ID   IE61_CHV9D              Reviewed;         503 AA.
AC   Q9E1W2;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=E3 ubiquitin-protein ligase IE61;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=Immediate-early protein 61;
DE            Short=IE61;
OS   Cercopithecine herpesvirus 9 (strain DHV) (CeHV-9) (Simian varicella
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=36348;
OH   NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11352673; DOI=10.1006/viro.2001.0912;
RA   Gray W.L., Starnes H.B., White M.W., Mahalingam R.;
RT   "The DNA sequence of the simian varicella virus genome.";
RL   Virology 284:123-130(2001).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH HOST BTRC.
RX   PubMed=26085158; DOI=10.1128/jvi.01149-15;
RA   Whitmer T., Malouli D., Uebelhoer L.S., DeFilippis V.R., Frueh K.,
RA   Verweij M.C.;
RT   "The ORF61 protein encoded by simian varicella virus and varicella-zoster
RT   Virus inhibits NF-kappaB signaling by interfering with IkappaBalpha
RT   degradation.";
RL   J. Virol. 89:8687-8700(2015).
CC   -!- FUNCTION: RING-finger E3 ubiquitin ligase that degrades host SP100, one
CC       of the major components of ND10 nuclear bodies, thereby disrupting the
CC       organization of these bodies. Also plays a role in the inhibition of
CC       host NF-kappa-B pathway by blocking the SCF(BTRC)-mediated addition of
CC       ubiquitin chains to host IkappaBalpha/NFKBIA, thereby interfering with
CC       its degradation. {ECO:0000250|UniProtKB:P09309,
CC       ECO:0000269|PubMed:26085158}.
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; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Interacts with host BTRC; this interaction seems to inactivate
CC       SCF-mediated protein degradation in general.
CC       {ECO:0000269|PubMed:26085158}.
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DR   EMBL; AF275348; AAG27237.1; -; Genomic_DNA.
DR   RefSeq; NP_077475.1; NC_002686.2.
DR   GeneID; 920510; -.
DR   KEGG; vg:920510; -.
DR   Proteomes; UP000159358; Genome.
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 virus of host protein ubiquitination; 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   Host-virus interaction; Metal-binding;
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 pathway; Zinc; Zinc-finger.
FT   CHAIN           1..503
FT                   /note="E3 ubiquitin-protein ligase IE61"
FT                   /id="PRO_0000442577"
FT   ZN_FING         19..58
FT                   /note="RING-type"
FT   REGION          175..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  54132 MW;  8C7FFFA1E46B3532 CRC64;
     MNPPAYTSTS GSVASTGNCA ICMSAISGLG KTLPCLHDFC FVCIQTWTST SAQCPLCRTV
     VSSILHNITS DANYEEYEVI FDDEGYNEDA PLQIPEEPGV NVSPQPPVHS TANSASNTAL
     MRSHAQPRVL APDNSSVFQP STSSHASFSS GFAPYSQTPP VGASNLEATR VSRSAVITPT
     TSTGPRLHLS PSSRSVSQRL QTLFGITKLP GVPTEPPAYA QAEAHFGQAN GYGQHRGALH
     GSYPAVLTAQ DTSQIPTRLP FRATDRDVME VLNSHVICSL CWVGWDEQLA TLFPPPIVEP
     TKTLILNYIA IYGVEDVKLK VSLRCLLHDL TVPFVENMLF LIDRCTDPTR ISMQAWTWHD
     TPIRLLSGPI KSPDGGSTSQ DTSVSNIHRS PPGGSSTQPS SGRRPGRPKG VKRRLFVDDD
     TGVSTNESVF PVINAPIHHK NSKLAALPTG STTDSNERLV VESPGASAEQ PSTSGSSPSP
     SRRRGRKQGI ARIEMLTKKV RRK