D10_VACCW
ID D10_VACCW Reviewed; 248 AA.
AC P04312; Q76ZR7;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=mRNA-decapping protein D10;
DE EC=3.1.3.-;
GN OrderedLocusNames=VACWR115; ORFNames=D10R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT fragment.";
RL Virology 153:96-112(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLU-141; GLU-144 AND GLU-145.
RX PubMed=17283339; DOI=10.1073/pnas.0611685104;
RA Parrish S., Resch W., Moss B.;
RT "Vaccinia virus D10 protein has mRNA decapping activity, providing a
RT mechanism for control of host and viral gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2139-2144(2007).
RN [4]
RP CHARACTERIZATION, COFACTOR, AND MUTAGENESIS OF GLU-132; GLU-141 AND
RP GLU-145.
RX PubMed=19210265; DOI=10.1042/bj20082296;
RA Souliere M.F., Perreault J.P., Bisaillon M.;
RT "Characterization of the vaccinia virus D10 decapping enzyme provides
RT evidence for a two-metal-ion mechanism.";
RL Biochem. J. 420:27-35(2009).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLU-99; ARG-118; ASP-120; LYS-129;
RP GLU-144; ASP-167; LYS-220 AND TYR-221.
RX PubMed=20639534; DOI=10.1093/nar/gkq628;
RA Souliere M.F., Perreault J.-P., Bisaillon M.;
RT "Insights into the molecular determinants involved in cap recognition by
RT the vaccinia virus D10 decapping enzyme.";
RL Nucleic Acids Res. 38:7599-7610(2010).
CC -!- FUNCTION: Decapping enzyme required for the removal of the 5'-end
CC m7GpppN cap tethered to viral and host mRNAs to allow their decay in
CC cells. May therefore accelerate viral and cellular mRNA turnover to
CC eliminate competing host mRNAs and allow stage-specific synthesis of
CC viral proteins. Acceleration of the turnover of cellular transcripts
CC may even promote the shutoff of host protein synthesis.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19210265};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19210265};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 nM for capped RNA;
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; M15058; AAA48266.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89394.1; -; Genomic_DNA.
DR PIR; A03886; QQVZ16.
DR RefSeq; YP_232997.1; NC_006998.1.
DR DNASU; 3707571; -.
DR GeneID; 3707571; -.
DR KEGG; vg:3707571; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR003301; Vaccinia_D10_decapping.
DR InterPro; IPR013683; Vaccinia_D10_N.
DR Pfam; PF08476; VD10_N; 1.
DR PRINTS; PR01364; VD10PROTEIN.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..248
FT /note="mRNA-decapping protein D10"
FT /id="PRO_0000057098"
FT DOMAIN 45..227
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 126..147
FT /note="Nudix box"
FT ACT_SITE 141
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT MUTAGEN 99
FT /note="E->A: 90% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
FT MUTAGEN 118
FT /note="R->A: 90% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
FT MUTAGEN 120
FT /note="D->A: 90% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
FT MUTAGEN 129
FT /note="K->A: 90% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
FT MUTAGEN 132
FT /note="E->A: 5-fold loss of affinity for magnesium, no
FT effect on manganese affinity."
FT /evidence="ECO:0000269|PubMed:19210265"
FT MUTAGEN 141
FT /note="E->A: Slight change in magnesium or manganese
FT binding."
FT /evidence="ECO:0000269|PubMed:17283339,
FT ECO:0000269|PubMed:19210265"
FT MUTAGEN 141
FT /note="E->Q: Complete loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:17283339,
FT ECO:0000269|PubMed:19210265"
FT MUTAGEN 144
FT /note="E->A: 90% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:17283339,
FT ECO:0000269|PubMed:20639534"
FT MUTAGEN 144
FT /note="E->Q: Complete loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:17283339,
FT ECO:0000269|PubMed:20639534"
FT MUTAGEN 145
FT /note="E->A: 2-fold loss of affinity for magnesium, 6-fold
FT loss of affinity for manganese."
FT /evidence="ECO:0000269|PubMed:17283339,
FT ECO:0000269|PubMed:19210265"
FT MUTAGEN 145
FT /note="E->Q: Complete loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:17283339,
FT ECO:0000269|PubMed:19210265"
FT MUTAGEN 167
FT /note="D->A: 75% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
FT MUTAGEN 220
FT /note="K->A: 75% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
FT MUTAGEN 221
FT /note="Y->A: 75% loss of decapping activity."
FT /evidence="ECO:0000269|PubMed:20639534"
SQ SEQUENCE 248 AA; 28913 MW; D302B5994EBF259B CRC64;
MNFYRSSIIS QIIKYNRRLA KSIICEDDSQ IITLTAFVNQ CLWCHKRVSV SAILLTTDNK
ILVCNRRDSF LYSEIIRTRN MFRKKRLFLN YSNYLNKQER SILSSFFSLD PATADNDRID
AIYPGGIPKR GENVPECLSR EIKEEVNIDN SFVFIDTRFF IHGIIEDTII NKFFEVIFFV
GRISLTSDQI IDTFKSNHEI KDLIFLDPNS GNGLQYEIAK YALDTAKLKC YGHRGCYYES
LKKLTEDD
