ID   VIE2_NPVHC              Reviewed;         375 AA.
AC   Q2NNU1;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   29-SEP-2021, entry version 59.
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=HynVgp006;
OS   Hyphantria cunea nuclear polyhedrosis virus (HcNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=28288;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16894193; DOI=10.1099/vir.0.81930-0;
RA   Ikeda M., Shikata M., Shirata N., Chaeychomsri S., Kobayashi M.;
RT   "Gene organization and complete sequence of the Hyphantria cunea
RT   nucleopolyhedrovirus genome.";
RL   J. Gen. Virol. 87:2549-2562(2006).
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; AP009046; BAE72295.1; -; Genomic_DNA.
DR   RefSeq; YP_473194.1; NC_007767.1.
DR   SMR; Q2NNU1; -.
DR   GeneID; 3890554; -.
DR   KEGG; vg:3890554; -.
DR   Proteomes; UP000202376; Genome.
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: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   Coiled coil; Early protein; Host nucleus; Host-virus interaction;
KW   Metal-binding; Modulation of host ubiquitin pathway by viral E3 ligase;
KW   Modulation of host ubiquitin pathway by virus; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..375
FT                   /note="E3 ubiquitin-protein ligase IE2"
FT                   /id="PRO_0000396078"
FT   ZN_FING         177..225
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          272..348
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  42905 MW;  EB7FE0A65B6655AA CRC64;
     MSRINNADTP TNRRNLSLAR GRRRLTYSPS TPMPTPRQTR APMPTPRQRR SLTPEHVVGD
     RNAPLRASYT INNSRYNVHG DAEFNPPEDD DDSIIFTDHA AEQARQRAVN LHESLTTTPR
     SPDYSPVHSP SGQVIDSDDY NSDDDERMLE QILLESAEPP QTPQPAPEPQ EDVEVLCHIC
     SCTFTDIKNY NSNFVTSSEC NHAVCFKCYV SIVFNKEAYK CSICNRTTLT CRAYNRAGYV
     ELSTVRTVRD NKLIKQHWMQ LTESNMPHNR DKTIIEELQL ELADLRATTA RAHHEVNMIK
     SDNLLLQQQV DFKNLELQQE LNAKVKLQKQ NDTLSAANTF LQNQLDAQVA ESKIKMDQFV
     RQHEAFLKKF KSSVM