ID   TRX2_HHV8P              Reviewed;         305 AA.
AC   F5HGN8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   29-SEP-2021, entry version 31.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=ORF26;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
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; AF148805; ABD28877.1; -; Genomic_DNA.
DR   RefSeq; YP_001129379.1; NC_009333.1.
DR   PDB; 6PPB; EM; 4.30 A; 6/7/c/d=1-305.
DR   PDBsum; 6PPB; -.
DR   SMR; F5HGN8; -.
DR   BioGRID; 1777012; 3.
DR   PRIDE; F5HGN8; -.
DR   DNASU; 4961509; -.
DR   GeneID; 4961509; -.
DR   KEGG; vg:4961509; -.
DR   Proteomes; UP000000942; 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..305
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000423883"
SQ   SEQUENCE   305 AA;  34373 MW;  5C5D9E83C24902BD CRC64;
     MALDKSIVVN FTSRLFADEL AALQSKIGSV LPLGDCHRLQ NIQALGLGCV CSRETSPDYI
     QIMQYLSKCT LAVLEEVRPD SLRLTRMDPS DNLQIKNVYA PFFQWDSNTQ LAVLPPFFSR
     KDSTIVLESN GFDLVFPMVV PQQLGHAILQ QLLVYHIYSK ISAGAPDDVN MAELDLYTTN
     VSFMGRTYRL DVDNTDPRTA LRVLDDLSMY LCILSALVPR GCLRLLTALV RHDRHPLTEV
     FEGVVPDEVT RIDLDQLSVP DDITRMRVMF SYLQSLSSIF NLGPRLHVYA YSAETLAASC
     WYSPR