Conserved Protein Domain Family
ACD_sHsps-like

?
cd06464: ACD_sHsps-like 
Click on image for an interactive view with Cn3D
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.
Statistics
?
PSSM-Id: 107221
View PSSM: cd06464
Aligned: 813 rows
Threshold Bit Score: 27.9037
Threshold Setting Gi: 149431914
Created: 8-Jul-2008
Updated: 17-Jan-2013
Structure
?
Program:
Drawing:
Aligned Rows:
 
putative dimer
Conserved site includes 12 residues -Click on image for an interactive view with Cn3D
Feature 1:putative dimer interface [polypeptide binding site]
Evidence:
  • Structure:2H50, Saccharomyces cerevisiae Hsp26 dimer interface, contacts at 3.5 A
    View structure with Cn3D
  • Comment:ScHsp26 assembles in shell-like particles composed of 24 subunits. These particles are storage forms which upon heat shock disassociate into dimers. Non-native substrate proteins bind the disassociated ScHsp26 and assemble into large globular assemblies having one monomer of substrate bound per dimer.
  • Structure:1GME_A, Triticum aestivum sHsp dimer interface, contacts at 3.5 A
    View structure with Cn3D
  • Comment:T. aestivum HSP16.9 assembles as a 12-mer, comprised of two discs, each disc having 6 alpha crystallin-like domains organized as a trimer of dimers.

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #####          # # ##                                        #                  
2BOL_A       102 DAYEVgkdgrlHFKVYFNVKN-FKAEEITIKADknKLVVRAQksvacg----daamsESVGRSIpLPPSVDRnhIQATIT 176
gi 156375673  54 KSADK------VTIATLDIGR-YRPEDITWSVEddHVLICGKhcakts----rgaegGKFVRSIpLPEDIKTqsVTARFC 122
gi 156362234   1 MEGDK------VEIATLDVKN-YRPEEISLKVEhgRIKIDGKhksege----hgyetSEFHRSYnLPDGVDVstVSSRIT 69
gi 156348268   1 MDADK------FQIATLDVRE-FKPEEITCKVEngKIKVSGLqrhese----egfdsKEFRRCYnLPEGVDEssISTRIA 69
gi 47496575   63 PPREGk----sHFQILLDVVQ-FLPEDIIIQTFegWLLIKAQhgtrmd---ehgfisRSFTRQYkLPDGVEIkdLSAVLC 134
gi 118103780  62 SQEEEk----tGFQVLLDVVQ-FRPEDIIIQTFegWLLIKAQhgprmd---ehgfisRSFTRQYkLPDGVENkdLSALFC 133
gi 163916234  52 QQEEDd-----KFKVLLDVVQ-FRPEDIIIQVFegWLIIKGEhgcrmd---ehgfisRSFTRTYqLPNGIGLtdLSAFFC 122
gi 13625983  230 DEATGg----eKLHVEVPIEPeFTADDLCVRMDanRVIVSGQkkyvdetassksahvKEFTRSYeIPETVDTfsVNSQLH 305
gi 129359    261 DDGSGg----kRLHVEVAVDPvYKPEDLFVNVDsnRVVVSGRhhkqksdqhgrsssfAEFSQSYaIPETVDPlsVSAQVV 336
gi 56752663  384 GINGRk----lHLEVTVDSIY-KADELCVRMDSn-CIVISGCqkkteg----sssstAEFTQSFeIPETVDPfsVTAQLI 453
                         90
                 ....*....|..
Feature 1           ##       
2BOL_A       177 t-dDVLVIEAPV 187
gi 156375673 123 mrdGQLIVEGTK 134
gi 156362234  70 g-dGLLHIEALK 80
gi 156348268  70 e-dGMLHVEALK 80
gi 47496575  135 h-dGILVVEVKD 145
gi 118103780 134 h-dGILVVEMKN 144
gi 163916234 123 h-dGILAVEGKQ 133
gi 13625983  306 g--NTLLVEAPL 315
gi 129359    337 g--NTLVLEAPL 346
gi 56752663  454 g--TTLVVEAPL 463

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap