ID   TEG5_EHV1B              Reviewed;         871 AA.
AC   P28929; Q6DLJ8;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Tegument protein UL47 homolog;
DE   AltName: Full=GP10;
GN   OrderedLocusNames=13;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
RN   [2]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=RacH;
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   -!- 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; AY665713; AAT67270.1; -; Genomic_DNA.
DR   PIR; E36796; TNBEA1.
DR   RefSeq; YP_053058.1; NC_001491.2.
DR   GeneID; 1487516; -.
DR   KEGG; vg:1487516; -.
DR   Proteomes; UP000001189; 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: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   Transcription; Transcription regulation; Virion; Virion tegument.
FT   CHAIN           1..871
FT                   /note="Tegument protein UL47 homolog"
FT                   /id="PRO_0000116077"
FT   REGION          1..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           13..33
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..128
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..209
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  96971 MW;  1691F0344FD59737 CRC64;
     MDQHHGARGG APIRRPRRSI ESRSHPFRAT GNTQRTYSTP RLSYRDGLSG RTASRDPQEQ
     ASNQDESSNP STSNAQQSTS FWGYLRRVFS DDVPAQPQAP RPRADFAPPA GEESSSEEEE
     EEGPAQAPLD EEDQLMYADQ YSVGDSSDEN DEEEDPRLGS DYPTSAESSE YHDHGEMVAG
     AGAESESETD IDAEEEEEDD EDDEDDMEVI RDESYRLPRT WLDKSIRLMD EALAQSSELS
     KAITKSTRSL YDSQFAPGGR GYTQTATPSR RLVQLSRAGM YDSDKIVMTG DYMEVDDDPD
     SAYQSWVRAI RHPLAMNPSW EETISNHTNP SFSTDIDYDI DELIEKNLAR TPPVFEGLLD
     SAEFFYKLPM LYTYATITQD EAYEERLAWS NTQALHGHEQ SSWQALLVYY SRGGMYVSPT
     QEPRGIWRRA LKQAMALQLK MCVLGLSDVV TKQNATHHHA AVTFLVDALL RTARNCYLAS
     RLLVFAWERR RETGAKRPAE PLIALSGVTL LQPLPPEVSE LLEQRTFDIG LRTPNSAVFR
     AFFGSLVYWA ELRLALRDPA SINCRYVGFH LQTSEIYLLA RAHSASPGYT KEELVAMEAI
     LTLATLMLEV ALQWVHVACA QLLSENDTIK AFRRVSASIP HALAPLGSIR LHDAEFEVLS
     NPDVMVARDE TALSQALFLG YFSVRTALTA CMRDYSHEAD GGSKETVTGV FLGVGLILQR
     LAGHLNFLLN CLAGAALYGG QKINIHSLTL PRYSLLADVM APMLQRQSLV DFWRARDNML
     EDLEITPRPG PPTQGKRVVV EMPLPSDDLP DMTPGASVNN GAGLGRMVDM AKQLQHYRET
     IIGEEATSSV GKRGLIRAGV GVAALRGRRR K