ID   DIPP_ASFB7              Reviewed;         250 AA.
AC   P32092;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=mRNA-decapping protein g5R {ECO:0000303|PubMed:23041356};
DE            Short=g5Rp;
DE            EC=3.1.3.- {ECO:0000269|PubMed:19695654};
DE   AltName: Full=ASFV-DP {ECO:0000303|PubMed:29021398};
DE   AltName: Full=Diphosphoinositol polyphosphate phosphohydrolase;
DE            Short=DIPP;
DE            EC=3.6.1.52 {ECO:0000269|PubMed:11773415};
GN   OrderedLocusNames=Ba71V-102; ORFNames=D250R;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus; Asfivirus haemorrhagiae;
OC   African swine fever virus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8382399; DOI=10.1006/viro.1993.1128;
RA   Pena L., Yanez R.J., Revilla Y., Vinuela E., Salas M.L.;
RT   "African swine fever virus guanylyltransferase.";
RL   Virology 193:319-328(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [3]
RP   CHARACTERIZATION, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION,
RP   COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11773415; DOI=10.1128/jvi.76.3.1415-1421.2002;
RA   Cartwright J.L., Safrany S.T., Dixon L.K., Darzynkiewicz E., Stepinski J.,
RA   Burke R., McLennan A.G.;
RT   "The g5R (D250) gene of African swine fever virus encodes a Nudix hydrolase
RT   that preferentially degrades diphosphoinositol polyphosphates.";
RL   J. Virol. 76:1415-1421(2002).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF GLU-147 AND 150-GLU-GLU-151, RNA-BINDING,
RP   CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX   PubMed=19695654; DOI=10.1016/j.virol.2009.07.026;
RA   Parrish S., Hurchalla M., Liu S.-W., Moss B.;
RT   "The African swine fever virus g5R protein possesses mRNA decapping
RT   activity.";
RL   Virology 393:177-182(2009).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, INDUCTION, AND INTERACTION
RP   WITH HOST RPL23A.
RX   PubMed=29021398; DOI=10.1128/jvi.00990-17;
RA   Quintas A., Perez-Nunez D., Sanchez E.G., Nogal M.L., Hentze M.W.,
RA   Castello A., Revilla Y.;
RT   "Characterization of the African Swine Fever Virus Decapping Enzyme during
RT   Infection.";
RL   J. Virol. 91:0-0(2017).
RN   [6]
RP   REVIEW.
RX   PubMed=23041356; DOI=10.1016/j.virusres.2012.09.014;
RA   Rodriguez J.M., Salas M.L.;
RT   "African swine fever virus transcription.";
RL   Virus Res. 173:15-28(2013).
RN   [7]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
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 (PubMed:19695654). May therefore accelerate viral and cellular
CC       mRNA turnover to eliminate competing host mRNAs and allow stage-
CC       specific synthesis of viral proteins. Acceleration of the turnover of
CC       cellular transcripts may even promote the shutoff of host protein
CC       synthesis (PubMed:29021398). In addition to the mRNA cap, g5R also
CC       efficiently hydrolyzes diphosphoinositol polyphosphates. Down-
CC       regulation of the level of PP-InsP5 (diphosphoinositol
CC       pentakisphosphate) may play a role in viral manipulation of the
CC       cellular secretory pathway, a step necessary for the formation of
CC       virions (PubMed:11773415). Binds viral and cellular poly(A) mRNAs,
CC       thereby decreasing both types of mRNAs (PubMed:19695654,
CC       PubMed:29021398). {ECO:0000269|PubMed:11773415,
CC       ECO:0000269|PubMed:19695654, ECO:0000269|PubMed:29021398}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC         polyphosphate + phosphate.; EC=3.6.1.52;
CC         Evidence={ECO:0000269|PubMed:11773415};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11773415};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:11773415};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.2 uM for diphosphoinositol pentakisphosphate
CC         {ECO:0000269|PubMed:11773415};
CC         KM=0.67 mM for GTP {ECO:0000269|PubMed:11773415};
CC         KM=0.58 mM for p5A {ECO:0000269|PubMed:11773415};
CC         KM=0.92 mM for ATP {ECO:0000269|PubMed:11773415};
CC         KM=1.36 mM for p4A {ECO:0000269|PubMed:11773415};
CC         KM=1.7 mM for Gp4G {ECO:0000269|PubMed:11773415};
CC         KM=3.9 mM for Ap4A {ECO:0000269|PubMed:11773415};
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:11773415};
CC   -!- SUBUNIT: Interacts with host RPL23A. {ECO:0000269|PubMed:29021398}.
CC   -!- SUBCELLULAR LOCATION: Host rough endoplasmic reticulum
CC       {ECO:0000269|PubMed:11773415, ECO:0000269|PubMed:29021398}.
CC       Note=Accumulates at the periphery of the viral factories.
CC       {ECO:0000269|PubMed:29021398}.
CC   -!- INDUCTION: Expressed early and up to late in the infection cycle.
CC       {ECO:0000269|PubMed:29021398, ECO:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L07263; AAA42693.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65331.1; -; Genomic_DNA.
DR   PIR; B45391; B45391.
DR   RefSeq; NP_042795.1; NC_001659.2.
DR   PDB; 7DNT; X-ray; 2.50 A; A=1-250.
DR   PDB; 7DNU; X-ray; 2.25 A; A=1-250.
DR   PDB; 8WQQ; X-ray; 2.30 A; A/B=6-248.
DR   AlphaFoldDB; P32092; -.
DR   SMR; P32092; -.
DR   GeneID; 22220331; -.
DR   KEGG; vg:22220331; -.
DR   Proteomes; UP000000624; Segment.
DR   GO; GO:0044168; C:host cell rough endoplasmic reticulum; EXP:UniProtKB.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; EXP:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:symbiont-mediated suppression of host gene expression; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR051325; Nudix_hydrolase_domain.
DR   PANTHER; PTHR21340:SF0; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [ASYMMETRICAL]; 1.
DR   PANTHER; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
DR   PDBsum; 7DNT; -.
DR   PDBsum; 7DNU; -.
DR   PDBsum; 8WQQ; -.
PE   1: Evidence at protein level;
KW   3D-structure; Early protein;
KW   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; Reference proteome; RNA-binding.
FT   CHAIN           1..250
FT                   /note="mRNA-decapping protein g5R"
FT                   /id="PRO_0000057089"
FT   DOMAIN          97..239
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           132..153
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   ACT_SITE        147
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:19695654"
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:0000305"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         147
FT                   /note="E->Q: Complete loss of mRNA-decapping activity."
FT                   /evidence="ECO:0000269|PubMed:19695654"
FT   MUTAGEN         150..151
FT                   /note="EE->QQ: Complete loss of mRNA-decapping activity."
FT                   /evidence="ECO:0000269|PubMed:19695654"
FT   STRAND          6..19
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   TURN            20..23
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          24..34
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           36..42
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:7DNT"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           64..71
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           75..83
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           100..104
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   TURN            105..109
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           110..118
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          174..187
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           194..197
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           203..206
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          207..216
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           217..224
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:7DNU"
FT   HELIX           232..246
FT                   /evidence="ECO:0007829|PDB:7DNU"
SQ   SEQUENCE   250 AA;  29875 MW;  3EF2522180E42237 CRC64;
     MDTAMQLKTS IGLITCRMNT QNNQIETILV QKRYSLAFSE FIHCHYSINA NQGHLIKMFN
     NMTINERLLV KTLDFDRMWY HIWIETPVYE LYHKKYQKFR KNWLLPDNGK KLISLINQAK
     GSGTLLWEIP KGKPKEDESD LTCAIREFEE ETGITREYYQ ILPEFKKSMS YFDGKTEYKH
     IYFLAMLCKS LEEPNMNLSL QYENRIAEIS KISWQNMEAV RFISKRQSFN LEPMIGPAFN
     FIKNYLRYKH
//