POXIN_NPVOP
ID POXIN_NPVOP Reviewed; 230 AA.
AC P11037;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Poxin {ECO:0000255|HAMAP-Rule:MF_04143};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04143};
GN Name=P26; ORFNames=ORF132;
OS Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=262177;
OH NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3686831; DOI=10.1016/0042-6822(87)90155-3;
RA Bicknell J.N., Leisy D.J., Rohrmann G.F., Beaudreau G.S.;
RT "Comparison of the p26 gene region of two baculoviruses.";
RL Virology 161:589-592(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT polyhedrosis virus genome.";
RL Virology 229:381-399(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX PubMed=2661722; DOI=10.1099/0022-1317-70-7-1815;
RA Gombart A.F., Blissard G.W., Rohrmann G.F.;
RT "Characterization of the genetic organization of the HindIII M region of
RT the multicapsid nuclear polyhedrosis virus of Orgyia pseudotsugata reveals
RT major differences among baculoviruses.";
RL J. Gen. Virol. 70:1815-1828(1989).
CC -!- FUNCTION: Nuclease that cleaves host 2',3'-cGAMP. {ECO:0000255|HAMAP-
CC Rule:MF_04143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3'-cGAMP + H2O = Gp(2'-5')Ap(3') + H(+);
CC Xref=Rhea:RHEA:59472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:143093, ChEBI:CHEBI:143098; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04143};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59473;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04143};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_04143}.
CC -!- DOMAIN: The substrate binding site is formed by the N-terminus of a
CC monomer and the C-terminus of the opposite monomer. {ECO:0000255|HAMAP-
CC Rule:MF_04143}.
CC -!- SIMILARITY: Belongs to the poxin family. {ECO:0000255|HAMAP-
CC Rule:MF_04143}.
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DR EMBL; M18367; AAA46727.1; -; Genomic_DNA.
DR EMBL; U75930; AAC59131.1; -; Genomic_DNA.
DR EMBL; D13929; BAA03032.1; -; Genomic_DNA.
DR PIR; A27405; WMNV26.
DR RefSeq; NP_046288.1; NC_001875.2.
DR SMR; P11037; -.
DR GeneID; 912076; -.
DR KEGG; vg:912076; -.
DR Proteomes; UP000009248; Genome.
DR GO; GO:0061507; F:2',3'-cyclic GMP-AMP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04143; Poxins; 1.
DR InterPro; IPR006853; Poxin_vir.
DR Pfam; PF04766; Baculo_p26; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nuclease.
FT CHAIN 1..230
FT /note="Poxin"
FT /id="PRO_0000132895"
FT ACT_SITE 43
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT ACT_SITE 174
FT /note="Shared with catalytic histidine of dimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT ACT_SITE 178
FT /note="Proton acceptor; shared with catalytic histidine of
FT dimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 88
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 219
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
SQ SEQUENCE 230 AA; 25565 MW; 8AA1D95C05CA687F CRC64;
MYIKMEVEFD EDTGALQIGG QEVFVMVFEP GQEVFDKSLD QHHQFPGVAT SVVFPQLSIG
TKVDVFTSSG GFGATDHHCF NYHVCNKRFV FGSVPALEIP ADVREHLRIG APITCADRLV
SLVTAVHAAD GAWLLRVTAA RAGQVSGHAR QQRRGAGRTV RAGRSVYGPV QLPYEQLKAH
AFRKRRPRRD AAESCALFYN DSEVRITFNK GEFELMHWRL PGPLVSHGFK
