ID   VIE2_NPVOP              Reviewed;         405 AA.
AC   P32511;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=E3 ubiquitin-protein ligase IE2;
DE            EC=2.3.2.27;
DE   AltName: Full=Immediate-early protein IE2;
DE   AltName: Full=RING-type E3 ubiquitin transferase IE2;
GN   Name=IE2; ORFNames=ORF151;
OS   Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=262177;
OH   NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1736546; DOI=10.1016/0042-6822(92)90297-3;
RA   Theilmann D.A., Stewart S.;
RT   "Molecular analysis of the trans-activating IE-2 gene of Orgyia
RT   pseudotsugata multicapsid nuclear polyhedrosis virus.";
RL   Virology 187:84-96(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA   Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT   "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT   polyhedrosis virus genome.";
RL   Virology 229:381-399(1997).
CC   -!- FUNCTION: RING-finger E3 ubiquitin ligase that plays an important
CC       regulatory role during the initial stages of infection. Migrates to
CC       specific nuclear foci early in infection supposely to prepare the sites
CC       for viral replication by targeting and ubiquitinating host proteins.
CC       {ECO:0000250|UniProtKB:O92503}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:O92503}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:O92503}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O92503}.
CC   -!- SIMILARITY: Belongs to the alphabaculovirus IE2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; M83827; AAA46749.1; -; Genomic_DNA.
DR   EMBL; U75930; AAC59150.1; -; Genomic_DNA.
DR   PIR; A42190; WMNVP1.
DR   RefSeq; NP_046307.1; NC_001875.2.
DR   SMR; P32511; -.
DR   PRIDE; P32511; -.
DR   GeneID; 912011; -.
DR   KEGG; vg:912011; -.
DR   Proteomes; UP000009248; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Early protein; Host nucleus;
KW   Host-virus interaction; Metal-binding;
KW   Modulation of host ubiquitin pathway by viral E3 ligase;
KW   Modulation of host ubiquitin pathway by virus; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..405
FT                   /note="E3 ubiquitin-protein ligase IE2"
FT                   /id="PRO_0000056351"
FT   ZN_FING         207..255
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  45669 MW;  4272E7B2875F85CD CRC64;
     MSRSNNANAP TPSNRRRNLS LVRGRRLTYS PPDAASAQRA SPPRSAPRAA PRRVHAVGDP
     GAPLRASYAL PNGVYNLHGD AHFNPPEEDD DILFVDTAAE QARQRAVNLH EAVNRHERLR
     RELGERMTRS PTLLNYSPSY SPTSPRSRSP DLIMPEDLQP AREQPLAPFN DSDDDERLLE
     QVMLESAEAP QLPQAPPAPQ VDVSVLCHIC SCTFTDIQNY NSNFVTSTEC NHAVCFKCYV
     SIVFGKESYK CSICNRTTIS CRAYNRDGYV ELSTMSTVRD SQAIKRHWAQ LSDSNMPHSN
     EMTTIQELQA ELAELRAATA RAHHDVNMAR SDSQLLRQQL DVKEAELAHE SNARLKLQKQ
     NETLSANNLS LQHQLNTQVI ESRVKMEQFK RQHDEFMEKF KLSLS