ID   TEG5_HHV2H              Reviewed;         696 AA.
AC   P89467;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Tegument protein UL47;
DE   AltName: Full=82/81 kDa tegument protein;
DE   AltName: Full=VMW82/81;
DE   AltName: Full=VP13/14;
GN   ORFNames=UL47;
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: Tegument protein that can bind to various RNA transcripts.
CC       Plays a role in the attenuation of selective viral and cellular mRNA
CC       degradation by modulating the activity of host shutoff RNase UL41/VHS.
CC       Also plays a role in the primary envelopement of virions in the
CC       perinuclear space, probably by interacting with two nuclear egress
CC       proteins UL31 and UL34. {ECO:0000250|UniProtKB:P10231}.
CC   -!- SUBUNIT: Interacts with US3 kinase. Interacts with UL31 and UL34; these
CC       interactions seem important for efficient virion nuclear egress.
CC       Interacts with UL41/VHS. {ECO:0000250|UniProtKB:P10231}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P10231}.
CC       Host nucleus {ECO:0000250|UniProtKB:P10231}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P10231}. Note=Major tegument protein of the
CC       virion. Undergoes nucleocytoplasmic shuttling during infection.
CC       Localizes to the major sites of transcription in the infected cell
CC       nucleus. {ECO:0000250|UniProtKB:P10231}.
CC   -!- DOMAIN: The nuclear export signal is CRM1-dependent.
CC       {ECO:0000250|UniProtKB:P10231}.
CC   -!- PTM: Phosphorylated by US3. This phosphorylation is required for proper
CC       nuclear localization. {ECO:0000250|UniProtKB:P10231}.
CC   -!- MISCELLANEOUS: Expressed in late in the infection. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae HHV-1 UL47 family.
CC       {ECO:0000305}.
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DR   EMBL; Z86099; CAB06733.1; -; Genomic_DNA.
DR   PIR; PS0359; PS0359.
DR   PRIDE; P89467; -.
DR   Proteomes; UP000001874; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR005029; Herpes_UL47.
DR   Pfam; PF03362; Herpes_UL47; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host nucleus; Late protein; Reference proteome;
KW   RNA-binding; Transcription; Transcription regulation; Virion;
KW   Virion tegument.
FT   CHAIN           1..696
FT                   /note="Tegument protein UL47"
FT                   /id="PRO_0000385493"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..84
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           70..84
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           650..673
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  73600 MW;  AB7FB21D563AA4A2 CRC64;
     MSVRGHAVRR RRASTRSHAP SAHRADSPVE DEPEGGGVGL MGYLRAVFNV DDDSEVEAAG
     EMASEEPPPR RRREARGHPG SRRASEARAA APPRRASFPR PRSVTARSQS VRGRRDSAIT
     RAPRGGYLGP MDPRDVLGRV GGSRVVPSPL FLDELNYEED DYPAAVAHDD GPGARPSATV
     EILAGRVSGP ELQAAFPLDR LTPRVAAWDE SVRSALALGH PAGFYPCPDS AFGLSRVGVM
     HFASPADPKV FFRQTLQQGE ALAWYVTGDA ILDLTDRRAK TSPSRAMGFL VDAIVRVAIN
     GWVCGTRLHT EGRGSELDDR AAELRRQFAS LTALRPVGAA AVPLLSAGGA APPHPGPDAA
     VFRSSLGSLL YWPGVRALLG RDCRVAARYA GRMTYIATGA LLARFNPGAV KCVLPREAAF
     AGRVLDVLAV LAEQTVQWLS VVVGARLHPH SAHPAFADVE QEALFRALPL GSPGVVAAEH
     EALGDTAARR LLATSGLNAV LGAAVYALHT ALATVTLKYA LACGDARRRR DDAAAARAVL
     ATGLILQRLL GLADTVVACV ALAAFDGGST APEVGTYTPL RYACVLRATQ PLYARTTPAK
     FWADVRAAAE HVDLRPASSA PRAPVSGTAD PAFLLEDLAA FPPAPLNSES VLGPRVRVVD
     IMAQFRKLLM GDEETAALRA HVSGRRATGL GGPPRP