Tag | Content |
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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 |
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42 | TYMDPTGKTRTWETV | acetylation | [1] | 57 | KLTTRKGKSADAVSV | acetylation | [1] | 210 | ALKHANAKPFEVPFL | acetylation | [1] |
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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. |
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SMART | |
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PRINTS | |