ID   E3_YLDV                 Reviewed;         185 AA.
AC   Q9DHS8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Protein E3 homolog {ECO:0000305};
DE   AltName: Full=Protein E3L homolog {ECO:0000303|PubMed:15448208};
GN   OrderedLocusNames=34L {ECO:0000303|PubMed:11277691};
OS   Yaba-like disease virus (YLDV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Yatapoxvirus.
OX   NCBI_TaxID=132475;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11277691; DOI=10.1006/viro.2000.0761;
RA   Lee H.-J., Essani K., Smith G.L.;
RT   "The genome sequence of Yaba-like disease virus, a yatapoxvirus.";
RL   Virology 281:170-192(2001).
RN   [2] {ECO:0007744|PDB:1SFU}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-75 IN COMPLEX WITH DNA.
RX   PubMed=15448208; DOI=10.1073/pnas.0405586101;
RA   Ha S.C., Lokanath N.K., Van Quyen D., Wu C.A., Lowenhaupt K., Rich A.,
RA   Kim Y.G., Kim K.K.;
RT   "A poxvirus protein forms a complex with left-handed Z-DNA: crystal
RT   structure of a Yatapoxvirus Zalpha bound to DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14367-14372(2004).
CC   -!- FUNCTION: RNA-binding protein that plays a role in the inhibition of
CC       multiple cellular antiviral responses activated by double-stranded RNA
CC       (dsRNA), such as inhibition of PKR activation, necroptosis, and IFN-
CC       mediated antiviral activities (By similarity). Recognizes and binds Z-
CC       RNA structures via its Z-binding domain and dsRNA via its DRBM domain:
CC       RNA-binding activity is required to escape host ZBP1-dependent
CC       necroptosis (By similarity). Mechanistically, the Z-binding domain
CC       binds Z-RNAs that are produced during Yaba-like disease virus
CC       infection, thereby competing with Z-RNA detection by host ZBP1,
CC       suppressing ZBP1-dependent necroptosis (By similarity).
CC       {ECO:0000250|UniProtKB:P21605}.
CC   -!- DOMAIN: The Z-binding domain recognizes and binds Z-nucleic acid
CC       structures. {ECO:0000269|PubMed:15448208}.
CC   -!- SIMILARITY: Belongs to the poxviridae E3 protein family. {ECO:0000305}.
CC   -!- CAUTION: Binds Z-DNA structures in vitro (PubMed:15448208). However, it
CC       probably binds Z-RNA in vivo (By similarity).
CC       {ECO:0000250|UniProtKB:P21605, ECO:0000269|PubMed:15448208}.
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DR   EMBL; AJ293568; CAC21272.1; -; Genomic_DNA.
DR   RefSeq; NP_073419.1; NC_002642.1.
DR   PDB; 1SFU; X-ray; 2.00 A; A/B=1-75.
DR   PDBsum; 1SFU; -.
DR   SMR; Q9DHS8; -.
DR   GeneID; 918721; -.
DR   KEGG; vg:918721; -.
DR   EvolutionaryTrace; Q9DHS8; -.
DR   Proteomes; UP000136581; Genome.
DR   GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IEA:InterPro.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR009179; E3L.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR042371; Z_dom.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF02295; z-alpha; 1.
DR   PIRSF; PIRSF004008; VAC_E3L; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS50139; Z_BINDING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host IRF7 by virus;
KW   Inhibition of host PKR by virus; Inhibition of host RLR pathway by virus;
KW   Modulation of host cell apoptosis by virus; Reference proteome;
KW   RNA-binding; Viral immunoevasion.
FT   CHAIN           1..185
FT                   /note="Protein E3 homolog"
FT                   /id="PRO_0000454582"
FT   DOMAIN          7..73
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00073"
FT   DOMAIN          112..179
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   HELIX           11..22
FT                   /evidence="ECO:0007829|PDB:1SFU"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:1SFU"
FT   HELIX           43..55
FT                   /evidence="ECO:0007829|PDB:1SFU"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:1SFU"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:1SFU"
SQ   SEQUENCE   185 AA;  21311 MW;  B7C7D386F33071DB CRC64;
     MDLLSCTVND AEIFSLVKKE VLSLNTNDYT TAISLSNRLK INKKKINQQL YKLQKEDTVK
     MVPSNPPKWF KNYNCDNGEK HDSKLEQKNH IPNHIFSDTV PYKKIINWKD KNPCIVLNEY
     CQFTCRDWSI DITTSGKSHC PMFTATVIIS GIKFKPAIGN TKREAKYNAS KITMDEILDS
     VIIKF