Tag | Content |
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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 |
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102 | RLGPGELKSGGFRRE | acetylation | [1] | 152 | DEISPGDKQKDPKTR | acetylation | [1] | 210 | GTGSSRRKAEQAAAE | acetylation | [1, 2] | 221 | AAAEQALKKLELE** | acetylation | [1] |
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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 |
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