ID   ICP0_SUHVF              Reviewed;         410 AA.
AC   P29129;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 87.
DE   RecName: Full=E3 ubiquitin-protein ligase ICP0;
DE            EC=2.3.2.27;
DE   AltName: Full=Early protein 0;
DE            Short=EP0;
DE   AltName: Full=RING-type E3 ubiquitin transferase ICP0 {ECO:0000305};
GN   Name=EP0;
OS   Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1)
OS   (Pseudorabies virus (strain Indiana-Funkhauser / Becker)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31523;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1654441; DOI=10.1128/jvi.65.10.5260-5271.1991;
RA   Cheung A.K.;
RT   "Cloning of the latency gene and the early protein 0 gene of pseudorabies
RT   virus.";
RL   J. Virol. 65:5260-5271(1991).
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}.
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}.
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DR   EMBL; M57504; AAA47463.1; -; mRNA.
DR   SMR; P29129; -.
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:0019046; P:release from viral latency; 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; 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   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript 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; Repressor; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation;
KW   Viral immunoevasion; Viral latency; Viral reactivation from latency; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..410
FT                   /note="E3 ubiquitin-protein ligase ICP0"
FT                   /id="PRO_0000056358"
FT   ZN_FING         46..85
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          243..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..313
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  43838 MW;  E35384FE86F82D11 CRC64;
     MGCTVSRRRT TTAEASSAWG IFGFYRPRSP SPPPQRLSLP LTVMDCPICL DVAATEAQTL
     PCMHKFCLDC IQRWTLTSTA CPLCNARVTS ILHHVDSDAS FVETPVEGAT DVDGEEDEPV
     GGGFAVIWGE DYTEEVRHEE AEGQGSGSGS RARPRVPVFN WLYGQVSTVI ESDPIREAVV
     DNIVEIIQEH GMNRQRVTEA MLPMFGANTH ALVDTLFDIS AQWMRRMQRR APMSHQGVNY
     IDTSESEAHS DSEVSSPDEE DSGASSSGVH TEDLTEASES ADDQRPAPRR SPRRARRAAV
     LRREQRRTRC LRRGRTGGQA QGETPEAPSS GEGSSAQHGA SGAGAGPGSA NTAASARSSP
     SSSPSSSMRR PSPSASAPET AAPRGGPPAS SSSGSPRSAT IFIDLTQDDD