ICP0_EHV1V
ID ICP0_EHV1V Reviewed; 532 AA.
AC P84445; Q6S6U1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=E3 ubiquitin-protein ligase ICP0;
DE EC=2.3.2.27;
DE AltName: Full=Infected cell protein 0;
DE AltName: Full=RING-type E3 ubiquitin transferase ICP0 {ECO:0000305};
GN Name=ICP0;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45947.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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:P28990}.
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; AY464052; AAS45947.1; -; Genomic_DNA.
DR RefSeq; YP_053107.1; NC_001491.2.
DR SMR; P84445; -.
DR GeneID; 2948570; -.
DR KEGG; vg:2948570; -.
DR Proteomes; UP000008296; 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; 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; 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 3: Inferred from homology;
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; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..532
FT /note="E3 ubiquitin-protein ligase ICP0"
FT /id="PRO_0000056355"
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 /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P28990"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P28990"
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
