DIPP_ASFB7
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 03-AUG-2022, entry version 98.
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.
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=1.70 mM for Gp4G {ECO:0000269|PubMed:11773415};
CC KM=3.90 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 PDBsum; 7DNT; -.
DR PDBsum; 7DNU; -.
DR SMR; P32092; -.
DR GeneID; 22220331; -.
DR KEGG; vg:22220331; -.
DR Proteomes; UP000000624; 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 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 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..103
FT /evidence="ECO:0007829|PDB:7DNU"
FT TURN 104..109
FT /evidence="ECO:0007829|PDB:7DNU"
FT HELIX 110..118
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
