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 08-NOV-2023, entry version 89.
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; Fowlpox virus.
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 SMR; P32817; -.
DR GeneID; 1486601; -.
DR KEGG; vg:1486601; -.
DR Proteomes; UP000008597; Segment.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
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; Nudix; 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
//
