ID   D10_FOWPN               Reviewed;         225 AA.
AC   P32817;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=mRNA-decapping protein D10;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=FPV053; ORFNames=D10, FP-D10, FPD10;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2177083; DOI=10.1099/0022-1317-71-12-2873;
RA   Binns M.M., Britton B.S., Mason C., Boursnell M.E.G.;
RT   "Analysis of the fowlpox virus genome region corresponding to the vaccinia
RT   virus D6 to A1 region: location of, and variation in, non-essential genes
RT   in poxviruses.";
RL   J. Gen. Virol. 71:2873-2881(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-440;
RA   Skinner M.A.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; AJ005163; CAA06400.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44397.1; -; Genomic_DNA.
DR   PIR; S42250; S42250.
DR   RefSeq; NP_039016.1; NC_002188.1.
DR   GeneID; 1486601; -.
DR   KEGG; vg:1486601; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Pfam; PF00293; NUDIX; 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..225
FT                   /note="mRNA-decapping protein D10"
FT                   /id="PRO_0000057095"
FT   DOMAIN          35..218
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           116..137
FT                   /note="Nudix box"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  26445 MW;  C9668C82951A64D7 CRC64;
     MGEYYKNKLL LRPSVYSDNI QKIKLVAYEY GKLHAKYPLS VIGIMKTIDD KFVLCHRYNS
     FLFSEIAFTK DKRRKIRLFK KYSKYMSNIE RDILSYKLSL PNNYNTNHID IIFPGGKIKD
     LESITNCLVR EIKEELNIDS SYLAICKNCF VYGSIYDRLI DKDFEVIALY VETDLTSRQI
     LNRFIPNREI KGISFIDARD INKDYLYTNV IKYIINAVRT SASNS