ID   TRX1_EHV1V              Reviewed;         465 AA.
AC   Q6S6P9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 42.
DE   RecName: Full=Triplex capsid protein 1 {ECO:0000255|HAMAP-Rule:MF_04018};
GN   Name=TRX1 {ECO:0000255|HAMAP-Rule:MF_04018}; OrderedLocusNames=22;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAS45906.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45906.1; -; Genomic_DNA.
DR   SMR; Q6S6P9; -.
DR   PRIDE; Q6S6P9; -.
DR   Proteomes; UP000008296; 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   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Virion.
FT   CHAIN           1..465
FT                   /note="Triplex capsid protein 1"
FT                   /id="PRO_0000115718"
SQ   SEQUENCE   465 AA;  51317 MW;  393A2B557423BA33 CRC64;
     MNLGGNRFVQ IGNGMSNIMY TDANGAVRWE QISPPAGFPQ QQRGRGRGHV AFGLPNTLDW
     LPGFVQATPN SITISNMGGI QISSAGVITA AINSEQNSWM LSSFNPSLKL TRQVTLTDFC
     DPTAERPGLP IIRLRHHLDA IGSSPSSTPP GRNPQELDEA WAALSELSVS GRSDTTGLRP
     SLLSLTFLVA SRSGEYSDKA AAEAVRAHVL ANYRDRRTEQ RLDRFGEYLQ AMVRTHVFPH
     KHMTVFGGLI SHVIQDKLAS LTAVAGGVQE GARTNNSAVP RSSVYVPACA FLDVDHELKL
     GDASAKFVYL IFVYSQRLRR EGVRVYVAVS KFDEVAFEDA VSFLFHKART ESAIRGTEGA
     DAPEPHPNAA LPLQELSSSR CEPRCPPSRL NNREFTNALY QWAPDLRGRP NRTSCMYAAY
     IRLGAIASDP PRTTRRSERF GSVDMPVVWL ENVRWDPQDW VECSY