ADPP_NPVAC
ID ADPP_NPVAC Reviewed; 216 AA.
AC P21290; P41445;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 23-FEB-2022, entry version 77.
DE RecName: Full=Protein ADP-ribose pyrophosphatase ORF38;
DE AltName: Full=ORF7;
DE EC=3.6.1.13 {ECO:0000269|PubMed:17174373};
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-216.
RX PubMed=2219715; DOI=10.1016/0042-6822(90)90266-t;
RA Guarino L.A., Smith M.W.;
RT "Nucleotide sequence and characterization of the 39K gene region of
RT Autographa californica nuclear polyhedrosis virus.";
RL Virology 179:1-8(1990).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=17174373; DOI=10.1016/j.virol.2006.11.017;
RA Ge J., Wei Z., Huang Y., Yin J., Zhou Z., Zhong J.;
RT "AcMNPV ORF38 protein has the activity of ADP-ribose pyrophosphatase and is
RT important for virus replication.";
RL Virology 361:204-211(2007).
CC -!- FUNCTION: Plays an important role in virus replication most probably
CC through its hydrolyzing ADP-ribose activity in host cells. May function
CC in viral DNA replication or transcription directly, or by removing
CC toxic substances or metabolic intermediates.
CC {ECO:0000269|PubMed:17174373}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13; Evidence={ECO:0000269|PubMed:17174373};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:17174373}.
CC Host nucleus {ECO:0000269|PubMed:17174373}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46681.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L22858; AAA66668.1; -; Genomic_DNA.
DR EMBL; M37122; AAA46681.1; ALT_FRAME; Genomic_DNA.
DR PIR; A45355; A45355.
DR PIR; F72854; F72854.
DR RefSeq; NP_054067.1; NC_001623.1.
DR GeneID; 1403870; -.
DR KEGG; vg:1403870; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..216
FT /note="Protein ADP-ribose pyrophosphatase ORF38"
FT /id="PRO_0000132975"
FT DOMAIN 1..177
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 48..70
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT CONFLICT 31
FT /note="Missing (in Ref. 2; AAA46681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 25257 MW; A99D6DFC2DD4AD77 CRC64;
MRNAAGLFMI IEPDKAVLLC ARRAYRSANA PAADMNDTFL EKISIPRGHR DCCDAKVYET
AVREFVEETG RFFDSAFIYK LPFTLQWKDD GVTYKYLIYV GVVRGNLINV NAKPNTYTVK
LLPGTFGNDY RIMLKPRRFN CEIARSLAIV PLNKYFNYMN DKQLITYDYS NYIEFFDFVR
SVKARFDNRQ LQDFFYATLK KIDNDAPQKL HALRRV
