ID   TEG5_BHV1P              Reviewed;         742 AA.
AC   P30021;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Tegument protein UL47;
GN   ORFNames=UL47;
OS   Bovine herpesvirus 1.1 (strain P8-2) (BoHV-1) (Infectious bovine
OS   rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10324;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1662698; DOI=10.1099/0022-1317-72-12-3077;
RA   Carpenter D.E., Misra V.;
RT   "The most abundant protein in bovine herpes 1 virions is a homologue of
RT   herpes simplex virus type 1 UL47.";
RL   J. Gen. Virol. 72:3077-3084(1991).
RN   [2]
RP   SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, AND NUCLEAR LOCALIZATION
RP   SIGNAL.
RX   PubMed=17005680; DOI=10.1128/jvi.01322-06;
RA   Verhagen J., Donnelly M., Elliott G.;
RT   "Characterization of a novel transferable CRM-1-independent nuclear export
RT   signal in a herpesvirus tegument protein that shuttles between the nucleus
RT   and cytoplasm.";
RL   J. Virol. 80:10021-10035(2006).
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   -!- INTERACTION:
CC       P30021; A1A4K3: DDB1; Xeno; NbExp=7; IntAct=EBI-11301368, EBI-11296420;
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; D10327; BAA01170.1; -; Genomic_DNA.
DR   EMBL; Z11610; CAA77683.1; -; Genomic_DNA.
DR   PIR; JQ1435; TNBEB1.
DR   IntAct; P30021; 2.
DR   PRIDE; P30021; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044095; C:host cell nucleoplasm; IMP:AgBase.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR005029; Herpes_UL47.
DR   Pfam; PF03362; Herpes_UL47; 1.
PE   1: Evidence at protein level;
KW   Host cytoplasm; Host nucleus; Late protein; Transcription;
KW   Transcription regulation; Virion; Virion tegument.
FT   CHAIN           1..742
FT                   /note="Tegument protein UL47"
FT                   /id="PRO_0000116076"
FT   REGION          1..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           10..30
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           95..122
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           485..495
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..85
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  80744 MW;  85979D8C2C953C89 CRC64;
     MDAARDGRPE RRPRRSGTYR THPFQRPSAR RSLLDALRAA DAEAAERPRV RRPRPDFQRP
     PDEDTSEDEN VYDYIDGDSS DSADDYDSDY FTANRGPNHG AGDAMDTDAP PERAPEGGAP
     QDYLTAHLRA IEALPESAPH RSLLERTART VYAHEFPPRD LSAGSRAPAQ RARRSLRGFP
     RGGGGGQEPG PDDEGDDAAD LREDLVPDEA YAHLERDERL SEGPPLLNME AAAAAAGERS
     VVEELFTYAP AQPQVEVPLP RILEGRVRPS AFFAQMPLDA LCRTPPNDQR VVRERRAWDM
     AGTPHGLLIT TWSTVDPEFS IGGMYVGAPE GTRPRLVWRR AMKQAMALQY RLGVGGLCRA
     VDGARMPPTE ALLFLAARAA ARSAQLPFFV AAGARGRRRA APARGGGWAA GSHAVHATGR
     VPHATLFRGS MGSLIYWHEL RVMLTAVPAL CARYAGAGLQ SAELYLLALR HSEAPGYTAN
     ERYALSAYLT LFVALAERAV RWLYLAGAHL LGPHPTAAAF REVRAKIPYE RLPLGSATLH
     DAEVETVDSA TFQEALAFSA LAHVYGEAYV AVRTATTLLM AEYAAHAERR DVREMTAAFL
     GVGLIAQRLM GSLEPAAELR SRRSGVRGPA CPTVREGTLA RYSLLADAAL PLVRPVSLVE
     FWEARDGVMR ELRLRPVASP PLAGKRRVME LYLSLDSIEA LVGREPLGSR PVLGPLVDIA
     EALADHPHLV TGDGRGPRLG GR