ID   TRX2_HHV2H              Reviewed;         318 AA.
AC   P89441;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=UL18;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z86099; CAB06742.1; -; Genomic_DNA.
DR   RefSeq; YP_009137169.1; NC_001798.2.
DR   PDB; 5ZZ8; EM; 3.75 A; 2/3/R/S/U/V/X/Y/x/y=1-318.
DR   PDB; 6M6G; EM; 5.39 A; K/O=1-318.
DR   PDB; 6M6H; EM; 4.50 A; R/S=1-318.
DR   PDBsum; 5ZZ8; -.
DR   PDBsum; 6M6G; -.
DR   PDBsum; 6M6H; -.
DR   SMR; P89441; -.
DR   PRIDE; P89441; -.
DR   DNASU; 1487301; -.
DR   GeneID; 1487301; -.
DR   KEGG; vg:1487301; -.
DR   Proteomes; UP000001874; 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..318
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000406184"
SQ   SEQUENCE   318 AA;  34344 MW;  76F6A8EB1D0495ED CRC64;
     MITDCFEADI AIPSGISRPD AAALQRCEGR VVFLPTIRRQ LALADVAHES FVSGGVSPDT
     LGLLLAYRRR FPAVITRVLP TRIVACPVDL GLTHAGTVNL RNTSPVDLCN GDPVSLVPPV
     FEGQATDVRL ESLDLTLRFP VPLPTPLARE IVARLVARGI RDLNPDPRTP GELPDLNVLY
     YNGARLSLVA DVQQLASVNT ELRSLVLNMV YSITEGTTLI LTLIPRLLAL SAQDGYVNAL
     LQMQSVTREA AQLIHPEAPM LMQDGERRLP LYEALVAWLA HAGQLGDILA LAPAVRVCTF
     DGAAVVQSGD MAPVIRYP