ID   D9_FOWPN                Reviewed;         231 AA.
AC   P21970; Q9J5F3;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative Nudix hydrolase FPV054;
DE            EC=3.6.-.-;
GN   OrderedLocusNames=FPV054; ORFNames=FP-D9, FPD9;
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 [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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
RC   STRAIN=FP-1;
RX   PubMed=2165135; DOI=10.1099/0022-1317-71-7-1517;
RA   Tartaglia J., Winslow J., Goebel S.J., Johnson G.P., Taylor J.,
RA   Paoletti E.;
RT   "Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox
RT   virus: relatedness to the central portion of the vaccinia virus HindIII D
RT   region.";
RL   J. Gen. Virol. 71:1517-1524(1990).
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. Does not cleave
CC       unmethylated RNAs or RNAs shorter than 24 nucleotides (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 early phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; AF198100; AAF44398.1; -; Genomic_DNA.
DR   EMBL; X17202; CAA35072.1; -; Genomic_DNA.
DR   RefSeq; NP_039017.1; NC_002188.1.
DR   GeneID; 1486602; -.
DR   KEGG; vg:1486602; -.
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   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR003300; Viral_VD9.
DR   PRINTS; PR01363; VD09PROTEIN.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   2: Evidence at transcript level;
KW   DNA replication; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..231
FT                   /note="Putative Nudix hydrolase FPV054"
FT                   /id="PRO_0000057090"
FT   DOMAIN          74..217
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           125..146
FT                   /note="Nudix box"
FT   ACT_SITE        140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   231 AA;  27267 MW;  B2337D8128761DFD CRC64;
     MFDISREQQN MLEKNKDCVI TFETNRERIT IENTNIKDIL SDRRIHIFAL CITSDNIPII
     GIRRTSFMYQ SVISKRRSFS EILAVDINHL KYMYNNEIKE ICIRSIVPFT YSGFNNFEEL
     VLLGGRVKNK ESIYQCLSRE LSEESDGILT IKTFGNKILK LTIEDKILRR TFYGYCIVCF
     IDQLYSEIIK PLYNIEIKEL GSLFDRSSNE KYEYLHFIYN TLLTYKYGGV L