UniProtKB - Q2V8X7 (NUD16_SHEEP)
U8 snoRNA-decapping enzyme
NUDT16
Functioni
RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (By similarity).
Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity).
Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
By similarityCatalytic activityi
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H+ + N7-methyl-GDPBy similarityEC:3.6.1.62By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:3.6.1.64By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:3.6.1.64By similarityThis reaction proceeds in the forwardBy similarity direction.
- a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H+ + NAD+By similarityThis reaction proceeds in the forwardBy similarity direction.
- a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + FMN + 2 H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-phosphopantetheine + a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + 2 H+By similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 24 | SubstrateBy similarity | 1 | |
Binding sitei | 50 | SubstrateBy similarity | 1 | |
Binding sitei | 57 | Substrate; via amide nitrogenBy similarity | 1 | |
Metal bindingi | 59 | Manganese 1; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 76 | Manganese 2By similarity | 1 | |
Metal bindingi | 76 | Manganese 3By similarity | 1 | |
Metal bindingi | 80 | Manganese 1By similarity | 1 | |
Metal bindingi | 80 | Manganese 3By similarity | 1 | |
Metal bindingi | 99 | Manganese 4By similarity | 1 | |
Binding sitei | 166 | SubstrateBy similarity | 1 | |
Binding sitei | 170 | SubstrateBy similarity | 1 | |
Metal bindingi | 173 | Manganese 4By similarity | 1 |
GO - Molecular functioni
- cobalt ion binding Source: UniProtKB
- dIDP diphosphatase activity Source: RHEA
- dITP diphosphatase activity Source: UniProtKB
- GTP binding Source: UniProtKB
- inosine-diphosphatase activity Source: UniProtKB-EC
- ITP binding Source: UniProtKB
- m7G(5')pppN diphosphatase activity Source: UniProtKB
- magnesium ion binding Source: UniProtKB
- manganese ion binding Source: UniProtKB
- metalloexopeptidase activity Source: UniProtKB
- mRNA binding Source: UniProtKB
- nucleotide phosphatase activity, acting on free nucleotides Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- RNA NAD-cap (NAD-forming) hydrolase activity Source: RHEA
- snoRNA binding Source: UniProtKB
- XTP binding Source: UniProtKB
GO - Biological processi
- adenosine to inosine editing Source: UniProtKB
- dITP catabolic process Source: UniProtKB
- IDP catabolic process Source: UniProtKB
- mRNA catabolic process Source: UniProtKB
- NAD-cap decapping Source: UniProtKB
- negative regulation of rRNA processing Source: UniProtKB
- positive regulation of cell cycle process Source: UniProtKB
- sno(s)RNA catabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase, RNA-binding |
Biological process | Nucleotide metabolism |
Ligand | Magnesium, Manganese, Metal-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:NUDT16 |
Organismi | Ovis aries (Sheep) |
Taxonomic identifieri | 9940 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Proteomesi |
|
Subcellular locationi
Nucleus
- Nucleus By similarity
- nucleolus By similarity
- nucleoplasm By similarity
Cytoplasm and Cytosol
- Cytoplasm By similarity
Note: Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm.By similarity
Nucleus
- nucleolus Source: UniProtKB
- nucleoplasm Source: UniProtKB-SubCell
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000280398 | 1 – 195 | U8 snoRNA-decapping enzymeAdd BLAST | 195 |
Expressioni
Developmental stagei
Inductioni
Interactioni
Subunit structurei
Homodimer.
By similarityGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 9940.ENSOARP00000009935 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 18 – 168 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 151 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 61 – 82 | Nudix boxAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG502S20E, Eukaryota |
OrthoDBi | 1385294at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR015797, NUDIX_hydrolase-like_dom_sf IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MAGMRRLELA EALHLGPGWR HACHAMLYAP DPGLLFGRIP LRYAVLMQMR
60 70 80 90 100
FDGRLGFPGG FVDLRDGSLE DGLNRELGEE LGEAAAAFRV ERADYRSSHA
110 120 130 140 150
GSRPRVVAHF YTKLLTLEQL TAVEMGAPRA RDHGLEVLGL VRVPLYTLRD
160 170 180 190
RVGGLPAFLE NTFIGNAREQ LLEAVQNLGL LEPGSFAHLK ISTPP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ285424 mRNA Translation: ABB97473.1 DQ285425 Genomic DNA Translation: ABB97474.1 |
RefSeqi | NP_001033102.1, NM_001038013.1 |
Genome annotation databases
GeneIDi | 654329 |
KEGGi | oas:654329 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ285424 mRNA Translation: ABB97473.1 DQ285425 Genomic DNA Translation: ABB97474.1 |
RefSeqi | NP_001033102.1, NM_001038013.1 |
3D structure databases
AlphaFoldDBi | Q2V8X7 |
SMRi | Q2V8X7 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9940.ENSOARP00000009935 |
Genome annotation databases
GeneIDi | 654329 |
KEGGi | oas:654329 |
Organism-specific databases
CTDi | 131870 |
Phylogenomic databases
eggNOGi | ENOG502S20E, Eukaryota |
OrthoDBi | 1385294at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR015797, NUDIX_hydrolase-like_dom_sf IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NUD16_SHEEP | |
Accessioni | Q2V8X7Primary (citable) accession number: Q2V8X7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 20, 2007 |
Last sequence update: | January 10, 2006 | |
Last modified: | May 25, 2022 | |
This is version 79 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families