TEG5_HHV1F
ID TEG5_HHV1F Reviewed; 693 AA.
AC P08313;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
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 1 (strain F) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10304;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029433; DOI=10.1128/jvi.61.4.992-1001.1987;
RA McKnight J.L.C., Pellett P.E., Jenkins F.J., Roizman B.;
RT "Characterization and nucleotide sequence of two herpes simplex virus 1
RT genes whose products modulate alpha-trans-inducing factor-dependent
RT activation of alpha genes.";
RL J. Virol. 61:992-1001(1987).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=15795259; DOI=10.1128/jvi.79.8.4730-4743.2005;
RA Yedowitz J.C., Kotsakis A., Schlegel E.F., Blaho J.A.;
RT "Nuclear localizations of the herpes simplex virus type 1 tegument proteins
RT VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization
RT and VP22 nuclear import.";
RL J. Virol. 79:4730-4743(2005).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=F;
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA45767.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M15621; AAA45767.1; ALT_FRAME; Genomic_DNA.
DR PIR; A26133; TNBE70.
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; RNA-binding; Transcription;
KW Transcription regulation; Virion; Virion tegument.
FT CHAIN 1..693
FT /note="Tegument protein UL47"
FT /id="PRO_0000116074"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..75
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT MOTIF 63..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 647..670
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 73856 MW; D025B30372854E86 CRC64;
MSAREPAGRR RRASTRPRAS PVADEPAGDG VGFMGYLRAV FRGDDDSELE ALEEMAGDEP
PVRRRREGPR ARRRRASEAP PTSHRRASRQ RPGPDAARSQ SVRGRLDDDD EVPRGPPQAR
QGGYLGPVDA RAILGRVGGS RVAPSPLFLE ELQYEEDDYP EDVGPEDGGG ARSPPKVEVL
EGRVPGPELR AAFPLDRLAP QVAVWDESVR SALALGHPAG FYPCPDSAFG LSRVGVMHFA
SPDNPAVFFR QTLQQGEALA WYITGDGILD LTDRRTKTSP AQAMSFLADA VVRLAINGWV
CGTRLHAEAR GSDLDDRAAE LRRQFASLTA LRPVGAAAVP LLSAGGLVSP QSGPDAAVFR
SSLGSLLYWP GVRALLDRDC RVAARYAGRM TYLATGALLA RFNPDAVRCV LTREAAFLGR
VLDVLAVMAE QTVHWLSVVV GARLHPHVHH PAFADVAREE LFRALPLGSP AVVGAEHEAL
GDTAARRLLA NSGLNAVLGA AVYALHTALA TVTLKYARAC GDAHRRRDDA AATRRILAAG
LVLQRLLGFA DTVVACVTLA AFDGGFTAPE VGTYTPLRYA CVLRATQPLY ARTTPAKFWA
DVRAAAEHVD LRPASSAPRA PVSGTADPAF LLKDLEPFPP APVSGGSVLG PGVRVVDIMS
QFRKLLMGDE GAAALRAHVS GRRATGLGGP PRP
