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ICP0_HHV2H
ID   ICP0_HHV2H              Reviewed;         825 AA.
AC   P28284;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 99.
DE   RecName: Full=E3 ubiquitin-protein ligase ICP0;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferaseICP0 {ECO:0000305};
DE   AltName: Full=VMW118 protein;
GN   Name=RL2;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dolan A.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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. Prevents antiviral response to viral
CC       DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3
CC       nuclear signaling to prevent interferon production by the infected
CC       cells. {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   -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
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DR   EMBL; D10471; BAA23427.1; -; Genomic_DNA.
DR   EMBL; Z86099; CAB06760.1; -; Genomic_DNA.
DR   PIR; JQ1501; EDBEXD.
DR   PRIDE; P28284; -.
DR   Proteomes; UP000001874; Genome.
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: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; 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   1: Evidence at protein level;
KW   Activator; DNA-binding; 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; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Transferase;
KW   Ubl conjugation; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..825
FT                   /note="E3 ubiquitin-protein ligase ICP0"
FT                   /id="PRO_0000056353"
FT   ZN_FING         126..167
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..378
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  81986 MW;  5CEB15858553A274 CRC64;
     MEPRPGTSSR ADPGPERPPR QTPGTQPAAP HAWGMLNDMQ WLASSDSEEE TEVGISDDDL
     HRDSTSEAGS TDTEMFEAGL MDAATPPARP PAERQGSPTP ADAQGSCGGG PVGEEEAEAG
     GGGDVCAVCT DEIAPPLRCQ SFPCLHPFCI PCMKTWIPLR NTCPLCNTPV AYLIVGVTAS
     GSFSTIPIVN DPRTRVEAEA AVRAGTAVDF IWTGNPRTAP RSLSLGGHTV RALSPTPPWP
     GTDDEDDDLA DVDYVPPAPR RAPRRGGGGA GATRGTSQPA ATRPAPPGAP RSSSSGGAPL
     RAGVGSGSGG GPAVAAVVPR VASLPPAAGG GRAQARRVGE DAAAAEGRTP PARQPRAAQE
     PPIVISDSPP PSPRRPAGPG PLSFVSSSSA QVSSGPGGGG LPQSSGRAAR PRAAVAPRVR
     SPPRAAAAPV VSASADAAGP APPAVPVDAH RAPRSRMTQA QTDTQAQSLG RAGATDARGS
     GGPGAEGGPG VPRGTNTPGA APHAAEGAAA RPRKRRGSDS GPAASSSASS SAAPRSPLAP
     QGVGAKRAAP RRAPDSDSGD RGHGPLAPAS AGAAPPSASP SSQAAVAAAS SSSASSSSAS
     SSSASSSSAS SSSASSSSAS SSSASSSAGG AGGSVASASG AGERRETSLG PRAAAPRGPR
     KCARKTRHAE GGPEPGARDP APGLTRYLPI AGVSSVVALA PYVNKTVTGD CLPVLDMETG
     HIGAYVVLVD QTGNVADLLR AAAPAWSRRT LLPEHARNCV RPPDYPTPPA SEWNSLWMTP
     VGNMLFDQGT LVGALDFHGL RSRHPWSREQ GAPAPAGDAP AGHGE
 
 
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