ICP0_BHV1J
ID ICP0_BHV1J Reviewed; 676 AA.
AC P29128;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 23-FEB-2022, entry version 98.
DE RecName: Full=E3 ubiquitin-protein ligase ICP0;
DE EC=2.3.2.27;
DE AltName: Full=IER 2.9/ER2.6;
DE AltName: Full=P135 protein;
DE AltName: Full=RING-type E3 ubiquitin transferase ICP0 {ECO:0000305};
GN Name=BICP0;
OS Bovine herpesvirus 1.1 (strain Jura) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31518;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1313901; DOI=10.1128/jvi.66.5.2763-2772.1992;
RA Wirth U.V., Fraefel C., Vogt B., Vlcek C., Paces V., Schwyzer M.;
RT "Immediate-early RNA 2.9 and early RNA 2.6 of bovine herpesvirus 1 are 3'
RT coterminal and encode a putative zinc finger transactivator protein.";
RL J. Virol. 66:2763-2772(1992).
RN [2]
RP FUNCTION IN IMMUNE EVASION.
RX PubMed=20106921; DOI=10.1128/jvi.02544-09;
RA Everett R.D., Boutell C., McNair C., Grant L., Orr A.;
RT "Comparison of the biological and biochemical activities of several members
RT of the alphaherpesvirus ICP0 family of proteins.";
RL J. Virol. 84:3476-3487(2010).
CC -!- FUNCTION: Evades nuclear antiviral defenses triggered by dsDNA viruses.
CC Acts during the initial stages of lytic infection and the reactivation
CC of latent viral genome. Prevents the antiviral effect of nuclear bodies
CC by degrading host PML and SP100. {ECO:0000269|PubMed:20106921}.
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 -!- INTERACTION:
CC P29128; Q13547: HDAC1; Xeno; NbExp=2; IntAct=EBI-11292028, EBI-301834;
CC P29128; Q92985: IRF7; Xeno; NbExp=5; IntAct=EBI-11292028, EBI-968267;
CC -!- DOMAIN: The strongly acidic region might serve as a transcriptional
CC activation domain.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
CC -!- PTM: Transactivation activity is possibly regulated through
CC phosphorylation by casein kinase II.
CC -!- SIMILARITY: Belongs to the simplexviruses ICp0 family. {ECO:0000305}.
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DR EMBL; M84465; AAA46062.1; -; Genomic_DNA.
DR EMBL; AJ004801; CAA06138.1; -; Genomic_DNA.
DR PIR; B38209; EDBE23.
DR RefSeq; NP_045363.1; NC_001847.1.
DR SMR; P29128; -.
DR IntAct; P29128; 4.
DR GeneID; 1487364; -.
DR KEGG; vg:1487364; -.
DR GO; GO:0042025; C:host cell nucleus; IMP:AgBase.
DR GO; GO:0075341; C:host cell PML body; IMP:AgBase.
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:0075342; P:disruption by symbiont of host cell PML body; IDA:UniProtKB.
DR GO; GO:0046774; P:suppression by virus of host intracellular interferon activity; IMP:AgBase.
DR GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IMP:AgBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Early protein; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host mitotic exit by virus;
KW Inhibition of host RLR pathway by virus; Metal-binding;
KW Modulation of host cell cycle by virus;
KW Modulation of host ubiquitin pathway by viral E3 ligase;
KW Modulation of host ubiquitin pathway by virus; Phosphoprotein; Repressor;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..676
FT /note="E3 ubiquitin-protein ligase ICP0"
FT /id="PRO_0000056356"
FT ZN_FING 13..52
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 101..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 67879 MW; 11B06BA4E5C4EB71 CRC64;
MAPPAAAPEL GSCCICLDAI TGAARALPCL HAFCLACIRR WLEGRPTCPL CKAPVQSLIH
SVASDECFEE IPVGGGPGAD GALEPDAAVI WGEDYDAGPI DLTAADGEAS GAGGEAGAAD
GSEAGGGAGG AEEAGEARGA GAGRAAGAAG GRAGRGADAA QEFIDRVARG PRLPLLPNTP
EHGPGAPYLR RVVEWVEGAL VGSFAVTARE LAAMTDYVMA MLAECGFDDD GLADAMEPLI
GEDDAPAFVR SLLFVAARCV TVGPSHLIPQ QSAPPGGRGV VFLDTSDSDS EGSEDDSWSE
SEESSSGLST SDLTAIDDTE TEPETDAEVE SRRTRGASGA ARARRPAERQ YVSTRGRQTP
AVQPAPRSLA RRPCGRAAAV SAPPSSRSRG GRRDPRLPAA PRAAPAAQAR ACSPEPREEG
RGAGLGVAAG ETAGWGAGSE EGRGERRARL LGEAGPPRVQ ARRRRRTELD RAPTPAPAPA
PAPAPISTVI DLTANAPARP ADPAPAAAPG PASAGAQIGT PAAAAAVTAA AAAPSVARSS
APSPAVTAAA TSTAAAISTR APTPSPAGRA PAADPRRAGA PALAGAARAE VGRNGNPGRE
RRPASAMARG DLDPGPESSA QKRRRTEMEV AAWVRESLLG TPRRSSAALA PQPGGRQGPS
LAGLLGRCSG GSAWRQ
