ID   TRX2_VZVD               Reviewed;         316 AA.
AC   P09291;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-DEC-2020, entry version 67.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=41;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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   -!- 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}. Host
CC       nucleus {ECO:0000255|HAMAP-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; X04370; CAA27924.1; -; Genomic_DNA.
DR   PIR; F27341; WZBE41.
DR   SMR; P09291; -.
DR   PRIDE; P09291; -.
DR   Proteomes; UP000002602; 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   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Reference proteome; Virion.
FT   CHAIN           1..316
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000115730"
SQ   SEQUENCE   316 AA;  34389 MW;  096BD7A66122442B CRC64;
     MAMPFEIEVL LPGELSPAET SALQKCEGKI ITFSTLRHRA SLVDIALSSY YINGAPPDTL
     SLLEAYRMRF AAVITRVIPG KLLAHAIGVG TPTPGLFIQN TSPVDLCNGD YICLLPPVFG
     SADSIRLDSV GLEIVFPLTI PQTLMREIIA KVVARAVERT AAGAQILPHE VLRGADVICY
     NGRRYELETN LQHRDGSDAA IRTLVLNLMF SINEGCLLLL ALIPTLLVQG AHDGYVNLLI
     QTANCVRETG QLINIPPMPR IQDGHRRFPI YETISSWIST SSRLGDTLGT RAILRVCVFD
     GPSTVHPGDR TAVIQV