3MOJ,2G0C


Conserved Protein Domain Family
RRM_BsYxiN_like

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cd12500: RRM_BsYxiN_like 
Click on image for an interactive view with Cn3D
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins
This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.
Statistics
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PSSM-Id: 409923
Aligned: 5 rows
Threshold Bit Score: 100.998
Created: 5-Mar-2012
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
 
RNA binding
Conserved site includes 22 residues -Click on image for an interactive view with Cn3D
Feature 1:RNA binding site [nucleic acid binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1            ##   #### ### ##     #  ####                          #####  #    
3MOJ_B      2 KLYFNGGKKkKIRAVDFVGTIAKidGVSADDIGIITIMDNASYVEILngKGPHVLKVMKNtTVKGKQLKVNKA 74  Bacillus subtilis
Q8XM28    404 KIHVNGGKKkKIRAFDIVGCFSNlpGLTGEDIGIIDVQDGFSYVDILngKGDKVLKSFKEvTIKGKKVKIQKA 476 Clostridium perfringens
Q185X0    423 KLYLNAGKKkKIRVLDIVGAFSNikGITNDDIGVIEVQDLCSYVDILnyKGDLILKKYKEiPIKKKMVKVKRD 495 Clostridium difficile 630
EFW03787  403 RLYFSVGKRkKIAAGNLVGAICAleDVNGDDIGIIQVQDMCSYVDILngKGKSVAQRLNNtLIKGRTMKVEIA 475 Coprobacillus sp. 29_1
2G0C_A      2 KLYFNGGKKkKIRAVDFVGTIAKidGVSADDIGIITIMDNASYVEILngKGPHVLKVMKNtTVKGKQLKVNKA 74  Bacillus subtilis

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