POXIN_VACCC
ID POXIN_VACCC Reviewed; 219 AA.
AC P20999;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 23-FEB-2022, entry version 56.
DE RecName: Full=Poxin {ECO:0000255|HAMAP-Rule:MF_04143};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04143};
DE AltName: Full=Immune nuclease {ECO:0000250|UniProtKB:Q01225};
GN ORFNames=B2R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
CC -!- FUNCTION: Nuclease that is responsible for viral evasion of host cGAS-
CC STING innate immunity. Cleaves 2',3'-cGAMP which is produced by host
CC cGAS following recognition of cytosolic DNA and blocks the subsequent
CC 2',3'-cGAMP-mediated activation of TMEM173/STING, which normally
CC spreads to adjacent cells and activates the interferon and NF-kappa-B
CC immune responses. {ECO:0000255|HAMAP-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; M35027; AAA48196.1; -; Genomic_DNA.
DR PIR; A42526; A42526.
DR SMR; P20999; -.
DR Proteomes; UP000008269; 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 GO; GO:0039503; P:suppression by virus of host innate immune response; 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; Reference proteome.
FT CHAIN 1..219
FT /note="Poxin"
FT /id="PRO_0000099353"
FT ACT_SITE 17
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT ACT_SITE 138
FT /note="Shared with catalytic histidine of dimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT ACT_SITE 142
FT /note="Proton acceptor; shared with catalytic histidine of
FT dimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 60
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 105
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 169
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 182
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 184
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
FT SITE 186
FT /note="Substrate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04143"
SQ SEQUENCE 219 AA; 24628 MW; EEDE3BB44C8F2A23 CRC64;
MAMFYAHALG GYDENLHAFP GISSTVANDV RKYSVVSVYN NKYDIVKDKY MWCYSQVNKR
YIGALLPMFE CNEYLQIGDP IHDQEGNQIS IITYRHKNYY ALSGIGYESL DLCLEGVGIH
HHVLETGNAV YGKVQHDYST IKEKAKEMST LSPGPIIDYH VWIGDCICQV TAVDVHGKEI
MRMRFKKGAV LPIPNLVKVK LGENDTENLS STISAAPSR