ID   TRX2_ELHVK              Reviewed;         292 AA.
AC   Q18LE1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   23-FEB-2022, entry version 34.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019};
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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; AF322977; ABG36578.1; -; Genomic_DNA.
DR   SMR; Q18LE1; -.
DR   IntAct; Q18LE1; 1.
DR   MINT; Q18LE1; -.
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; Virion.
FT   CHAIN           1..292
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000408178"
SQ   SEQUENCE   292 AA;  32632 MW;  D95664497AF7A886 CRC64;
     MNEVKCVFET KLSPGDVAKL NKIVGAVVPV ARCTPLISPR DVGLHKHVSH RTDYGKLHMA
     LNMMYPTVFR KLEGNQMVMT PMQHGNIYTI RNTGPFSWEV GDRLAIIPPV FSVEHTTIMQ
     TPSWDLMLPI IVPVQVAKEI NIRNLVLTLM SLNRPGRDVE LSQEVRRIHF RDVTIDIPAT
     LDTRQLNSVR NVCLALALIT NVAPSLLQQY VPRLALAETD MLLVKCYDLL KKLDLPGDGN
     GGEPPNIPNE IQRMSGLLNL ITYVSSIVTE NSLFIVNDIT PDNKMATCTF TL