NUD16_HOMVI
ID NUD16_HOMVI Reviewed; 187 AA.
AC P0DKY8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=U8 snoRNA-decapping enzyme;
DE EC=3.6.1.62 {ECO:0000269|PubMed:18820299};
DE AltName: Full=IDP phosphatase;
DE Short=IDPase;
DE EC=3.6.1.64 {ECO:0000250|UniProtKB:Q96DE0};
DE AltName: Full=Inosine diphosphate phosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 16;
DE Short=Nudix motif 16;
DE AltName: Full=m7GpppN-mRNA hydrolase;
GN Name=NUDT16;
OS Homalodisca vitripennis (Glassy-winged sharpshooter) (Homalodisca
OS coagulata).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Membracoidea;
OC Cicadellidae; Cicadellinae; Proconiini; Homalodisca.
OX NCBI_TaxID=197043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Hunter W.B., Dang P.M., Puterka G., Shatters R.G., McKenzie C.L.,
RA Sinisterra X.H.;
RT "Expressed sequence tags from 5th Instar Glassy-winged Sharpshooter,
RT Homalodisca coagulata (Hemiptera: Cicadellidae).";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION AS A DECAPPING ENZYME, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RX PubMed=18820299; DOI=10.1093/nar/gkn605;
RA Taylor M.J., Peculis B.A.;
RT "Evolutionary conservation supports ancient origin for Nudt16, a nuclear-
RT localized, RNA-binding, RNA-decapping enzyme.";
RL Nucleic Acids Res. 36:6021-6034(2008).
CC -!- FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage
CC of the cap structure of snoRNAs in a metal-dependent manner. Has
CC diphosphatase activity and removes m7G caps from U8 snoRNA
CC (PubMed:18820299). May catalyze the cleavage of the cap structure on
CC mRNAs. May also act as a phosphatase; hydrolyzes the non-canonical
CC purine nucleotides inosine diphosphate (IDP) and deoxyinosine
CC diphosphate (dITP) (By similarity). May bind to the U8 snoRNA.
CC {ECO:0000250|UniProtKB:Q96DE0, ECO:0000269|PubMed:18820299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000269|PubMed:18820299};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000269|PubMed:18820299};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.64;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dIDP + H2O = dIMP + H(+) + phosphate; Xref=Rhea:RHEA:35211,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61194, ChEBI:CHEBI:62286; EC=3.6.1.64;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35212;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18820299};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18820299};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18820299};
CC Note=Decapping activity is higher in the presence of manganese than in
CC Magnesium or cobalt. {ECO:0000269|PubMed:18820299};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96DE0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96DE0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DKY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DKY8-2; Sequence=VSP_046049;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NUDT16 subfamily.
CC {ECO:0000305}.
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DR EMBL; DN199400; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DKY8; -.
DR SMR; P0DKY8; -.
DR PRIDE; P0DKY8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097383; F:dIDP diphosphatase activity; IEA:RHEA.
DR GO; GO:1990003; F:inosine-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; Nucleus;
KW RNA-binding.
FT CHAIN 1..187
FT /note="U8 snoRNA-decapping enzyme"
FT /id="PRO_0000421836"
FT DOMAIN 43..187
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 85..106
FT /note="Nudix box"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046049"
SQ SEQUENCE 187 AA; 21100 MW; F3C2AED20B855122 CRC64;
MSSDTGDRTW GHLAATEHYG RITDTTDYIQ VDKENLKNDP YYNSSQASHC MIFARNNKKT
FGVYNPRAAI LMQMRFDGNL GFPGGLVDAG EDSIKALNRE LTEEMNLDTS KHSVSESSYV
VTHWSISKRL CLHFYALEVS LAELYEIEKR ALLAKDYGSE VLGTIRMPLY TMGDGYRGFP
TFLTTPS
