DIPP_ASFP4
ID DIPP_ASFP4 Reviewed; 250 AA.
AC P0C996;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=mRNA-decapping protein g5R {ECO:0000250|UniProtKB:P32092};
DE Short=g5Rp;
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=Pret-114;
OS African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561443;
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 [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 -!- INDUCTION: Expressed early and up to late in the infection cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C996; -.
DR Proteomes; UP000000859; 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..250
FT /note="mRNA-decapping protein g5R"
FT /id="PRO_0000373096"
FT DOMAIN 97..243
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 132..153
FT /note="Nudix box"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P32092"
FT BINDING 138
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"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 29823 MW; 399F922180E94F57 CRC64;
MDTAMQLKTS IGLITCRMNT QNNQIETILV QKRYSLAFSE FIHCHYSINA NQGHLIKMFN
NMTINERLLV KTLDFDRMWY HIWIETPVYE LYHKKYQKFR KNWLLPDNGK KLISLINQAK
GSGTLLWEIP KGKPKEDESD LTCAIREFEE ETGITREYYQ ILPEFKKSMS YFDGKTEYKH
IYFLAMLCKS LEEPNMNLSL QYENRIAEIS KISWQNMEAV RFISKRQSLN LEPIIGPAFN
FIKNYLRYKH
