ID   TRX2_EHV2               Reviewed;         300 AA.
AC   Q66629;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-DEC-2020, entry version 52.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=26;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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; U20824; AAC13813.1; -; Genomic_DNA.
DR   PIR; S55620; S55620.
DR   RefSeq; NP_042622.1; NC_001650.2.
DR   SMR; Q66629; -.
DR   GeneID; 1461081; -.
DR   KEGG; vg:1461081; -.
DR   Proteomes; UP000007083; 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..300
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000406074"
SQ   SEQUENCE   300 AA;  33418 MW;  0056525A5A7B4DCB CRC64;
     MQVDSRIVVT LTSRLYADEI SKLQERVGSV VPLKDSHRLQ NLNSVGMYSV YMRNVAPDFV
     AMFSYLSEAT LAILDEVTPD TLVFSRLDHS QNYELKNVYY PSFAWHSHTL LTVVPPVFGR
     EAATVALESN GFEIVFPVVM PHALAQAVLQ KLMLYNIYAR LSDANVGDVN MDHVRFHATT
     LHHMGRAYTL HIDQANPGGM LGLLDNLAIY LAIISALLPN SLARLLPAIM RHEQHELLNI
     FAGVAPPDDG GDFNIEDDMQ KMESFMAYMQ SVSSIFNLGP KLRLGQYSSE TQSGTAWLAS