ID   TRX2_EBVB9              Reviewed;         301 AA.
AC   P25214; Q777C3;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   23-FEB-2022, entry version 75.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; ORFNames=BDLF1;
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).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA   Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA   Illanes D., Sarracino D., Kieff E.;
RT   "Proteins of purified Epstein-Barr virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=19158247; DOI=10.1128/jvi.01733-08;
RA   Henson B.W., Perkins E.M., Cothran J.E., Desai P.;
RT   "Self-assembly of Epstein-Barr virus capsids.";
RL   J. Virol. 83:3877-3890(2009).
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_04019,
CC       ECO:0000269|PubMed:19158247}.
CC   -!- SUBUNIT: Interacts with TRX1 and major capisd protein/MCP.
CC       {ECO:0000255|HAMAP-Rule:MF_04019}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04019,
CC       ECO:0000269|PubMed:15534216}. Host nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_04019}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRX2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04019}.
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DR   EMBL; V01555; CAA24837.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53446.1; -; Genomic_DNA.
DR   PIR; S33042; S33042.
DR   RefSeq; YP_401696.1; NC_007605.1.
DR   PDB; 6W19; EM; 5.50 A; 2/3/k/l/m/n/o/p/q/r/s/t=1-301.
DR   PDB; 6W2D; EM; 4.00 A; k/m/p/r=1-301.
DR   PDB; 6W2E; EM; 4.40 A; k/m/p/r=1-301.
DR   PDB; 7BQX; EM; 4.20 A; 6/7/f/g=1-301.
DR   PDB; 7BR7; EM; 4.30 A; 6/7/f/g=1-301.
DR   PDB; 7BR8; EM; 3.80 A; 6/7/f/g=1-301.
DR   PDB; 7BSI; EM; 4.10 A; 6/7/8/9/c/d/f/g/i/j=1-301.
DR   PDBsum; 6W19; -.
DR   PDBsum; 6W2D; -.
DR   PDBsum; 6W2E; -.
DR   PDBsum; 7BQX; -.
DR   PDBsum; 7BR7; -.
DR   PDBsum; 7BR8; -.
DR   PDBsum; 7BSI; -.
DR   SMR; P25214; -.
DR   IntAct; P25214; 1.
DR   MINT; P25214; -.
DR   DNASU; 3783692; -.
DR   GeneID; 3783692; -.
DR   KEGG; vg:3783692; -.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04019; HSV_TRX2; 1.
DR   InterPro; IPR002690; Herpes_capsid_2.
DR   Pfam; PF01802; Herpes_V23; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host nucleus; Reference proteome; Virion.
FT   CHAIN           1..301
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000115732"
SQ   SEQUENCE   301 AA;  33624 MW;  982B65730BF5D25C CRC64;
     MDLKVVVSLS SRLYTDEIAK MQQRIGCILP LASTHGTQNV QGLGLGQVYS LETVPDYVSM
     YNYLSDCTLA VLDEVSVDSL ILTKIVPGQT YAIKNKYQPF FQWHGTGSLS VMPPVFGREH
     ATVKLESNDV DIVFPMVLPT PIAEEVLQKI LLFNVYSRVV MQAPGNADML DVHMHLGSVS
     YLGHHYELAL PEVPGPLGLA LLDNLSLYFC IMVTLLPRAS MRLVRGLIRH EHHDLLNLFQ
     EMVPDEIARI DLDDLSVADD LSRMRVMMTY LQSLASLFNL GPRLATAAYS QETLTATCWL
     R