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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
 
 
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