ICP0_EHV1B
ID ICP0_EHV1B Reviewed; 532 AA.
AC P28990; Q6S6U1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase ICP0;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ICP0 {ECO:0000305};
GN Name=63;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(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).
RN [3]
RP STRUCTURE BY NMR OF 1-63.
RX PubMed=8263911; DOI=10.1006/jmbi.1993.1657;
RA Everett R.D., Barlow P.N., Milner A., Luisi B., Orr A., Hope G., Lyon D.;
RT "A novel arrangement of zinc-binding residues and secondary structure in
RT the C3HC4 motif of an alpha herpes virus protein family.";
RL J. Mol. Biol. 234:1038-1047(1993).
RN [4]
RP STRUCTURE BY NMR OF 1-63.
RX PubMed=8126734; DOI=10.1006/jmbi.1994.1222;
RA Barlow P.N., Luisi B., Milner A., Elliott M., Everett R.D.;
RT "Structure of the C3HC4 domain by 1H-nuclear magnetic resonance
RT spectroscopy. A new structural class of zinc-finger.";
RL J. Mol. Biol. 237:201-211(1994).
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 -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
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DR EMBL; AY665713; AAT67320.1; -; Genomic_DNA.
DR PIR; I36801; WZBEF5.
DR RefSeq; YP_053107.1; NC_001491.2.
DR PDB; 1CHC; NMR; -; A=1-63.
DR PDBsum; 1CHC; -.
DR SMR; P28990; -.
DR GeneID; 2948570; -.
DR KEGG; vg:2948570; -.
DR EvolutionaryTrace; P28990; -.
DR Proteomes; UP000001189; 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 3D-structure; Activator; DNA-binding; Early protein;
KW Host-virus interaction; 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; Ubl conjugation pathway; Viral immunoevasion; Zinc;
KW Zinc-finger.
FT CHAIN 1..532
FT /note="E3 ubiquitin-protein ligase ICP0"
FT /id="PRO_0000056354"
FT ZN_FING 8..47
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 206..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1CHC"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:1CHC"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1CHC"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:1CHC"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1CHC"
SQ SEQUENCE 532 AA; 58630 MW; B4CB7E16FA26FDFA CRC64;
MATVAERCPI CLEDPSNYSM ALPCLHAFCY VCITRWIRQN PTCPLCKVPV ESVVHTIESD
SEFKETKVSV DFDYDSEEDE DSFEGQFLAV DSGDAPANIS AWNGPMAFVP LNANGTAGAP
RLQPLVDWLV ERLDQLFETP ELALVMRNIV MDTLCEHGCN EEELTRQFWP MFHEDTVPFV
TDLIVQAELC VASRPILPIA RGRGVEYIDS SSSSSSSEEE TDSDIEVDPN NLTDPEDTSD
ETSTDNSSAQ APRQEDSRPA RARPGPPTRG RRRGRRPAAP GPASRRSARL RRRQPRTNSR
TNGGDNGEII DLTLDSDGDT EPADVSGSLN TTDQPVLIPD EEEAAPASPH TSSNSAIICL
VSELTPESEE PPRDQPVAPS GSSAGERPMR PRCSLREFAR RFMALAPRDS STSEAAGPSR
LGAGPRATEP FSVAVVLVDR SSEGAGLFGG RFAQHVRRRT EDESARRRGN VLLRPRRQSV
PPVPYPDIAS TSPLIRQGGQ RVRDLQRAFQ TQPAEPEEMR CPHNCQRYRR NQ
