CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
52ALLDACLKVRQQQGDacetylation[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
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. 
Interpro
 IPR002589; A1pp.
 IPR024900; O-Ac-ADP-ribose_deAcase. 
Pfam
 PF01661; Macro 
SMART
 SM00506; A1pp 
PROSITE
 PS51154; MACRO 
PRINTS