SGDGT----IKVWDLETGELLRTL--KGHTGPVRDVAAS--ADGTYLAS--G 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  601 GRESILSVWQWQWGHLLGKVatlqeglsgaafhplddnliithgRGHlafwhrrkdgffertdivkqpsRSHVTSVQFEP 680
Cdd:cd00200    70 SSDKTIRLWDLETGECVRTL------------------------TGH----------------------TSYVSSVAFSP 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  681 DGDVITADS-DGFITIYSVDSdgaYFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqnykkiadtklpeaa 759
Cdd:cd00200   104 DGRILSSSSrDKTIKVWDVET---GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD----------------- 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  760 ggVRTiypqrpgrndgniyvgttrnnileGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALWRKNKLIWtI 839
Cdd:cd00200   164 --LRT------------------------GKCVATLT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-L 212

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  840 QT----GYECVALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFR 911
Cdd:cd00200   213 GTlrghENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 673-956 1.17e-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: 93.55  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  673 VTSVQFEPDGDVI-TADSDGFITIYSVDSDgayFVRTEFEAHNKGIGCLIMLGEGT-LLSGGEkDRKIAAWDsLQNYKKI 750
Cdd:cd00200    12 VTCVAFSPDGKLLaTGSGDGTIKVWDLETG---ELLRTLKGHTGPVRDVAASADGTyLASGSS-DKTIRLWD-LETGECV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  751 adTKLPEAAGGVRTI--YPQRP----GRNDGNIYVGTTRNNilegslqrRFTQVVFGHGRQLWGLAAHPDDELYATAGHD 824
Cdd:cd00200    87 --RTLTGHTSYVSSVafSPDGRilssSSRDKTIKVWDVETG--------KCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  825 KHVALW--RKNKLIWTIQTGYECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAM 900
Cdd:cd00200   157 GTIKLWdlRTGKCVATLTGHTGEVnSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  901 GSQNGSIYLFRVSrdgfSYKKVNKIRG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWD 956
Cdd:cd00200   237 GSEDGTIRVWDLR----TGECVQTLSGhTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
DCX1 cd16109
Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are ...
 169-249 1.37e-19

Dublecortin-like domain 1; Members of the 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 single repeats. The family represents the first repeat of the DCX domain which 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: 340526  Cd Length: 85  Bit Score: 84.27  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  169 KARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLLDK----ISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSS 243
Cdd:cd16109     1 KAKKVRFYRNGDRFFKGIVYAVSSER-FRSFEALLADltrsLSDNVNLPQGVRTIFTIDGSRKItSLDELEDGESYVCAS 79


                  ....*.
gi 442632378  244 FKAFKP 249
Cdd:cd16109    80 TDAFKK 85
WD40 COG2319
WD40 repeat [General function prediction only];
607-1073 2.16e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.90  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  607 SVWQWQWGHLLGKVATLQEGLSGAAFHPLDDNLIITHGRGHLAFWHRRKDGFFERTDIVKQPSRSHVTSVQFEPDGDVI- 685
Cdd:COG2319    15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLa 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  686 TADSDGFITIYSVDSDGAyfvRTEFEAHNKGIGCLIMLGEG-TLLSGGEkDRKIAAWDslqnykkiadtklpeaaggvrt 764
Cdd:COG2319    95 SASADGTVRLWDLATGLL---LRTLTGHTGAVRSVAFSPDGkTLASGSA-DGTVRLWD---------------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  765 iypqrpgrndgniyvgttrnnILEGSLQRRFTqvvfGHGRQLWGLAAHPDDELYATAGHDKHVALW--RKNKLIWTIQTG 842
Cdd:COG2319   149 ---------------------LATGKLLRTLT----GHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlATGKLLRTLTGH 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  843 YECV-ALAFHPFG-TLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSrdgfSYK 920
Cdd:COG2319   204 TGAVrSVAFSPDGkLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA----TGE 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  921 KVNKIRG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDAKSLSPERSPIAMKDVKWltnncTVGFLVAGQWsnryysttnt 999
Cdd:COG2319   280 LLRTLTGhSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR-----SVAFSPDGKT---------- 344

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632378 1000 ivatcsrsaahdmLASGDAEGYLRLFRYPCISPRAEF--HESKVYSgmlacVRFLCGDHTLITvGGTDASLMVWDI 1073
Cdd:COG2319   345 -------------LASGSDDGTVRLWDLATGELLRTLtgHTGAVTS-----VAFSPDGRTLAS-GSADGTVRLWDL 401
DCX1_DCX cd16112
Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 169-252 4.70e-14

Dublecortin-like domain 1 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 structure, it also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340529  Cd Length: 89  Bit Score: 68.79  E-value: 4.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  169 KARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLL----DKISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSS 243
Cdd:cd16112     1 KAKKVRFYRNGDRYFKGIVYAVSSDR-FRSFDALLadltRSLSDNINLPQGVRYIYTIDGSRKIgSMDELEEGESYVCSS 79


                  ....*....
gi 442632378  244 FKAFKPASY 252
Cdd:cd16112    80 DNFFKKVEY 88
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 796-1072 9.24e-14

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 73.14  E-value: 9.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  796 TQVVFGHGRQLWGLAAHPDDELYATAGHDKHVALWR--KNKLIWTIQTGYECVA-LAFHPFGT-LAAGSTEGHLLVINCE 871
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDleTGELLRTLKGHTGPVRdVAASADGTyLASGSSDKTIRLWDLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  872 NGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFrvsrDGFSYKKVNKIRG-SQPLTHLDWSMDGNFVQTVTIDF 950
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW----DVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  951 DLLFWDAKSLSPERSPIAMKD----VKWLTNNCTVGF-----------LVAGQWSNRYYSTTNTIVAtCSRSAAHDMLAS 1015
Cdd:cd00200   158 TIKLWDLRTGKCVATLTGHTGevnsVAFSPDGEKLLSsssdgtiklwdLSTGKCLGTLRGHENGVNS-VAFSPDGYLLAS 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632378 1016 GDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFlCGDHTLITVGGTDASLMVWD 1072
Cdd:cd00200   237 GSEDGTIRVWDLRTGECVQTLsgHTNSVT-----SLAW-SPDGKRLASGSADGTIRIWD 289
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 171-243 3.31e-13

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: 65.71  E-value: 3.31e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDL-PRGARYVFSMDGDRKYHLDELEDGAFYVVSS 243
Cdd:cd01617     1 KRITVFRNGDKNFKGVKVLVKP-RRFRTFDQLLDELTEKLGLpTGGVRKLYTPSGKLVKSLSDLEDGESYVVCG 73
DCX1_DCDC2_like cd17071
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ...
 171-249 8.90e-13

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and similar proteins; DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of 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. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340591  Cd Length: 80  Bit Score: 64.55  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDLPRGA-RYVFS-MDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17071     1 KIIVVYKNGDPFFPGKKFVVNE-RQVRTFDAFLNEVTSGIKAPFGAvRSIYTpTGGHRVKDLDSLQNGGVYVAAGSERFK 79


                  .
gi 442632378  249 P 249
Cdd:cd17071    80 K 80
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 516-831 3.85e-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: 68.13  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  516 DEDAQRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWSTESLQTLYVFGMGEldSGVTAVAFSQLngGSYI 595
Cdd:cd00200    40 TGELLRTLKGHTGPVRDVAASADGTYLASG---SSDKT----IRLWDLETGECVRTLTGHT--SYVSSVAFSPD--GRIL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  596 LAvdSGRESILSVWQWQWGhllGKVATLQ---EGLSGAAFHPldDNLIITHGR--GHLAFWhrrkDGffeRTDIVKQPSR 670
Cdd:cd00200   109 SS--SSRDKTIKVWDVETG---KCLTTLRghtDWVNSVAFSP--DGTFVASSSqdGTIKLW----DL---RTGKCVATLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  671 SH---VTSVQFEPDG-DVITADSDGFITIYSVDSDgayFVRTEFEAHNKGIGCLIMLGEGTLLSGGEKDRKIAAWDslqn 746
Cdd:cd00200   175 GHtgeVNSVAFSPDGeKLLSSSSDGTIKLWDLSTG---KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  747 ykkiadtklpeaaggvrtiypqrpgrndgniyvgttrnnilegSLQRRFTQVVFGHGRQLWGLAAHPDDELYATAGHDKH 826
Cdd:cd00200   248 -------------------------------------------LRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284


                  ....*
gi 442632378  827 VALWR 831
Cdd:cd00200   285 IRIWD 289
DCX1_DCLK1 cd17140
Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 169-252 7.24e-12

Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of doublecortin (DCX) protein superfamily 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, this DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340660  Cd Length: 89  Bit Score: 62.33  E-value: 7.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  169 KARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLL----DKISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSS 243
Cdd:cd17140     1 KAKKVRFYRNGDRYFKGIVYAISPDR-FRSFEALLadltRTLSDNVNLPQGVRTIYTIDGLKKIsSLDQLVEGESYVCGS 79


                  ....*....
gi 442632378  244 FKAFKPASY 252
Cdd:cd17140    80 IEPFKKLEY 88
DCX1_DCLK2 cd17141
Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ...
 169-248 1.28e-11

Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier (Ubiquitination) 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. Molecular actions of DCX members are less well characterized and it shows that DCLK2 members regulate cyclic AMP signaling. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340661  Cd Length: 85  Bit Score: 61.46  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  169 KARRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLL----DKISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSS 243
Cdd:cd17141     1 KAKKVRFYRNGDRYFKGLVYAVSSDR-FRSFDALLmeltRSLSDNVNLPQGVRTIYTIDGSKKItSLDELLEGESYVCAS 79


                  ....*
gi 442632378  244 FKAFK 248
Cdd:cd17141    80 NEPFR 84
DCX pfam03607
Doublecortin;
192-247 4.68e-11

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 59.00  E-value: 4.68e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632378   192 PGRDVTSLDNLLDKISPKMD-LPRGA-RYVFSMDGDRKYHLDELEDGAFYVVSSFKAF 247
Cdd:pfam03607    3 NKRRFRSFDALLDELTEKVVkLPFGAvRKLYTLDGKRVTSLDELEDGGVYVAAGREKF 60
DCX1_RP_like cd16110
Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 171-245 1.03e-10

Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) family. It has 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: 340527  Cd Length: 75  Bit Score: 58.46  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  171 RRVVFYRNGDPFFPGVEL-----RYRpgrdvtSLDNLLDKISPKMDLPRGARYVFSMDGDRKYH-LDELEDGAFYVVSSF 244
Cdd:cd16110     1 KNVTFYKDGDVHFSGVRVainprRYR------TFDALLDELSRKVPLPFGVRSITTPRGRHSITsLEQLEDGGKYVCSSK 74


                  .
gi 442632378  245 K 245
Cdd:cd16110    75 R 75
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 171-249 2.30e-10

Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. 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. The RP1 protein is expressed in photoreceptors and is required for correct stacking of outer segment discs. It interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340665  Cd Length: 79  Bit Score: 57.90  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSSFKAFKP 249
Cdd:cd17145     1 KRVCFYKSGDPQFGGLRMVVNS-RSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHItSLEDLEDGKSYICSHQKKVKP 79
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 173-243 3.84e-10

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a 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 cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340530  Cd Length: 74  Bit Score: 56.82  E-value: 3.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632378  173 VVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDLPRGA-RYVFSMDGDRKYHLDELEDGAFYVVSS 243
Cdd:cd16113     4 IHVFPNGDLLHPPSKVLLTK-RRLPNWDTVLEEVTEKVKLQTGAvRKLYTLDGKRISDPDELVNGGQYVAVG 74
DCX1_RP1L1 cd17146
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ...
 171-249 7.71e-10

Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. 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. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.


Pssm-ID: 340666  Cd Length: 79  Bit Score: 56.38  E-value: 7.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDLPRGARYVFSMDGDRKY-HLDELEDGAFYVVSSFKAFKP 249
Cdd:cd17146     1 KKITFYKSGDPQFGGVKMAVNK-RTFKSFSALLDDLSQRVPLPFGVRTITTPRGTHSIsRLEQLEDGGCYLCSDKKYVKP 79
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 847-1073 1.55e-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: 60.43  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  847 ALAFHP-FGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLNCVAYNQVGDMIAMGSQNGSIYLFRVSRDgfsyKKVNKI 925
Cdd:cd00200    14 CVAFSPdGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  926 RG-SQPLTHLDWSMDGNFVQTVTIDFDLLFWDakslsperspiamkdvkWLTNNCTVGFLVAGQWsnryysttntiVATC 1004
Cdd:cd00200    90 TGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VETGKCLTTLRGHTDW-----------VNSV 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632378 1005 SRSAAHDMLASGDAEGYLRLFRYPCISPRAEF--HESKVYsgmlaCVRFLcGDHTLITVGGTDASLMVWDI 1073
Cdd:cd00200   142 AFSPDGTFVASSSQDGTIKLWDLRTGKCVATLtgHTGEVN-----SVAFS-PDGEKLLSSSSDGTIKLWDL 206
DCX1_DCDC2C cd17151
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
 171-248 3.30e-09

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340671  Cd Length: 79  Bit Score: 54.41  E-value: 3.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDLPRGARYVFS-MDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17151     1 KTILVYRNGDPFYQAHKVVIHR-RRVKTFDALLRQLTETVKVPFGVRCLYTpRNGHRVKGLDDLQGGGKYVAAGRERFK 78
DCX1_DCDC2B cd17150
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
 171-248 7.85e-08

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340670  Cd Length: 79  Bit Score: 50.57  E-value: 7.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPgRDVTSLDNLLDKISPKMDLPRGARYVFS-MDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17150     1 KNVVVYRNGDPFFTGRKFVVNQ-RQFLTFEAFLNEVTSNIQAPVAVRNLYTpREGHRVTELGDLQNGGHYVAAGFERFK 78
DCX1_DCDC2 cd17149
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 171-248 5.01e-07

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of doublecortin (DCX) family. It 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. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340669  Cd Length: 80  Bit Score: 48.23  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  171 RRVVFYRNGDPFFPGVELRYRPGRdVTSLDNLLDKISPKMDLPRGA-RYVFS-MDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17149     1 KNVLVYRNGDPFYAGRRLVINEKR-VSSFEVFLKEVTGGVQAPFGAvRNIYTpRGGHRVRSLEQLQSGEQYVAAGRERFK 79
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 300-375 3.93e-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: 3.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378    300 RVIRIINNLD---HSVqcRVLLNLRTSQPFEEVLEDLGQVLKIN---GAKKMYTGTGQEVRSFSQLRNefadvDTFYLAT 373
Cdd:smart00537    6 KRIRFYRNGDrffKGV--RLVVNRKRFKSFEALLQDLTEVVKLDlphGVRKLYTLDGKKVTSLDELED-----GGSYVAS 78


                    ..
gi 442632378    374 GT 375
Cdd:smart00537   79 GT 80
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 300-374 4.77e-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: 4.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632378  300 RVIRIINNLD-HSVQCRVLLNLRTSQPFEEVLEDLGQVLKIN--GAKKMYTGTGQEVRSFSQLRNefadvDTFYLATG 374
Cdd:cd01617     1 KRITVFRNGDkNFKGVKVLVKPRRFRTFDQLLDELTEKLGLPtgGVRKLYTPSGKLVKSLSDLED-----GESYVVCG 73
DCX2 cd17069
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are ...
 315-375 4.98e-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: 4.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632378  315 RVLLNLRTSQPFEEVLEDLGQVLKIN-GA-KKMYTGTGQEVrsfSQLRNEFADvDTFYLATGT 375
Cdd:cd17069    21 RILLNKKTAHSFEQVLTDITEAIKLDsGAvRKLFTLDGRQV---TCLQDFFGD-DDVFIAYGP 79
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
636-955 3.23e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 48.06  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  636 DDNLIITHGRGhLAFWHRRKDGFfERTDIVKQPSRSHVTSVQFEPDGDVITADSDGF---------ITIYSVDSDGAYFV 706
Cdd:COG3292    91 DGRLWIGTDGG-LSRYDPKTDKF-TRYPLDPGLPNNSIRSIAEDSDGNIWVGTSNGLyrydpktgkFKRFTLDGLPSNTI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  707 RTEFEAHNkgiGCLIMLGEGTLLSGGEKDRkIAAWD----SLQNYKKIADTK-LPEAAggVRTIYPQRpgrnDGNIYVGT 781
Cdd:COG3292   169 TSLAEDAD---GNLWVDSDGNLWIGTDGNG-LYRLDpntgKFEHITHDPDPNsLSSNS--IYSLFEDR----EGNLWVGT 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  782 TRN--NILEgSLQRRFTQVVFGHGRQL-----WGLAAHPDDELYAT--AGHDKHvALWRKNKLIWTIQT-------GYEC 845
Cdd:COG3292   239 YGGglNYLD-PNNSKFKSYRHNDPNGLsgnsvRSIAEDSDGNLWIRlwIGTYGG-GLFRLDPKTGKFKRynpnglpSNSV 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  846 VALAFHPFGTLAAGSTEGHLLVINCENGAVMLTLRVCGSPLN---CVAYNQVGDmIAMGSQNGsiyLFRVSRDGFSYKKV 922
Cdd:COG3292   317 YSILEDSDGNLWIGTSGGGLYRYDPKTGKFTKFSEDNGLSNNfirSILEDSDGN-LWVGTNGG---LYRLDPKTGKFTNF 392

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442632378  923 NKIRGSQPLTHldwsmdgNFVQTVTIDFDLLFW 955
Cdd:COG3292   393 THDPDKNGLSS-------NYINSIFEDSDGRLW 418
DCX_DCLK3 cd16111
Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of ...
 300-374 9.07e-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: 42.04  E-value: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  300 RVIRIINNLDHSV-QCRVLLNLRTSQPFEEVLEDLGQVL-----KINGAKKMYTGTGQEVRSFSQLrneFADVDTFyLAT 373
Cdd:cd16111     3 KVITVVRNGGQPRtKITILLNRRSVQTFEQLMADISEALgfprwKNDRVRKLYSLRGREVRSVSDF---FREDDVF-IAT 78


                  .
gi 442632378  374 G 374
Cdd:cd16111    79 G 79
DCX2_DCX cd17142
Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 315-369 1.07e-04

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: 1.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  315 RVLLNLRTSQPFEEVLEDLGQVLKINGA--KKMYTGTGQEVrsfSQLRNEFADVDTF 369
Cdd:cd17142    21 RVLLNKKTAHSFEQVLTDITEAIKLETGvvKKLYTLDGKQV---TCLHDFFGDDDVF 74
DCX4_DCDC5 cd17159
Doublecortin-like domain 4 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is ...
 171-248 1.27e-04

Doublecortin-like domain 4 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of 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. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8.


Pssm-ID: 340679  Cd Length: 73  Bit Score: 41.51  E-value: 1.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632378  171 RRVVFYRNGDPFFPGVelrYRPGRdvtSLDNLLDKISPKMDLPRGARYVFSMDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17159     1 KRVLVYPNGGSPERAV---YAWGK---SIEELLDSCTERLGLRKPAKYLYTPDGEQIQSWDDIERDMLLCVSTGEPFL 72
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
751-896 3.66e-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: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  751 ADTKLPEAAGGVRTIYPQRPGRNDGNIYVGTTRNNILE------GSLQRRFTqvvfgHGRQLWGLAAHPDD-ELYATAGH 823
Cdd:COG3391    56 LLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSvidlatGKVVATIP-----VGGGPRGLAVDPDGgRLYVADSG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  824 DKHVAL--WRKNKLIWTIQTGYECVALAFHPFGTLA-AGSTEGH-----LLVINCENGAVMLTLRVCGSPLNcVAYNQVG 895
Cdd:COG3391   131 NGRVSVidTATGKVVATIPVGAGPHGIAVDPDGKRLyVANSGSNtvsviVSVIDTATGKVVATIPVGGGPVG-VAVSPDG 209


                  .
gi 442632378  896 D 896
Cdd:COG3391   210 R 210
DCX_DCDC5_like cd17072
Doublecortin-like domain found in doublecortin domain-containing protein 5 (DCDC5) and similar ...
 172-240 1.15e-03

Doublecortin-like domain found in doublecortin domain-containing protein 5 (DCDC5) and similar proteins; DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of 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. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8 as well as with the Rab8 nucleotide exchange factor Rabin8. This family also includes DCDC1, which is a hydrophilic intracellular protein that contains only one DCX repeat. Therefore, DCDC1 might only bind to microtubules without microtubule polymerization properties. DCDC1 is mainly expressed in adult testis.


Pssm-ID: 340592  Cd Length: 71  Bit Score: 38.41  E-value: 1.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632378  172 RVVFYRNGDpffpGVELR--YRPGRDVTsLDNLLDKISPKMDLPRGARYVFSMDGDRKYHLDELE-DGAFYV 240
Cdd:cd17072     2 RLRVLKNGE----RDLERavYVVGPDLE-LQLFLDRCTERLNLPFAARRLFDENGKEIFTLRDLErDQLVYV 68
DCX2_DCDC2 cd17152
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 178-248 1.47e-03

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It 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 cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340672  Cd Length: 80  Bit Score: 38.63  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632378  178 NGDPFFPGVELRYrPGRDVTSLDNLLDKISPKMDLPRGA-RYVFSMDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17152     9 NGDLLNPAVRLLI-PRKTLNQWEKILEMITEKVTLRTGAvRRLYTLDGKLINDGSELENGQFYVAVGREKFK 79
DCX2_DCLK1 cd17143
Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 315-369 2.91e-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: 2.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  315 RVLLNLRTSQPFEEVLEDLGQVLKIN--GAKKMYTGTGQEVRSfsqLRNEFADVDTF 369
Cdd:cd17143    21 RILLNKKTAHSFEQVLTDITDAIKLDsgVVKRLYTLDGKQVMC---LQDFFGDDDIF 74
DCX3_DCDC5 cd17158
Doublecortin-like domain 3 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is ...
 172-224 4.17e-03

Doublecortin-like domain 3 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of 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. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8.


Pssm-ID: 340678  Cd Length: 73  Bit Score: 36.91  E-value: 4.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632378  172 RVVFYRNGDPffpgvelRYRPGRDV--TSLDNLLDKISPKMDLPRGARYVFSMDG 224
Cdd:cd17158     2 KILAYKNGEG-------RLRDGVLIigSTFPGLLDQCTHRLGLARAARRLYTADG 49
DCX2_DCDC5 cd17157
Doublecortin-like domain 2 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is ...
 171-233 6.26e-03

Doublecortin-like domain 2 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of 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. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8.


Pssm-ID: 340677  Cd Length: 86  Bit Score: 36.94  E-value: 6.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  171 RRVVFYRNGDpffpGVElryrpGRDVTS----LDNLLDKISPKMDLPRGARYVFSMDGDRKYHLDEL 233
Cdd:cd17157     1 RRILVFKNGD----GSE-----GYEIVAdldeFEQFLDACTSKLNLGSPARVLYDWEGKEIKDLSEA 58
WD40 pfam00400
WD domain, G-beta repeat;
520-562 6.82e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 6.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 442632378   520 QRHYTGHTEDIMCMDVHPSRELVASGqkaGRDRksqaHVRIWS 562
Cdd:pfam00400    4 LKTLEGHTGSVTSLAFSPDGKLLASG---SDDG----TVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 521-562 7.57e-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: 35.37  E-value: 7.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 442632378    521 RHYTGHTEDIMCMDVHPSRELVASGqkaGRDRKsqahVRIWS 562
Cdd:smart00320    6 KTLKGHTGPVTSVAFSPDGKYLASG---SDDGT----IKLWD 40
DCX2_DCLK2 cd17144
Dublecortin-like domain 2 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ...
 315-369 8.56e-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: 8.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632378  315 RVLLNLRTSQPFEEVLEDLGQVLKINGA--KKMYTGTGQEVrsfSQLRNEFADVDTF 369
Cdd:cd17144    21 RILLNKKTAHSFEQVLTDITEAIKLDSGvvKRLCTLDGKQV---TCLQDFFGDDDVF 74
DCX2_DCDC2C cd17154
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
 170-248 8.69e-03

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340674  Cd Length: 80  Bit Score: 36.33  E-value: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632378  170 ARRVVFYRNGDPFFPGVELRYrPGRDVTSLDNLLDKISPKMDLPRGA-RYVFSMDGDRKYHLDELEDGAFYVVSSFKAFK 248
Cdd:cd17154     1 SRTINVFTNGEVLVPPAKIII-PKFTLRSWENVLAMITEKAFLRTGGvFRLCTLNGHPVSDSTELEDNHYYVAVGSEKFK 79
 
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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