D10_RFVKA
ID D10_RFVKA Reviewed; 260 AA.
AC P32097; Q77PB7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=mRNA-decapping protein D10;
DE EC=3.1.3.-;
GN ORFNames=D10R, s085R;
OS Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS Kasza)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX NCBI_TaxID=10272;
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1660196; DOI=10.1016/0042-6822(91)90529-k;
RA Strayer D.S., Jerng H.H., O'Connor K.;
RT "Sequence and analysis of a portion of the genomes of Shope fibroma virus
RT and malignant rabbit fibroma virus that is important for viral replication
RT in lymphocytes.";
RL Virology 185:585-595(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1329373; DOI=10.1016/0168-1702(92)90104-h;
RA Strayer D.S., Jerng H.H.;
RT "Sequence and analysis of the BamHI 'D' fragment of Shope fibroma virus:
RT comparison with similar regions of related poxviruses.";
RL Virus Res. 25:117-132(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA Willer D.O., McFadden G., Evans D.H.;
RT "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL Virology 264:319-343(1999).
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 (By similarity).
CC {ECO:0000250}.
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 -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; M74532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF170722; AAF17969.1; -; Genomic_DNA.
DR RefSeq; NP_051974.1; NC_001266.1.
DR SMR; P32097; -.
DR PRIDE; P32097; -.
DR GeneID; 1486930; -.
DR KEGG; vg:1486930; -.
DR Proteomes; UP000000868; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR003301; Vaccinia_D10_decapping.
DR InterPro; IPR013683; Vaccinia_D10_N.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF08476; VD10_N; 1.
DR PRINTS; PR01364; VD10PROTEIN.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..260
FT /note="mRNA-decapping protein D10"
FT /id="PRO_0000057096"
FT DOMAIN 46..230
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"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 30460 MW; ACF5BFCBFD3BAB54 CRC64;
MNERLQYSHL MNYITKHNRK LSKTYTWNDD SQRVSATGFS NQRLRWSNKT SICLILSTLD
NKFIACSRKH SFLYSEIVRC RSVFRKKRLF LTYTRFLKKK ERPFLSSKLN VPLDDPGTEH
NDIIFPGGLP KNEEDPIMCL SREIKEEINI DSKDIYIDSR FFVHLFIEDL LSNRVYETIL
FLGNTTLTSN EILNNFLANR EIKSLVFLDA LEKGLMCDVL RYVLAISQLK CFGSTGDKTE
LLYDKVTESE KKMAPRYGFD