1EG4,1EG3


Conserved Protein Domain Family
EFh_DMD

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cd16246: EFh_DMD 
Click on image for an interactive view with Cn3D
EF-hand-like motif found in dystrophin
Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.
Statistics
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PSSM-Id: 320004
View PSSM: cd16246
Aligned: 6 rows
Threshold Bit Score: 351.257
Threshold Setting Gi: 82180935
Created: 12-Nov-2014
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 40 residues -Click on image for an interactive view with Cn3D
Feature 1:EF-hand-like motif [structural motif]
Evidence:
  • Comment:The EF-like motifs don't contain the canonical pattern of calcium binding residues.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1         ########################################                                        
1EG4_A         80 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEhnnlvnVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 159
gi 82180935    57 GLSAACEALDQHNLKQNDQLMDILQIINCLTTIYDRLEQEhnnlvnVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGVI 136
gi 118684    3122 NLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEhnnlvnVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGVV 3201
gi 82109132    57 SMPAACEAFEQHNLKQNEQFMDIVQVINCLTSIYDRLEQQhsslvnVPLCVDMCLNWLLNVYDTGRAGKIRTLSFKTGII 136
1EG3_A         80 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEhnnlvnVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 159
gi 632974311   57 SLPSACEAFDQRNLKQNDQLMDIMEIINCLTTIYDRLEQEhsnlvnVPLCVDMCLNWLLNVYDTGRTGKIRVLSFKTGIM 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                         
1EG4_A        160 SlckahLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQlgevasfggsniEPSVRSCFQFANNKPEIEAALFLDW 239
gi 82180935   137 SlckahLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQlgevasfggsniEPSVRSCFQYANNKPEIEAALFLDW 216
gi 118684    3202 SlckahLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQlgevasfggsniEPSVRSCFQFANNKPEIEAALFLDW 3281
gi 82109132   137 SlckahLEDKYRFLFREVASATGFCDQRRLGLLLHDAIQIPRQlgevasfggsniEPSVRSCFQFANNKPELEASVFLDW 216
1EG3_A        160 SlckahLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQlgevasfggsniEPSVRSCFQFANNKPEIEAALFLDW 239
gi 632974311  137 SlckahLEDKYRYLFKQVASPTGFCDQRRLGLLLHDAIQVPRQlgevasfggsniEPSVRSCFQFANNKPDIEAALFLDW 216

                  ..
Feature 1           
1EG4_A        240 MR 241
gi 82180935   217 MR 218
gi 118684    3282 MR 3283
gi 82109132   217 MR 218
1EG3_A        240 MR 241
gi 632974311  217 MR 218

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