Tag | Content |
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CPLM ID | CPLM-002751 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribonuclease D |
Protein Synonyms/Alias | RNase D |
Gene Name | rnd |
Gene Synonyms/Alias | b1804; JW1793 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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273 | SEIRFHGKTLLALVE | acetylation | [1] | 308 | PGYRKAFKAIKSLIT | acetylation | [1] | 311 | RKAFKAIKSLITDVS | acetylation | [1] | 343 | QLLNWHWKLKPQNNL | 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] |
Functional Description | Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides. |
Sequence Annotation | DOMAIN 3 169 3'-5' exonuclease. DOMAIN 210 289 HRDC. |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase; Nuclease; Reference proteome; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 375 AA |
Protein Sequence | MNYQMITTDD ALASLCEAVR AFPAIALDTE FVRTRTYYPQ LGLIQLFDGE HLALIDPLGI 60 TDWSPLKAIL RDPSITKFLH AGSEDLEVFL NVFGELPQPL IDTQILAAFC GRPMSWGFAS 120 MVEEYSGVTL DKSESRTDWL ARPLTERQCE YAAADVWYLL PITAKLMVET EASGWLPAAL 180 DECRLMQMRR QEVVAPEDAW RDITNAWQLR TRQLACLQLL ADWRLRKARE RDLAVNFVVR 240 EEHLWSVARY MPGSLGELDS LGLSGSEIRF HGKTLLALVE KAQTLPEDAL PQPMLNLMDM 300 PGYRKAFKAI KSLITDVSET HKISAELLAS RRQINQLLNW HWKLKPQNNL PELISGWRGE 360 LMAEALHNLL QEYPQ 375 |
Gene Ontology | |
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