RNB_HHV2H
ID RNB_HHV2H Reviewed; 151 AA.
AC P89479;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 23-FEB-2022, entry version 80.
DE RecName: Full=Probable RNA-binding protein;
GN Name=US11;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
CC -!- FUNCTION: Plays a role in the inhibition of host immune response.
CC Participates in the inhibition of host autophagy by interacting with
CC and inhibiting host PKR/EIF2AK2. This interaction also prevents the
CC interferon-induced shut down of protein synthesis following viral
CC infection. Downmodulates the host RLR signaling pathway via direct
CC interaction with host DDX58 and IFIH1. May also participate in nuclear
CC egress of viral particles through interactions with host NCL and
CC regulation of the viral UL34 mRNA. {ECO:0000250|UniProtKB:P04487}.
CC -!- SUBUNIT: Associates with RNA derived from the 60S ribosomal subunits.
CC Seems to form large heterogeneous polymers of up to 200 identical
CC subunits in the cytoplasm. Interacts with host EIF2AK2. Interacts with
CC host NCL. Interacts with host DDX58; this interaction prevents DDX58
CC binding to host MAVS. Interacts with host IFIH1; this interaction
CC prevents host IFH1 binding to MAVS. {ECO:0000250|UniProtKB:P04487}.
CC -!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus
CC {ECO:0000250|UniProtKB:P04487}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P04487}. Note=Following infection, it is
CC released into the cell cytoplasm. {ECO:0000250|UniProtKB:P04487}.
CC -!- DOMAIN: The N-terminal tetrapeptide may be responsible for virion
CC incorporation. {ECO:0000250|UniProtKB:P04487}.
CC -!- DOMAIN: The C-terminal half, rich in Arg and Pro residues, seems to be
CC responsible for the RNA-binding activity, and for the association with
CC ribosomes and the localization to the nucleolus. This region may adopt
CC a poly-L-proline II helix secondary structure.
CC {ECO:0000250|UniProtKB:P04487}.
CC -!- PTM: May be phosphorylated on Ser residues by host kinases.
CC {ECO:0000250|UniProtKB:P04487}.
CC -!- SIMILARITY: Belongs to the simplex virus US11 protein family.
CC {ECO:0000305}.
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DR EMBL; Z86099; CAB06719.1; -; Genomic_DNA.
DR RefSeq; YP_009137224.1; NC_001798.2.
DR PRIDE; P89479; -.
DR DNASU; 1487352; -.
DR GeneID; 1487352; -.
DR KEGG; vg:1487352; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IEA:UniProtKB-KW.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW DNA-binding; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Inhibition of host autophagy by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host MDA5 by virus; Inhibition of host PKR by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Late protein; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Viral immunoevasion.
FT CHAIN 1..151
FT /note="Probable RNA-binding protein"
FT /id="PRO_0000115742"
FT REPEAT 90..95
FT /note="1"
FT REPEAT 96..101
FT /note="2"
FT REPEAT 102..104
FT /note="3"
FT REPEAT 105..110
FT /note="4"
FT REPEAT 111..116
FT /note="5"
FT REPEAT 117..122
FT /note="6"
FT REPEAT 123..128
FT /note="7"
FT REPEAT 129..130
FT /note="8"
FT REPEAT 131..134
FT /note="9"
FT REPEAT 135..140
FT /note="10"
FT REPEAT 141..146
FT /note="11"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..146
FT /note="11 X 6 AA tandem repeats"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 16298 MW; FAB751F23C3DB6AE CRC64;
MASGVSPAHP QTPVGAGSRD LSLKGTPSDG MQPRGADTLE GHSLPTDGPP HRGGDHDPAA
GKRGDSGLLR VCAALSIPKP SEAVRPSRIP RAPRVPREPR VPREPREPRV PRSPREPRVP
RIPRDPRPPR PPRVPREPRP PREPRATRGL A
