ID   DIPP_ASFK5              Reviewed;         246 AA.
AC   P0C998;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=mRNA-decapping protein g5R;
DE            Short=g5Rp {ECO:0000250|UniProtKB:P32092};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:P32092};
DE   AltName: Full=ASFV-DP {ECO:0000250|UniProtKB:P32092};
DE   AltName: Full=Diphosphoinositol polyphosphate phosphohydrolase;
DE            Short=DIPP;
DE            EC=3.6.1.52 {ECO:0000250|UniProtKB:P32092};
GN   OrderedLocusNames=Ken-114;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561445;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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. In addition to
CC       the mRNA cap, g5R also efficiently hydrolyzes diphosphoinositol
CC       polyphosphates. Down-regulation of the level of PP-InsP5
CC       (diphosphoinositol pentakisphosphate) may play a role in viral
CC       manipulation of the cellular secretory pathway, a step necessary for
CC       the formation of virions. Binds viral and cellular poly(A) mRNAs,
CC       thereby decreasing both types of mRNAs. {ECO:0000250|UniProtKB:P32092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC         polyphosphate + phosphate.; EC=3.6.1.52;
CC         Evidence={ECO:0000250|UniProtKB:P32092};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P32092};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P32092};
CC   -!- SUBUNIT: Interacts with host RPL23A. {ECO:0000250|UniProtKB:P32092}.
CC   -!- SUBCELLULAR LOCATION: Host rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P32092}. Note=Accumulates at the periphery of
CC       the viral factories. {ECO:0000250|UniProtKB:P32092}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C998; -.
DR   Proteomes; UP000000861; Genome.
DR   GO; GO:0044168; C:host cell rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052842; F:inositol diphosphate pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Early protein; Eukaryotic host gene expression shutoff by virus;
KW   Host endoplasmic reticulum; Host gene expression shutoff by virus;
KW   Host-virus interaction; Hydrolase; Late protein; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; RNA-binding.
FT   CHAIN           1..246
FT                   /note="mRNA-decapping protein g5R"
FT                   /id="PRO_0000373098"
FT   DOMAIN          91..239
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           128..149
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   ACT_SITE        143
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P32092"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P32092"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P32092"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P32092"
SQ   SEQUENCE   246 AA;  29201 MW;  0F806E98FE452C91 CRC64;
     MQLKTSIGLI TCRMNTQSNQ IETILVQKRY SLAFSEFIHC HYSINSNHSH LIKMFNNMTI
     NERLLIKTLD FDRMWYHIWI ETPVYELYHK KYQKFKKNWL IPDNGKKLIS LINQAKGSGT
     LLWEIPKGKP KENESDLACA IREFEEETGI AREDYQILPA FKKSMSYFEG KTEYKHIYFL
     AVLCKSLEEP NMNLSLQYET RIAEISKISW QNMEAVRFIS KHQSLNLEPI IGPAFNFIKN
     YLRYKH