IE61_VZVD
ID IE61_VZVD Reviewed; 467 AA.
AC P09309;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=E3 ubiquitin-protein ligase IE61;
DE EC=2.3.2.27;
DE AltName: Full=Immediate-early protein 61;
DE Short=IE61;
DE AltName: Full=RING-type E3 ubiquitin transferase IE61 {ECO:0000305};
GN Name=61;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1366099; DOI=10.1128/jvi.66.12.7303-7308.1992;
RA Moriuchi H., Moriuchi M., Smith H.A., Straus S.E., Cohen J.I.;
RT "Varicella-zoster virus open reading frame 61 protein is functionally
RT homologous to herpes simplex virus type 1 ICP0.";
RL J. Virol. 66:7303-7308(1992).
RN [3]
RP FUNCTION, AUTOUBIQUITINATION, AND MUTAGENESIS OF CYS-19.
RX PubMed=20392849; DOI=10.1128/jvi.00335-10;
RA Walters M.S., Kyratsous C.A., Silverstein S.J.;
RT "The RING finger domain of Varicella-Zoster virus ORF61p has E3 ubiquitin
RT ligase activity that is essential for efficient autoubiquitination and
RT dispersion of Sp100-containing nuclear bodies.";
RL J. Virol. 84:6861-6865(2010).
RN [4]
RP FUNCTION.
RX PubMed=22090112; DOI=10.1128/jvi.06400-11;
RA Sloan E., Henriquez R., Kinchington P.R., Slobedman B., Abendroth A.;
RT "Varicella-zoster virus inhibition of the NF-kappaB pathway during
RT infection of human dendritic cells: role for open reading frame 61 as a
RT modulator of NF-kappaB activity.";
RL J. Virol. 86:1193-1202(2012).
RN [5]
RP FUNCTION.
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 I-kappa-B-alpha/NFKBIA, thereby interfering
CC with its degradation. {ECO:0000269|PubMed:20392849,
CC ECO:0000269|PubMed:22090112, 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;
CC -!- SUBUNIT: Interacts with host BTRC; this interaction seems to inactivate
CC SCF-mediated protein degradation in general.
CC {ECO:0000250|UniProtKB:Q9E1W2}.
CC -!- INDUCTION: Immediate early (EI) protein.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:20392849}.
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DR EMBL; X04370; CAA27944.1; -; Genomic_DNA.
DR PIR; I27215; WZBE61.
DR PRIDE; P09309; -.
DR Proteomes; UP000002602; 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 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 DNA-binding; 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; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="E3 ubiquitin-protein ligase IE61"
FT /id="PRO_0000056359"
FT ZN_FING 19..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 101..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 19
FT /note="C->G: Loss of SP100-containing nuclear bodies
FT dispersion."
FT /evidence="ECO:0000269|PubMed:20392849"
SQ SEQUENCE 467 AA; 50916 MW; 25EFA6977EA6994C CRC64;
MDTILAGGSG TSDASDNTCT ICMSTVSDLG KTMPCLHDFC FVCIRAWTST SVQCPLCRCP
VQSILHKIVS DTSYKEYEVH PSDDDGFSEP SFEDSIDILP GDVIDLLPPS PGPSRESIQQ
PTSRSSREPI QSPNPGPLQS SAREPTAESP SDSQQDSIQP PTRDSSPGVT KTCSTASFLR
KVFFKDQPAV RSATPVVYGS IESAQQPRTG GQDYRDRPVS VGINQDPRTM DRLPFRATDR
GTEGNARFPC YMQPLLGWLD DQLAELYQPE IVEPTKMLIL NYIGIYGRDE AGLKTSLRCL
LHDSTGPFVT NMLFLLDRCT DPTRLTMQTW TWKDTAIQLI TGPIVRPETT STGETSRGDE
RDTRLVNTPQ KVRLFSVLPG IKPGSARGAK RRLFHTGRDV KRCLTIDLTS ESDSACKGSK
TRKVASPQGE SNTPSTSGST SGSLKHLTKK SSAGKAGKGI PNKMKKS
