VIE2_NPVCF
ID VIE2_NPVCF Reviewed; 348 AA.
AC Q8QME4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Choristoneura fumiferana nuclear polyhedrosis virus (CfMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=208973;
OH NCBI_TaxID=7141; Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15784887; DOI=10.1099/vir.0.80490-0;
RA de Jong J.G., Lauzon H.A.M., Dominy C., Poloumienko A., Carstens E.B.,
RA Arif B.M., Krell P.J.;
RT "Analysis of the Choristoneura fumiferana nucleopolyhedrovirus genome.";
RL J. Gen. Virol. 86:929-943(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: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; AF512031; AAA67992.1; -; Genomic_DNA.
DR RefSeq; NP_848453.1; NC_004778.3.
DR PRIDE; Q8QME4; -.
DR GeneID; 1482775; -.
DR KEGG; vg:1482775; -.
DR Proteomes; UP000204418; 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; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..348
FT /note="E3 ubiquitin-protein ligase IE2"
FT /id="PRO_0000396079"
FT ZN_FING 179..227
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 272..306
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 39281 MW; DBE21E93C4B26B23 CRC64;
MSRQINANTP VSRRRSGLRG RRLSYSPEDA VPTPAPRFSI LEARRAADRP AEERMRAWHV
IGDTSEPVTL RFVHNNAQYT VHGNAPFNTA DFQEERDSQE TEAANRAHQR AVHLHEHLHE
VQETAAPLPN YSPVHSPDLT VMEDLETPRQ RFETMFHAVD AESEDEAVPL PQVDMAVFCH
ICSCFFTDIK NYNSSFVTTS ECNHAVCFKC YTSIMFDKEL FKCSMCNRAT PTCRVYNHKG
FVELLPTRAV RDKQAIKTHW AQLLDNNMSD SKVPEQNDVQ KLQAELAELR AEMASMRAEM
ASKQLGATMA LENRRGSSSS GASSSSTSTS SSSSSSWLWE CLLNTRNY
