ID   D9_VACCW                Reviewed;         213 AA.
AC   P04311; Q76ZR8;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=mRNA-decapping protein D9;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=VACWR114; ORFNames=D9R;
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-126 AND 129-GLU-GLU-130.
RX   PubMed=17881455; DOI=10.1128/jvi.01668-07;
RA   Parrish S., Moss B.;
RT   "Characterization of a second vaccinia virus mRNA-decapping enzyme
RT   conserved in poxviruses.";
RL   J. Virol. 81:12973-12978(2007).
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. Does not cleave
CC       unmethylated RNAs or RNAs shorter than 24 nucleotides.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; M15058; AAA48265.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89393.1; -; Genomic_DNA.
DR   PIR; A03885; QQVZ15.
DR   RefSeq; YP_232996.1; NC_006998.1.
DR   DIP; DIP-2192N; -.
DR   IntAct; P04311; 1.
DR   MINT; P04311; -.
DR   DNASU; 3707570; -.
DR   GeneID; 3707570; -.
DR   KEGG; vg:3707570; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR003300; Viral_VD9.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR01363; VD09PROTEIN.
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..213
FT                   /note="mRNA-decapping protein D9"
FT                   /id="PRO_0000057093"
FT   DOMAIN          30..209
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           111..132
FT                   /note="Nudix box"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         126
FT                   /note="E->Q: Complete loss of mRNA decapping activity."
FT                   /evidence="ECO:0000269|PubMed:17881455"
FT   MUTAGEN         129..130
FT                   /note="EE->QQ: Complete loss of mRNA decapping activity."
FT                   /evidence="ECO:0000269|PubMed:17881455"
SQ   SEQUENCE   213 AA;  24994 MW;  306288883C5899A5 CRC64;
     MGITMDEEVI FETPRELISI KRIKDIPRSK DTHVFAACIT SDGYPLIGAR RTSFAFQAIL
     SQQNSDSIFR VSTKLLRFMY YNELREIFRR LRKGSINNID PHFEELILLG GKLDKKESIK
     DCLRRELKEE SDERITVKEF GNVILKLTTR DKLFNKVYIG YCMACFINQS LEDLSHTSIY
     NVEIRKIKSL NDCINDDKYE YLSYIYNMLV NSK