2C0B,1SN8


Conserved Protein Domain Family
S1_RNase_E
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cd04453: S1_RNase_E 
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S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential endoribonuclease in the processing and degradation of RNA. In addition to its role in mRNA degradation, RNase E has also been implicated in the processing of rRNA, and the maturation of tRNA, 10Sa RNA and the M1 precursor of RNase P. RNase E associates with PNPase (3' to 5' exonuclease), Rhl B (DEAD-box RNA helicase) and enolase (glycolytic enzyme) to form the RNA degradosome. RNase E tends to cut mRNA within single-stranded regions that are rich in A/U nucleotides. The N-terminal region of RNase E contains the catalytic site. Within the conserved N-terminal domain of RNAse E and RNase G, there is an S1-like subdomain, which is an ancient single-stranded RNA-binding domain. S1 domain is an RNA-binding module originally identified in the ribosomal protein S1. The S1 domain is required for RNA cleavage by RNase E. RNase G is paralogous to RNase E with an N-terminal catalytic domain that is highly homologous to that of RNase E. RNase G not only shares sequence similarity with RNase E, but also functionally overlaps with RNase E. In Escherichia coli, RNase G is involved in the maturation of the 5' end of the 16S rRNA. RNase G plays a secondary role in mRNA decay.
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Statistics
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PSSM-Id: 239900
Aligned: 53 rows
Threshold Bit Score: 71.4713
Created: 14-Jun-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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oligonucleotidehomodimer
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:oligonucleotide binding site [chemical binding site]
Evidence:
  • Structure:2C0B_L; Escherichia coli RNase E (RneS1) binds oligonucleotide. Contacts determined at 4Angstrom distance
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                                           #                                       #  #
2C0B_L       39 PGHEQKKANIYKGKITRIEPSLEAAFVDYGa-ERHGFLPlkeiareyfpan-ysahgrpnikdVLREGQEVIVQIDKEER 116 Escherichia coli
YP_756363    35 AGQRVIEGEIYRGRVRRVEPALNAAFVDLGv-GEEGFLPfgks----------------grpkGLHEGAAIGVRIAREAY 97  Maricaulis maris...
BAB06733     31 PVEERIVGNVYRGRVVNVLPGMQACFVDIGr-EKNGFLYrdellsfhlsneeedekkkrnisdFVQEGEELLVQVTKEGF 109 Bacillus halodur...
ZP_01016262  33 DKREALLGDLYRAKVLGHDPRLGAAFVDLGt-GGEGFLRrp--------------------gkLPPVGATLIVEIKREAM 91  Parvularcula ber...
ZP_00957560  25 RGKRAWRGEVYRARVTKIDHAINGAFCDIGr-GPAGFLPfgka----------------grpdGLHEGAAIGVQIAREQF 87  Oceanicaulis ale...
AAD27911     76 VKTNVQCDSVYLGVITKFVPHMGGAFVNIGs-ARHSFMDiksnrepfifp--pfcdgskkqaaDVRKGTKIIVQVVKEGL 152 thale cress
BAE52141     32 DRPSLLLDSVFRGRVTALDKGLDAAFVDLGtgPRPGFLPgar-------------------alGLSEGSAVVARVRAEGR 92  Magnetospirillum...
YP_427851    37 RAHAVETGAIVAGRVTAAVPGHQALFVDLGr-GPAGFLGaedt-----------------prgLPGEGALLAFQVLREAV 98  Rhodospirillum r...
YP_744849    40 PGRPDGFGDMYRGRVIARVSAMAGAFVALPd-GAEGFLPdsac-----------------hasLPKTGEPVFVRVTRSAS 101 Granulibacter be...
CAM74265     30 IRPSLLAGAVVLGRVVELAPKMGAIFVDIGq-DKPGFLQg----------------------vKLNQGASVLVQVKADAQ 86  Magnetospirillum...

Feature 1         ##         #  
2C0B_L      117 GNKGAALTTFISLAGS 132 Escherichia coli
YP_756363    98 AEKGPNLGLVDVEPGE 113 Maricaulis maris MCS10
BAB06733    110 GTKGPRLTGVVAFPGR 125 Bacillus halodurans C-125
ZP_01016262  92 GAKGPDVTDKWSAALP 107 Parvularcula bermudensis HTCC2503
ZP_00957560  88 QEKGPTLALFDVEPGE 103 Oceanicaulis alexandrii HTCC2633
AAD27911    153 GTKGPTLTAYPKLRSR 168 thale cress
BAE52141     93 GGKGPLLTPAGDFPAT 108 Magnetospirillum magneticum AMB-1
YP_427851    99 AGKGPTVTAAPTLAGR 114 Rhodospirillum rubrum ATCC 11170
YP_744849   102 GGKGPRLATIPAPAHD 117 Granulibacter bethesdensis CGDNIH1
CAM74265     87 GLKGAVLTTEVVLSGR 102 Magnetospirillum gryphiswaldense MSR-1

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