ID   RNB_HHV1M               Reviewed;         161 AA.
AC   P56958;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   23-FEB-2022, entry version 53.
DE   RecName: Full=RNA-binding protein;
DE   AltName: Full=Vmw21;
GN   Name=US11;
OS   Human herpesvirus 1 (strain MP) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10307;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Diaz J.-J.;
RL   Submitted (JUN-2000) to UniProtKB.
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   PRIDE; P56958; -.
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; Repeat; RNA-binding; Viral immunoevasion.
FT   CHAIN           1..161
FT                   /note="RNA-binding protein"
FT                   /id="PRO_0000115741"
FT   REPEAT          85..90
FT                   /note="1"
FT   REPEAT          91..96
FT                   /note="2"
FT   REPEAT          97..102
FT                   /note="3"
FT   REPEAT          103..108
FT                   /note="4"
FT   REPEAT          109..114
FT                   /note="5"
FT   REPEAT          115..120
FT                   /note="6"
FT   REPEAT          121..126
FT                   /note="7"
FT   REPEAT          127..132
FT                   /note="8"
FT   REPEAT          133..138
FT                   /note="9"
FT   REPEAT          139..144
FT                   /note="10"
FT   REPEAT          145..150
FT                   /note="11"
FT   REPEAT          151..156
FT                   /note="12"
FT   REGION          1..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..156
FT                   /note="12 X 6 AA approximate tandem repeats"
FT   COMPBIAS        91..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   161 AA;  17745 MW;  1CF68615474462FF CRC64;
     MSQTQPPAPV GPGDPDVYLK GVPSAGMHPR GVHAPRGHPR MISGPPQRGD NDQAAGQCGD
     SGLLRVGADT TISKPSEAVR PPTIPRTPRV PREPRVPRPP REPREPRVPR ASRDPRVPRD
     PRDPRQPRSP REPRSPREPR PPREPRTPRT TREPRTARGA V