ID   VIE2_NPVR1              Reviewed;         407 AA.
AC   Q8B9B2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-SEP-2021, entry version 72.
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;
OS   Rachiplusia ou multiple nucleopolyhedrovirus (strain R1) (RoMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=654904;
OH   NCBI_TaxID=7113; Helicoverpa zea (Corn earworm moth) (Heliothis zea).
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
OH   NCBI_TaxID=29057; Ostrinia nubilalis (European corn borer) (Pyralis nubilalis).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12810877; DOI=10.1099/vir.0.19146-0;
RA   Harrison R.L., Bonning B.C.;
RT   "Comparative analysis of the genomes of Rachiplusia ou and Autographa
RT   californica multiple nucleopolyhedroviruses.";
RL   J. Gen. Virol. 84:1827-1842(2003).
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; AY145471; AAN28041.1; -; Genomic_DNA.
DR   SMR; Q8B9B2; -.
DR   Proteomes; UP000007020; 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   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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..407
FT                   /note="E3 ubiquitin-protein ligase IE2"
FT                   /id="PRO_0000396077"
FT   ZN_FING         206..254
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..158
FT                   /evidence="ECO:0000255"
FT   COILED          336..393
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  46665 MW;  33CF1F78B5659D7B CRC64;
     MSRQINAATP SSSRHHRLSL SRRRINFTTP SEAQPSSSSR SQTSSSSRSH RRQERRQEQR
     VSEENVQIIG NVNEPLTRSY HRQGVTYNVH GEVNISNADP LLSQEDDVIL INSENVDRER
     FPDISSQQYQ NNIASETAAQ RALQRALDLE AQLMNEIAPR SPVYSPSYAP NSPNYVIPQS
     PDLFASPQSS EQQQQSEPEE DVEVSCNICF TTFKDTKNVN SSFVTTTHCN HAVCFKCYVK
     IIMANSVYKC FCSATSSNCR VYNKHGYVEF MPIDVTRNQD SIKQHWRELL ENNTVNNQTT
     DLNYVEQLQK ELAELRAKTC QVEHKMTMLN SDYIMLKHKH AVAELDLQKA NYDLQESTKK
     SEELQSTVNN LQEQLNKQVV ESQAKFLEFE RNNSDLVSKL QTVMSRR