1QMH


Conserved Protein Domain Family
RNA_Cyclase
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cd00295: RNA_Cyclase 
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RNA 3' phosphate cyclase domain - RNA phosphate cyclases are enzymes that catalyze the ATP-dependent conversion of 3'-phosphate at the end of RNA into 2', 3'-cyclic phosphodiester bond. The enzymes are conserved in eucaryotes, bacteria and archaea. The exact biological role of this enzyme is unknown, but it has been proposed that it is likely to function in cellular RNA metabolism and processing. RNA phosphate cyclase has been characterized in human (with at least three isozymes), and E. coli, and it seems to be taxonomically widespread. The crystal structure of RNA phospate cyclase shows that it consists of two domains. The larger domain contains three repeats of a fold originally identified in the bacterial translation initiation factor IF3.
Links
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Statistics
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PSSM-Id: 238183
Aligned: 2 rows
Threshold Bit Score: 477.617
Created: 6-Mar-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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putative activeadenylation
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:putative active site [active site]
Evidence:
  • Structure:1QMH_B charged pocket believed to be the active site of RNA cyclase activity
  • Comment:The putative location of the active site of cyclase is supported by mutagenesis experiments
  • Structure:1QMH_B binding citrate, which is believed to mimic the binding of the RNA backbone
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1             ##   #                  #  # #     ##                                   
1QMH_B      8 LDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLLRQHLTAVKAATEICGATVEGAELGSQRLLFRPGTVRGG 87  Escherichia coli
Q09870      3 TGQLKRFKGCEYLTHRLVLATLSGTPIRVEGIYPDEADPGVKDYQVSFLRLLEKLTNGSVIEISYTGTSFIYRPGNIIGG 82  fission yeast

Feature 1                     #                                                               
1QMH_B     88 DYRFAIGSAGSCTLVLQTVLPALWFadGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGIHQQTTLLRHGFYPAGGGV 167 Escherichia coli
Q09870     83 RVVHDCPTTKGIGYFLEPILILCLFakTPTSLTLTGVTSSNEDIGVDVLRTSVLPSLQKRFQVGDELELRILKRGSAPGG 162 fission yeast

Feature 1                                                                                     
1QMH_B    168 VATEVSPVASFNTLQLgerg--nivqMRGEVLLagv--prHVAEREIATLAGSFSLHEQNIHNLPRDq-------GPGNT 236 Escherichia coli
Q09870    163 GGEVNFLCPVIKESLPpirlsefgrvFRIRGIAsstrvspAFANRLVESARGVLNPFIPDVFIYTDVrrgdecgnSPGYS 242 fission yeast

Feature 1                                                        #                      #     
1QMH_B    237 VSLEVEsen-itERFFVVGEKRVSAEVVAAQLVKEVKRYLASTAAVGEYLADQLVLPMALAg-AGEFTVAHPSCHLL--T 312 Escherichia coli
Q09870    243 ITLVAEtnkgcsYAAEHCGEAGETPEDVGSFCAKKLLEVIESGGCVDPYTQPSTLTGMLLSseDVNTIVVGQLGITSqlV 322 fission yeast

Feature 1                       
1QMH_B    313 NIAVV-ERFLPVRFSLIE 329 Escherichia coli
Q09870    323 VFLRDvKALFNCEYRFKE 340 fission yeast

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