Conserved Protein Domain Family
RING-HC_TRIM58_C-IV

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cd16606: RING-HC_TRIM58_C-IV 
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins
TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV 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, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Statistics
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PSSM-Id: 319520
View PSSM: cd16606
Aligned: 4 rows
Threshold Bit Score: 110.111
Threshold Setting Gi: 545808543
Created: 19-Apr-2016
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 Homo sapiens TRIM31 (2YSL) 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 124053416  13 DARCPVCLDFLQePVSVDCGHSFCLRCISEFCEKSDGAQgGVYACPQCRGP 63
gi 545808543  13 EARCPVCLDFLQnPVSVDCGHSFCLKCISEFCEKSDSAQsGLYACPQCRGP 63
gi 671034525  13 EARCPVCLDFLQdPVSVACGHSFCLRCISEFCEKSDSAQgGLYACPQCRGP 63
gi 81889233   12 EARCSVCLDFLQePISVDCGHSFCLRCISEFCEKSDSAQ-GVYACPQCRGP 61

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