ID   IE0_NPVAC               Reviewed;         261 AA.
AC   P41710;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   23-FEB-2022, entry version 74.
DE   RecName: Full=Immediate-early protein IE-0;
DE            Short=Immediate early 0 protein;
DE   AltName: Full=Immediate early transactivator 0;
GN   Name=IE0; ORFNames=ORF141;
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 [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   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FP25 AND C42.
RX   PubMed=17626083; DOI=10.1128/jvi.00588-07;
RA   Fang M., Dai X., Theilmann D.A.;
RT   "Autographa californica multiple nucleopolyhedrovirus EXON0 (ORF141) is
RT   required for efficient egress of nucleocapsids from the nucleus.";
RL   J. Virol. 81:9859-9869(2007).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST BETA-TUBULIN.
RX   PubMed=19155039; DOI=10.1016/j.virol.2008.12.023;
RA   Fang M., Nie Y., Theilmann D.A.;
RT   "AcMNPV EXON0 (AC141) which is required for the efficient egress of budded
RT   virus nucleocapsids interacts with beta-tubulin.";
RL   Virology 385:496-504(2009).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22754648; DOI=10.3390/v4050761;
RA   Luria N., Lu L., Chejanovsky N.;
RT   "Conserved structural motifs at the C-terminus of baculovirus protein IE0
RT   are important for its functions in transactivation and supporting hr5-
RT   mediated DNA replication.";
RL   Viruses 4:761-776(2012).
RN   [5]
RP   FUNCTION.
RX   PubMed=25173193; DOI=10.1016/j.virol.2014.07.044;
RA   Sokal N., Nie Y., Willis L.G., Yamagishi J., Blissard G.W., Rheault M.R.,
RA   Theilmann D.A.;
RT   "Defining the roles of the baculovirus regulatory proteins IE0 and IE1 in
RT   genome replication and early gene transactivation.";
RL   Virology 468:160-171(2014).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH AC66 AND UBIL.
RX   PubMed=29142135; DOI=10.1128/jvi.01713-17;
RA   Biswas S., Willis L.G., Fang M., Nie Y., Theilmann D.A.;
RT   "Autographa californica Nucleopolyhedrovirus AC141 (Exon0), a potential E3
RT   ubiquitin ligase, interacts with viral Ubiquitin and AC66 to facilitate
RT   nucleocapsid egress.";
RL   J. Virol. 92:0-0(2018).
CC   -!- FUNCTION: Putative viral E3 ligase that plays an essential regulatory
CC       role in both viral DNA replication and transcriptional transactivation.
CC       The role in transcription has been shown to include activation of gene
CC       expression from early viral promoters. Promotes also the efficient
CC       egress of nucleocapsids from the host nucleus. May act as an E3 ligase
CC       that promotes ubiquitination of nucleocapsids proteins by vUbi and
CC       subsequent viral egress for the host nucleus.
CC       {ECO:0000269|PubMed:17626083, ECO:0000269|PubMed:22754648,
CC       ECO:0000269|PubMed:25173193, ECO:0000269|PubMed:29142135}.
CC   -!- SUBUNIT: Interacts with proteins C42 and FP25. Interacts with host
CC       beta-tubulin. Interacts with Ac66 and vUb.
CC       {ECO:0000269|PubMed:17626083, ECO:0000269|PubMed:19155039,
CC       ECO:0000269|PubMed:29142135}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:17626083,
CC       ECO:0000269|PubMed:22754648, ECO:0000269|PubMed:25173193}. Host
CC       cytoplasm {ECO:0000269|PubMed:17626083, ECO:0000269|PubMed:25173193}.
CC       Virion {ECO:0000269|PubMed:17626083}.
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DR   EMBL; L22858; AAA66771.1; -; Genomic_DNA.
DR   PIR; G72867; G72867.
DR   RefSeq; NP_054172.1; NC_001623.1.
DR   PRIDE; P41710; -.
DR   GeneID; 1403974; -.
DR   KEGG; vg:1403974; -.
DR   Proteomes; UP000008292; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   InterPro; IPR007954; Baculo_IE-1.
DR   InterPro; IPR001841; Znf_RING.
DR   Pfam; PF05290; Baculo_IE-1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   DNA replication; Early protein; Host cytoplasm; Host nucleus;
KW   Metal-binding; Reference proteome; Transcription; Transcription regulation;
KW   Viral DNA replication; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..261
FT                   /note="Immediate-early protein IE-0"
FT                   /id="PRO_0000056360"
FT   ZN_FING         212..257
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   261 AA;  30109 MW;  7721E0C528EC2CBE CRC64;
     MIRTSSHVLN VQENIMTSNC ASSPYSCEAT SACAEAQQVM IDNFVFFHMY NADIQIDAKL
     QCGVRSAAFA MIDDKHLEMY KHRIENKFFY YYDQCADIAK PDRLPDDDGA CCHHFIFDAQ
     RIIQCIKEIE SAYGVRDRGN VIVFYPYLKQ LRDALKLIKN SFACCFKIIN SMQMYVNELI
     SNCLLFIEKL ETINKTVKVM NLFVDNLVLY ECNVCKEIST DERFLKPKEC CEYAICNACC
     VNMWKTATTH AKCPACRTSY K