DIPP_MIMIV
ID DIPP_MIMIV Reviewed; 360 AA.
AC Q5UQW2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Putative mRNA-decapping protein;
DE EC=3.1.3.-;
DE AltName: Full=Diphosphoinositol polyphosphate phosphohydrolase;
DE Short=DIPP;
DE EC=3.6.1.52;
GN OrderedLocusNames=MIMI_L375;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- FUNCTION: Might function as a decapping enzyme required for the removal
CC of the 5'-end m7GpppN cap tethered to viral and host mRNAs to allow
CC their decay in cells. In addition to the mRNA cap, probably also
CC efficiently hydrolyzes diphosphoinositol polyphosphates (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; AY653733; AAV50644.1; -; Genomic_DNA.
DR RefSeq; YP_003986880.1; NC_014649.1.
DR SMR; Q5UQW2; -.
DR GeneID; 9924996; -.
DR KEGG; vg:9924996; -.
DR Proteomes; UP000001134; Genome.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..360
FT /note="Putative mRNA-decapping protein"
FT /id="PRO_0000250619"
FT DOMAIN 163..347
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ZN_FING 11..28
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT MOTIF 242..264
FT /note="Nudix box"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 43662 MW; A154FBBB46C24815 CRC64;
MEYETNFRKK HICSNCGRSG HEFRNCIEPI TSYGIINVCI SDEYNESMII KDKFCTKKNT
YYRVSSRKHP EISCFISNHI RVRDHENMYK LDNEMIPYRS NEDIHKFCYY KNRILFMMVS
RRFSLGFIEF IRGKYDVSDT KSIINLFQHM YEHEIKFINK NRYKYDNILY HFLNRNNEPK
KIVLNRIYEG KYSNEYCEAK IKFNMLLNSS NEENNNIPVY LEFYIKHIKP KWKSPEWGFP
KGRRDKRSEE NMVCACREFE EETGYKKSDY SVLNKIEPIE EKLTGTNGVN YKHIYYLAIN
NCDINSDLTD YDTYEIGEIK WFTYDEAMAR IRPYHIEKKR ILTRVYLFIL NYLIHNINNT
