ID   TRX1_HHV14              Reviewed;         465 AA.
AC   P17586; P10222;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-DEC-2020, entry version 55.
DE   RecName: Full=Triplex capsid protein 1 {ECO:0000255|HAMAP-Rule:MF_04018};
GN   Name=TRX1 {ECO:0000255|HAMAP-Rule:MF_04018}; OrderedLocusNames=UL38;
OS   Human herpesvirus 1 (strain A44) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10300;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2539510; DOI=10.1128/jvi.63.5.2169-2179.1989;
RA   Pertuiset B., Boccara M., Cebrian J., Berthelot N., Chousterman S.,
RA   Puvion-Dutilleul F., Sisman J., Sheldrick P.;
RT   "Physical mapping and nucleotide sequence of a herpes simplex virus type 1
RT   gene required for capsid assembly.";
RL   J. Virol. 63:2169-2179(1989).
CC   -!- FUNCTION: Structural component of the T=16 icosahedral capsid. The
CC       capsid is composed of pentamers and hexamers of major capsid
CC       protein/MCP, which are linked together by heterotrimers called
CC       triplexes. These triplexes are formed by a single molecule of triplex
CC       protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally,
CC       TRX1 is required for efficient transport of TRX2 to the nucleus, which
CC       is the site of capsid assembly. {ECO:0000255|HAMAP-Rule:MF_04018}.
CC   -!- SUBUNIT: Interacts with TRX2, MCP and capsid vertex component 2/CVC2.
CC       {ECO:0000255|HAMAP-Rule:MF_04018}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04018}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04018}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRX1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04018}.
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; M22962; AAA45769.1; -; Genomic_DNA.
DR   PIR; A31478; WMBE44.
DR   SMR; P17586; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04018; HSV_TRX1; 1.
DR   InterPro; IPR004999; Herpes_1.
DR   Pfam; PF03327; Herpes_VP19C; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Virion.
FT   CHAIN           1..465
FT                   /note="Triplex capsid protein 1"
FT                   /id="PRO_0000115713"
SQ   SEQUENCE   465 AA;  50232 MW;  30240B9C5D592EE7 CRC64;
     MKTNPLPATP SVWGGSTVEL PPTTRDTAGQ GLLRRVLRPP ISRRDGPVLP RGSGPRRAAS
     TLWLLGLDGT DAPPGALTPN DDTEQALDKI LRGTMRGGAA LIGSPRHHLT RQVILTDLCQ
     PNADRAGTLL LALRHPADLP HLAHQRAPPG RQTERLGEAW GQLMEATALG SGRAESGCTR
     AGLVSFNFLV AACAASYDAR DAADAVRAHV TANYRGTRVG ARLDRFSECL RAMVHTHVFP
     HEVMRFFGGL VSWVTQDELA SVTAVCAGPQ EAAHTGHPGR PRSAVILPAC AFVDLDAELG
     LGGPGAAFLY LVLTYRQRRD QELCCVYVIK SQLPPRGLEP ALERLFGRLR ITNTIHGTED
     MTPPAPNRNP DFPLAGLAAN PQTPRCSAGQ VTNPQFADRL YRWQPDLRGR PTARTCTYAA
     FAELGMMPED SPRCLHRTER FGAVTVPVVI LEGVVWCPGE WRACA