ID   D9_RFVKA                Reviewed;         206 AA.
AC   P32098; Q9Q8Z3;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=mRNA-decapping protein D9;
DE            EC=3.1.3.-;
GN   ORFNames=D9R, s084R;
OS   Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS   Kasza)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=10272;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1660196; DOI=10.1016/0042-6822(91)90529-k;
RA   Strayer D.S., Jerng H.H., O'Connor K.;
RT   "Sequence and analysis of a portion of the genomes of Shope fibroma virus
RT   and malignant rabbit fibroma virus that is important for viral replication
RT   in lymphocytes.";
RL   Virology 185:585-595(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1329373; DOI=10.1016/0168-1702(92)90104-h;
RA   Strayer D.S., Jerng H.H.;
RT   "Sequence and analysis of the BamHI 'D' fragment of Shope fibroma virus:
RT   comparison with similar regions of related poxviruses.";
RL   Virus Res. 25:117-132(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA   Willer D.O., McFadden G., Evans D.H.;
RT   "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL   Virology 264:319-343(1999).
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; M74532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF170722; AAF17968.1; -; Genomic_DNA.
DR   RefSeq; NP_051973.1; NC_001266.1.
DR   PRIDE; P32098; -.
DR   GeneID; 1486929; -.
DR   KEGG; vg:1486929; -.
DR   Proteomes; UP000000868; 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..206
FT                   /note="mRNA-decapping protein D9"
FT                   /id="PRO_0000057091"
FT   DOMAIN          23..206
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           104..125
FT                   /note="Nudix box"
FT   ACT_SITE        119
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  24030 MW;  035A1A2E1CD0DCDD CRC64;
     MTTFETPRET VFIESVDSIP QSKKTHVFAI CVTVDNKPIV AARRSSFVFQ EITMNMNPPI
     VVTISKHLTN YMYNNEIKEI KRKLQKGSAP IYKTSFEELI LLGGKLNKSE TIDDCIRREI
     KEETDSKLTI KSIGTTCVKI TITDKLFNRK YVNYCKLCYI DELMEEVISF VIYNVEIRKL
     KSLLDCDNND KFNYLRFIYN TLLYSK