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 27-MAR-2024, entry version 105.
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; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha2; Human herpesvirus 2.
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 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:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0039593; P:peturbation 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 GO; GO:0075342; P:symbiont-mediated disruption of host cell PML body; IDA:UniProtKB.
DR CDD; cd23130; RING-HC_EHV1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 SUPFAM; SSF57850; RING/U-box; 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
//
