ID   D9_VACCC                Reviewed;         213 AA.
AC   P21011;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=mRNA-decapping protein D9;
DE            EC=3.1.3.-;
GN   ORFNames=D9R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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 (By similarity).
CC       {ECO:0000250}.
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; M35027; AAA48108.1; -; Genomic_DNA.
DR   PIR; H42515; H42515.
DR   Proteomes; UP000008269; 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   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..213
FT                   /note="mRNA-decapping protein D9"
FT                   /id="PRO_0000057092"
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"
SQ   SEQUENCE   213 AA;  25024 MW;  747688883C43EF7E CRC64;
     MGITMDEEVI FETPRELISI KRIKDIPRSK DTHVFAACIT SDGYPLIGAR RTSFAFQAIL
     SQQNSDSIFR VSTKLLRFMY YNELREIFRR LRKGSINNID PHFEELILLG GKLDKKESIK
     DCLRRELKEE SDERITVKEF GNVILKLTTR DKLFNKVYIS YCMACFINQS LEDLSHTSIY
     NVEIRKIKSL NDCINDDKYE YLSYIYNMLV NSK