ID   POXIN_NPVBM             Reviewed;         240 AA.
AC   O92490;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   23-FEB-2022, entry version 53.
DE   RecName: Full=Poxin {ECO:0000255|HAMAP-Rule:MF_04143, ECO:0000303|PubMed:30728498};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04143, ECO:0000269|PubMed:30728498};
DE   AltName: Full=Protein p26;
DE   AltName: Full=p26;
GN   Name=p26;
OS   Bombyx mori nuclear polyhedrosis virus (BmNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=271108;
OH   NCBI_TaxID=7091; Bombyx mori (Silk moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3 {ECO:0000312|EMBL:AAC63803.1};
RX   PubMed=9185864; DOI=10.1016/s0378-1119(96)00671-3;
RA   Kamita S.G., Maeda S.;
RT   "Sequencing of the putative DNA helicase-encoding gene of the Bombyx mori
RT   nuclear polyhedrosis virus and fine-mapping of a region involved in host
RT   range expansion.";
RL   Gene 190:173-179(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3 {ECO:0000312|EMBL:AAC63803.1};
RX   PubMed=10355780; DOI=10.1099/0022-1317-80-5-1323;
RA   Gomi S., Majima K., Maeda S.;
RT   "Sequence analysis of the genome of Bombyx mori nucleopolyhedrovirus.";
RL   J. Gen. Virol. 80:1323-1337(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H4 {ECO:0000312|EMBL:BBA20619.1};
RA   Bando H.;
RT   "Characterization of a BmNPV isolated in Hokkaido, Japan.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=30728498; DOI=10.1038/s41586-019-0928-6;
RA   Eaglesham J.B., Pan Y., Kupper T.S., Kranzusch P.J.;
RT   "Viral and metazoan poxins are cGAMP-specific nucleases that restrict cGAS-
RT   STING signalling.";
RL   Nature 566:259-263(2019).
CC   -!- FUNCTION: Nuclease that cleaves host 2',3'-cGAMP. {ECO:0000255|HAMAP-
CC       Rule:MF_04143, ECO:0000269|PubMed:30728498}.
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, ECO:0000269|PubMed:30728498};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59473;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04143,
CC         ECO:0000305|PubMed:30728498};
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; L33180; AAC63803.1; -; Genomic_DNA.
DR   EMBL; LC150780; BBA20619.1; -; Genomic_DNA.
DR   PIR; T41874; T41874.
DR   RefSeq; NP_047534.1; NC_001962.1.
DR   SMR; O92490; -.
DR   GeneID; 1488745; -.
DR   KEGG; vg:1488745; -.
DR   Proteomes; UP000204315; 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   1: Evidence at protein level;
KW   Hydrolase; Nuclease.
FT   CHAIN           1..240
FT                   /note="Poxin"
FT                   /id="PRO_0000446972"
FT   ACT_SITE        46
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT   ACT_SITE        181
FT                   /note="Shared with catalytic histidine of dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT   ACT_SITE        185
FT                   /note="Proton acceptor; shared with catalytic histidine of
FT                   dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT   SITE            93
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT   SITE            146
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT   SITE            226
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
SQ   SEQUENCE   240 AA;  27348 MW;  4B4F1F3A0D76DA9F CRC64;
     MELYNIKYAI DPTNKIVIEQ VDNVDAFVHI LEPGQEVFDE TLSRYHQFPG VVSSIIFTQL
     VLNTIISVLS EDGSLLPLKL ENTCFNFHVC NKRFVFGNLP AAIVNNETKQ KLRIGSPIFA
     GEKLVSVVTT FHRVGENEWL LPVTGIQEAS RLSGHIKVPN GVRVEKLRPN MSVYGTVQLP
     YDKIKRHALE QENKTPNALE SCVLFYRDSE IRITYNRGDY EIMHLRMPGP LIQPNTIYYS