ID   ICP0_BHV1K              Reviewed;         676 AA.
AC   P29836;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   23-FEB-2022, entry version 89.
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 1.2 (strain K22) (BoHV-1) (Infectious bovine
OS   rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31519;
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).
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:0000250|UniProtKB:P29128}.
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   -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
CC   -!- PTM: The strongly acidic region might serve as a transcriptional
CC       activation domain, possibly regulated through phosphorylation by casein
CC       kinase II.
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DR   EMBL; M84464; AAA46061.1; -; Genomic_DNA.
DR   PIR; A38209; EDBE22.
DR   SMR; P29836; -.
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; ISS:UniProtKB.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0039593; P:suppression by virus of host exit from mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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_0000056357"
FT   ZN_FING         13..52
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          101..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..486
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;  67701 MW;  9BB0683C9BFCA65D CRC64;
     MAPPAAAPEL GSCCICLDAI TGAARALPCL HAFCLACIRR WLEGRPTCPL CKAPVQSLIH
     SVASDECFEE IPVGGGPGAD GALEPDAAVI WGEDYDAGPI DLTAADGEAP GAGGEAGAAG
     GSEAGGGAGG AEAAGEARGA GAGRAAGAAG GRAGRGADAA QEFIDRVARG PRLPLLPNTP
     GHGPGAPYLR RVVEWVEGAL VGTFAVTARE LAAMTDYVMA MLAECGFDDD GLADAMEPLI
     GEDDAPAFVR SLLFVAARCV TVGPSHLIPQ QSAPPGGRGV VFLDTSDSDS EGSEDDSWSE
     SEESSSGLST SDLTAIDDTE TEPETDAEVE SRRTRGASGA ARARRPAERQ YVSTRGRQTP
     AVQPAPRSLA RRPCGRAAAV SAPPSSRSRG GRRDPRLPAA PRAAPAAQAR ACSPEPREEG
     RGAGLGVAAG ETAGWGVGSE EGRGERRAKL LGEAGPPRVQ ARRRRRTELD RAPTPAPAPA
     PAPAPISTMI DLTANAPARP ADPAPAAALG PALAGAQIGT PAAAAAVTAA AAAPSVARGS
     APSPAVTAAA TGTAAAISTR APTPSPAGRA PAADPRRAGA PALAGAARAE AGRNGNPGRE
     RRPASAMARG DLDPGPESSA QKRRRTEMEV AAWVRESLLG TPRRSSAALA PQPGGRQGPS
     LAGLLGRCSG GSAWRQ