Tag | Content |
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CPLM ID | CPLM-003083 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | O-acetyl-ADP-ribose deacetylase |
Protein Synonyms/Alias | Regulator of RNase III activity |
Gene Name | ymdB |
Gene Synonyms/Alias | b1045; JW1032 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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52 | ALLDACLKVRQQQGD | 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 | Deacetylates O-acetyl-ADP ribose. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation. |
Sequence Annotation | DOMAIN 1 175 Macro. REGION 121 127 Substrate binding (Probable). ACT_SITE 35 35 Proton acceptor (Potential). |
Keyword | 3D-structure; Complete proteome; Hydrolase; Reference proteome; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 177 AA |
Protein Sequence | MKTRIHVVQG DITKLAVDVI VNAANPSLMG GGGVDGAIHR AAGPALLDAC LKVRQQQGDC 60 PTGHAVITLA GDLPAKAVVH TVGPVWRGGE QNEDQLLQDA YLNSLRLVAA NSYTSVAFPA 120 ISTGVYGYPR AAAAEIAVKT VSEFITRHAL PEQVYFVCYD EENAHLYERL LTQQGDE 177 |
Gene Ontology | GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; IDA:EcoCyc. GO:0001883; F:purine nucleoside binding; IEA:HAMAP. GO:0008428; F:ribonuclease inhibitor activity; IDA:EcoCyc. GO:0032074; P:negative regulation of nuclease activity; IDA:EcoCyc. GO:0060701; P:negative regulation of ribonuclease activity; IEA:HAMAP. GO:0042278; P:purine nucleoside metabolic process; IEA:HAMAP. GO:0006950; P:response to stress; IEA:UniProtKB-KW. |
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