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 24-JAN-2024, entry version 101.
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; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC Varicellovirus cercopithecinealpha9.
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; Segment.
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 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 PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF1; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
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 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
//
