Conserved Protein Domain Family
DSRM_RED2_rpt2

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cd19899: DSRM_RED2_rpt2 
second double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins
RED2 (also known as double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the second DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. RED2 lacks editing activity for currently known substrate RNAs, and may have an inactive editase domain.
Statistics
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PSSM-Id: 380728
Aligned: 6 rows
Threshold Bit Score: 125.756
Created: 24-Oct-2018
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative RNA
Feature 1:putative RNA binding site [nucleic acid binding site]
Evidence:
  • Comment:Based on structure evidence that Rattus norvegicus RED1 (2L3J) binds dsRNA.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1               # ##  ##                ### # #               ####  #               
Q9NS39       271 PAAPGERNPVVLLNRLRAGLRYVCLAEPA--ERRARSFVMAVSVDGRTFEGSGRSKKLARGQAAQAALQELFDIQ 343 human
PKK31818     221 SKAESEKNPVVLLNELRSGLRYVCLSETVe-KQHSKSFVMAVRVDGRTFEGSGRSKKLAKGQAAQAALQALFNIR 294 rock pigeon
OCT75526     229 SPAEREKNPVVMLNELRPGLRYVCLSETVe-KQHIKRFVMAMRVDGRTFEGSGRSKKLAKAQAAQNALQDLFNIR 302 African clawed frog
XP_006001115 261 SPTESNKNPVVLLNELRPGLRYVCLSETVe-KQHIKSFVMAVRVDGRTFEGLGRSKKLAKTHAAQAALQTLFNIK 334 coelacanth
CAK10842     242 PVSPPQPSPVVLLNDLRPGLRYACLSEHAqgKRAHRSFIMAVRVDGRIFEGSGRSKKQAKRQAAVCALQALFNFR 316 zebrafish
XP_007899400 289 FPAASRKNPVEMLNELRPGLSYVCLSEMA--EKHVKSFVMAVSVDGRTFEGSGRSKKLAKAQSAQAALQTLFNIQ 361 elephant shark

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