ID   TRX1_EBVB9              Reviewed;         364 AA.
AC   P03187; Q777G2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-JUN-2021, entry version 73.
DE   RecName: Full=Triplex capsid protein 1 {ECO:0000255|HAMAP-Rule:MF_04018};
GN   Name=TRX1 {ECO:0000255|HAMAP-Rule:MF_04018}; ORFNames=BORF1;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
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}.
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DR   EMBL; V01555; CAA24840.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53404.1; -; Genomic_DNA.
DR   PIR; H93065; QQBE9.
DR   RefSeq; YP_401654.1; NC_007605.1.
DR   PDB; 6W19; EM; 5.50 A; 1/f/g/h/i/j=1-364.
DR   PDB; 6W2D; EM; 4.00 A; f/h=1-364.
DR   PDB; 6W2E; EM; 4.40 A; f/h=1-364.
DR   PDB; 7BQX; EM; 4.20 A; 5/e=1-364.
DR   PDB; 7BR7; EM; 4.30 A; 5/e=1-364.
DR   PDB; 7BR8; EM; 3.80 A; 5/e=1-364.
DR   PDB; 7BSI; EM; 4.10 A; 5/a/b/e/h=1-364.
DR   PDBsum; 6W19; -.
DR   PDBsum; 6W2D; -.
DR   PDBsum; 6W2E; -.
DR   PDBsum; 7BQX; -.
DR   PDBsum; 7BR7; -.
DR   PDBsum; 7BR8; -.
DR   PDBsum; 7BSI; -.
DR   SMR; P03187; -.
DR   PRIDE; P03187; -.
DR   DNASU; 3783724; -.
DR   GeneID; 3783724; -.
DR   KEGG; vg:3783724; -.
DR   Proteomes; UP000153037; Genome.
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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host nucleus; Reference proteome; Virion.
FT   CHAIN           1..364
FT                   /note="Triplex capsid protein 1"
FT                   /id="PRO_0000115723"
SQ   SEQUENCE   364 AA;  39191 MW;  6843A9A0A0CDD794 CRC64;
     MKVQGSVDRR RLQRRIAGLL PPPARRLNIS RGSEFTRDVR GLVEEHAQAS SLSAAAVWRA
     GLLAPGEVAV AGGGSGGGSF SWSGWRPPVF GDFLIHASSF NNAEATGTPL FQFKQSDPFS
     GVDAVFTPLS LFILMNHGRG VAARVEAGGG LTRMANLLYD SPATLADLVP DFGRLVADRR
     FHNFITPVGP LVENIKSTYL NKITTVVHGP VVSKAIPRST VKVTVPQEAF VDLDAWLSGG
     AGGGGGVCFV GGLGLQPCPA DARLYVALTY EEAGPRFTFF QSSRGHCQIM NILRIYYSPS
     IMHRYAVVQP LHIEELTFGA VACLGTFSAT DGWRRSAFNY RGSSLPVVEI DSFYSNVSDW
     EVIL