CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ADP-sugar pyrophosphatase 
Protein Synonyms/Alias
 8-oxo-dGDP phosphatase; Nucleoside diphosphate-linked moiety X motif 5; Nudix motif 5 
Gene Name
 Nudt5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
42TYMDPTGKTRTWETVacetylation[1]
57KLTTRKGKSADAVSVacetylation[1]
210ALKHANAKPFEVPFLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Hydrolyzes with similar activities ADP-ribose and ADP- mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (By similarity). 
Sequence Annotation
 DOMAIN 57 197 Nudix hydrolase.
 REGION 46 47 Substrate binding; shared with dimeric
 MOTIF 97 118 Nudix box.
 METAL 96 96 Magnesium 1; via carbonyl oxygen (By
 METAL 112 112 Magnesium 2 (By similarity).
 METAL 112 112 Magnesium 3 (By similarity).
 METAL 116 116 Magnesium 1 (By similarity).
 METAL 116 116 Magnesium 3 (By similarity).
 METAL 166 166 Magnesium 3 (By similarity).
 BINDING 28 28 Substrate (By similarity).
 BINDING 84 84 Substrate (By similarity).
 BINDING 98 98 Substrate; via amide nitrogen (By
 BINDING 133 133 Substrate (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 9 9 Phosphoserine (By similarity).
 MOD_RES 10 10 Phosphoserine (By similarity).
 MOD_RES 210 210 N6-acetyllysine (By similarity).
 MOD_RES 218 218 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 219 AA 
Protein Sequence
METQEPKDSS PPTEQRILSE ELISEGKWVK FEKTTYMDPT GKTRTWETVK LTTRKGKSAD 60
AVSVIPVLQR TLHHECIVLV KQFRPPMGGY CLEFPAGLIE DGESPEAAAL RELEEETGYK 120
GDIAECSPAV CMDPGLSNCT THVVTVTING DDAGNVRPKP KPGDGEFVEV ISLPKNDLLT 180
RLDALGAEDR LTVDARVYAY ALALKHANAK PFEVPFLKF 219 
Gene Ontology
 GO:0047631; F:ADP-ribose diphosphatase activity; IEA:EC.
 GO:0019144; F:ADP-sugar diphosphatase activity; ISS:UniProtKB.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0030515; F:snoRNA binding; ISS:UniProtKB.
 GO:0009191; P:ribonucleoside diphosphate catabolic process; ISS:UniProtKB. 
Interpro
 IPR020476; Nudix_hydrolase.
 IPR020084; NUDIX_hydrolase_CS.
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 
Pfam
 PF00293; NUDIX 
SMART
  
PROSITE
 PS51462; NUDIX
 PS00893; NUDIX_BOX 
PRINTS
 PR00502; NUDIXFAMILY.