ID   VIE2_NPVBM              Reviewed;         422 AA.
AC   O92503;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   23-FEB-2022, entry version 88.
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   Bombyx mori nuclear polyhedrosis virus (BmNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=271108;
OH   NCBI_TaxID=7091; Bombyx mori (Silk moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3;
RX   PubMed=10355780; DOI=10.1099/0022-1317-80-5-1323;
RA   Gomi S., Majima K., Maeda S.;
RT   "Sequence analysis of the genome of Bombyx mori nucleopolyhedrovirus.";
RL   J. Gen. Virol. 80:1323-1337(1999).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=15722524; DOI=10.1099/vir.0.80523-0;
RA   Imai N., Matsumoto S., Kang W.;
RT   "Formation of Bombyx mori nucleopolyhedrovirus IE2 nuclear foci is
RT   regulated by the functional domains for oligomerization and ubiquitin
RT   ligase activity.";
RL   J. Gen. Virol. 86:637-644(2005).
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:0000269|PubMed:15722524}.
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:0000269|PubMed:15722524}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:15722524}.
CC   -!- PTM: Auto-ubiquitinated.
CC   -!- SIMILARITY: Belongs to the alphabaculovirus IE2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; L33180; AAC63817.1; -; Genomic_DNA.
DR   PIR; T41888; T41888.
DR   RefSeq; NP_047548.1; NC_001962.1.
DR   SMR; O92503; -.
DR   MINT; O92503; -.
DR   GeneID; 1488759; -.
DR   KEGG; vg:1488759; -.
DR   Proteomes; UP000204315; 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   1: Evidence at protein level;
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; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..422
FT                   /note="E3 ubiquitin-protein ligase IE2"
FT                   /id="PRO_0000396076"
FT   ZN_FING         220..268
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          314..414
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..215
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  48784 MW;  4325B3BC737223F5 CRC64;
     MSRQINAVTP SSSSRRHRLS LSRRRINFTT SPEALPSSSS RSQPSSSSRS QPYSSSRSQP
     YSSSRRRRRQ ERSQEQRVSE DNVQIIGNAN EPLTRTYHSQ GVTYHVHGQV NISNDDPLLS
     QEDDTIESVD RASQQYQNSI ASETAAQRAL QRGLDLESQL MSEISPRSPA YSPPYPSNDV
     LSQSPDLFDS PQSPQQHELE LEDEDEEEEE EEGEEVEVSC NICFTTLKDT KNVDSSFVTS
     IDCNHAVCFK CYVRIIMDNS TYKCFCSASS SDFRVYNKHG YVEFMPLTLI RNRDSIKQHW
     RELLENNTVN NRIIDLNDVE RLERERSELR AKNSQVEHKM TMLNCDYAML KHEHKITELK
     LKWANRDLEE FTKKTQELQS TVNDLQEQLR KQVAESQAKF SQFERRNSEL VAELYTIEMS
     KP