Conserved Protein Domain Family
RING-HC_MuRF_C-II

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cd16577: RING-HC_MuRF_C-II 
RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55/MuRF-2 and TRIM54/MuRF-3
This family corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.
Statistics
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PSSM-Id: 319491
View PSSM: cd16577
Aligned: 10 rows
Threshold Bit Score: 87.492
Threshold Setting Gi: 260791768
Created: 3-May-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding siteRING-HC finger
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Mus musculus RNF146 (4QPL) binds two Zn2+ ions through its RING-HC finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
Feature 1          #  #            # #  #  #                           #  # 
gi 209572715  24 LICPICLEMFSKPvVILPCQHNLCRKCANDVFqasnplwqsrgsttvssggrFRCPSCR 82
gi 193083079  22 LMCPICLEIYTKPvVILPCQHNLCRKCANDVFqnrgtp--------mgsggrFRCPTCR 72
gi 229287735   8 LTCPICLEMFNKPvLILPCQHNLCRKCANDVFqsrgtps------vvgsggrFRCPTCR 60
gi 78099806   24 LICPICLEMFTKPvVILPCQHNLCRKCASDIFqasnpylptrggttmasggrFRCPSCR 82
gi 21362898   21 LICPICLEMFTKPvVILPCQHNLCRKCANDIFqaanpywtsrgssvsmsggrFRCPTCR 79
gi 632939270  24 LICPICLEMFTKPvVILPCQHNLCRKCANDIFqsrgta--------lgsggrFRCPSCR 74
gi 465973126 206 LICPICLEVFTKPvVILPCQHNLCRKCANDIFqsrgtt--------lgsagrFRCPSCR 256
gi 41055281   23 LSCPICLDMFTKPvVILPCQHNLCRGCASDLYdsrnpy--------rfsggvFRCPTCR 73
gi 260791768  39 LKCPICLDLLTVPvLMLPCQHNFCQACLQDMFqgpy------------rsrrIRCPVCR 85
gi 260831196   8 LHCPVCLDVYTKPvLMLPCQHNLCRQCVQNIVytqdeddegy-rggpgrpsaFPCPQCR 65

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