POXIN_NPVAC
ID POXIN_NPVAC Reviewed; 240 AA.
AC P08358;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 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 [GENOMIC DNA].
RC STRAIN=L1;
RX PubMed=3023539; DOI=10.1099/0022-1317-67-11-2565;
RA Liu A., Qin J., Rankin C., Hardin S.E., Weaver R.F.;
RT "Nucleotide sequence of a portion of the Autographa californica nuclear
RT polyhedrosis virus genome containing the EcoRI site-rich region (hr5) and
RT an open reading frame just 5' of the p10 gene.";
RL J. Gen. Virol. 67:2565-2570(1986).
RN [2]
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 [3]
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; X04611; CAA28280.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66766.1; -; Genomic_DNA.
DR PIR; A29150; WMNVP6.
DR RefSeq; NP_054166.1; NC_001623.1.
DR PDB; 6XB3; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-240.
DR PDBsum; 6XB3; -.
DR SMR; P08358; -.
DR PRIDE; P08358; -.
DR GeneID; 1403969; -.
DR KEGG; vg:1403969; -.
DR Proteomes; UP000008292; 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 3D-structure; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..240
FT /note="Poxin"
FT /id="PRO_0000132894"
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"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6XB3"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 82..104
FT /evidence="ECO:0007829|PDB:6XB3"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6XB3"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:6XB3"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:6XB3"
SQ SEQUENCE 240 AA; 27282 MW; CBDE4B2C5D38EEBF CRC64;
MELYNIKYAI DPTNKIVIEQ VDNVDAFVHI LEPGQEVFDE TLSQYHQFPG VVSSIIFPQL
VLNTIISVLS EDGSLLTLKL ENTCFNFHVC NKRFVFGNLP AAVVNNETKQ KLRIGAPIFA
GKKLVSVVTA FHRVGENEWL LPVTGIREAS QLSGHMKVLN GVRVEKWRPN MSVYGTVQLP
YDKIKQHALE QENKTPNALE SCVLFYKDSE IRITYNKGDY EIMHLRMPGP LIQPNTIYYS
