Conserved Protein Domain Family
ACD_HspB3_Like

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cd06477: ACD_HspB3_Like 
Alpha crystallin domain (ACD) found in mammalian HspB3, also known as heat-shock protein 27-like protein (HSPL27, 17-kDa) and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB3 is expressed in adult skeletal muscle, smooth muscle, and heart, and in several other fetal tissues. In muscle cells HspB3 forms an oligomeric 150 kDa complex with myotonic dystrophy protein kinase-binding protein (MKBP/ HspB2), this complex may comprise one of two independent muscle-cell specific chaperone systems. The expression of HspB3 is induced during muscle differentiation controlled by the myogenic factor MyoD. HspB3 may also interact with Hsp22 (HspB8).
Statistics
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PSSM-Id: 107232
View PSSM: cd06477
Aligned: 4 rows
Threshold Bit Score: 154.196
Threshold Setting Gi: 163916234
Created: 28-May-2008
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
putative dimer
Feature 1:putative dimer interface [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #####      # # ##                                    #                     ##   
gi 47496575   63 PPREGksHFQILLDVVQFLPEDIIIQTFEGWLLIKAQhGTRMDEHGFIsRSFTRQYKLPDGVEIk-dLSAVLCHDGILVV 141
gi 163916234  52 QQEEDd-KFKVLLDVVQFRPEDIIIQVFEGWLIIKGEhGCRMDEHGFIsRSFTRTYQLPNGIGLt-dLSAFFCHDGILAV 129
gi 118103780  62 SQEEEktGFQVLLDVVQFRPEDIIIQTFEGWLLIKAQhGPRMDEHGFIsRSFTRQYKLPDGVENk-dLSALFCHDGILVV 140
gi 150832514  60 DEDSGepMFQILLDVTQFKPEDILIQVFEGWLLIRGRhGVRMGEHGLVsRSFTRHYQLPDCQLHagdLKAMLCHDGMLVV 139

                 ....
Feature 1            
gi 47496575  142 EVKD 145
gi 163916234 130 EGKQ 133
gi 118103780 141 EMKN 144
gi 150832514 140 ETKD 143

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