CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003040
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease 3 
Protein Synonyms/Alias
 Ribonuclease III; RNase III 
Gene Name
 rnc 
Gene Synonyms/Alias
 b2567; JW2551 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
102RLGPGELKSGGFRREacetylation[1]
152DEISPGDKQKDPKTRacetylation[1]
210GTGSSRRKAEQAAAEacetylation[1, 2]
221AAAEQALKKLELE**acetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111
Functional Description
 Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, showing substrate recognition is different. Removes the intervening sequences from Salmonella typhimurium rRNA precursor. 
Sequence Annotation
 DOMAIN 6 128 RNase III.
 DOMAIN 155 225 DRBM.
 ACT_SITE 45 45 Potential.
 ACT_SITE 117 117 Probable.
 METAL 41 41 Magnesium (Probable).
 METAL 114 114 Magnesium (By similarity).
 METAL 117 117 Magnesium (Probable).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Metal-binding; mRNA processing; Nuclease; Nucleotide-binding; Reference proteome; RNA-binding; rRNA processing; rRNA-binding; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 226 AA 
Protein Sequence
MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSY VIANALYHRF 60
PRVDEGDMSR MRATLVRGNT LAELAREFEL GECLRLGPGE LKSGGFRRES ILADTVEALI 120
GGVFLDSDIQ TVEKLILNWY QTRLDEISPG DKQKDPKTRL QEYLQGRHLP LPTYLVVQVR 180
GEAHDQEFTI HCQVSGLSEP VVGTGSSRRK AEQAAAEQAL KKLELE 226 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004525; F:ribonuclease III activity; IDA:EcoCyc.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:HAMAP.
 GO:0006396; P:RNA processing; IDA:EcoCyc.
 GO:0016075; P:rRNA catabolic process; IEA:InterPro.
 GO:0006364; P:rRNA processing; IEA:HAMAP.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR011907; RNase_III.
 IPR000999; RNase_III_dom. 
Pfam
 PF00035; dsrm
 PF00636; Ribonuclease_3 
SMART
 SM00358; DSRM
 SM00535; RIBOc 
PROSITE
 PS50137; DS_RBD
 PS00517; RNASE_3_1
 PS50142; RNASE_3_2 
PRINTS