ID   D10_VACCC               Reviewed;         248 AA.
AC   P21012;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=mRNA-decapping protein D10;
DE            EC=3.1.3.-;
GN   ORFNames=D10R;
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 (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 late phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; M35027; AAA48109.1; -; Genomic_DNA.
DR   PIR; I42515; I42515.
DR   Proteomes; UP000008269; 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   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..248
FT                   /note="mRNA-decapping protein D10"
FT                   /id="PRO_0000057097"
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:0000250"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   248 AA;  28934 MW;  7417554BA996394A CRC64;
     MNFYRSSIIS QIIKYNRRLA KSIICEDDSQ IITLTAFVNQ CLWCHKRVSV SAILLTTDNK
     ILVCNRRDSF LYSEIIRTRN MFRKKRLFLN YSNYLSKQER SILSSFFSLY PATADNDRID
     AIYPGGIPKR GENVPECLSR EIKEEVNIDN SFVFIDTRFF IHGIIEDTII NKFFEVIFFV
     GRISLTSDQI IDTFKSNHEI KDLIFLDPNS GNGLQYEIAK YALDTAKLKC YGHRGCYYES
     LKKLTEDD