DIPP_ASFM2
ID DIPP_ASFM2 Reviewed; 246 AA.
AC Q65217;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Mal-110; ORFNames=g5R;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
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].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [2]
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 -!- 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; X71982; CAA50807.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; Q65217; -.
DR Proteomes; UP000000860; 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; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; RNA-binding.
FT CHAIN 1..246
FT /note="mRNA-decapping protein g5R"
FT /id="PRO_0000250618"
FT DOMAIN 91..239
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 128..149
FT /note="Nudix box"
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"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 246 AA; 29278 MW; F061909CBA452BFB CRC64;
MQLKTSIGLI TCRMNTQSNQ IETILVQKRY SLAFSEFIHC HYSINSNHSH LIKMFNNMTI
NERLLIKTLD FDRMWYHIWI ETPVYELYHK KYQKFKKNWL IPDNGKKLIS LINQAKGSGT
LLWEIPKGKP KENESDLACA IREFEEETGI AREDYQILPE FKKSMSYFEG KTEYKHIYFL
AVLCKSLEEP NMNLSLQYET RIAEISKISW QNMEAVRFIS KRQSLNLEPI IGPAFNFIKN
YLRYKH
