D10_VAR67
ID D10_VAR67 Reviewed; 248 AA.
AC P33071;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=mRNA-decapping protein D10;
DE EC=3.1.3.-;
GN ORFNames=D10R;
OS Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=587200;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383392; DOI=10.1016/0168-1702(93)90110-9;
RA Shchelkunov S.N., Blinov V.M., Totmenin A.V., Marennikova S.S.,
RA Kolykhalov A.A., Frolov I.V., Chizhikov V.E., Gytorov V.V., Gashikov P.V.,
RA Belanov E.F., Belavin P.A., Resenchuk S.M., Andzhaparidze O.G.,
RA Sandakhchiev L.S.;
RT "Nucleotide sequence analysis of variola virus HindIII M, L, I genome
RT fragments.";
RL Virus Res. 27:25-35(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT "Genes of variola and vaccinia viruses necessary to overcome the host
RT protective mechanisms.";
RL FEBS Lett. 319:80-83(1993).
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; X67119; CAA47599.1; -; Genomic_DNA.
DR EMBL; X69198; CAA49041.1; -; Genomic_DNA.
DR PIR; S33114; S33114.
DR RefSeq; NP_042144.1; NC_001611.1.
DR PRIDE; P33071; -.
DR GeneID; 1486416; -.
DR KEGG; vg:1486416; -.
DR Proteomes; UP000002060; 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; PF00293; NUDIX; 1.
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_0000057099"
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; 28911 MW; 6461198855973294 CRC64;
MNFYRSSIIS QIIKYNRRLA KSIICEDDSQ IITLTAFVNQ CLWCHKRVSV SAILLTTDNK
ILVCNRRDSF LYSEIIRTRN MSRKKRLFLN YSNYLNKQER SILSSFFSLD PATIDNDRID
AIYPGGILKR GENVPECLSR EIKEEVNIDN SFVFIDTRFF IHGIIEDTII NKFFEVIFFV
GRISLTSDQI IDTFKSNHEI KDLIFLDPNS GNGLQYEIAK YALDTAKLKC YGHRGCYYES
LKKLTEDD