ID   TRX2_HHV6Z              Reviewed;         296 AA.
AC   Q9QJ27;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-JUN-2021, entry version 49.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=U56;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(1999).
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; AF157706; AAD49659.1; -; Genomic_DNA.
DR   RefSeq; NP_050237.1; NC_000898.1.
DR   PDB; 6Q1F; EM; 9.00 A; 6/7/W/X/Y/Z/a/b/c/d=1-296.
DR   PDBsum; 6Q1F; -.
DR   SMR; Q9QJ27; -.
DR   PRIDE; Q9QJ27; -.
DR   DNASU; 1497058; -.
DR   GeneID; 1497058; -.
DR   KEGG; vg:1497058; -.
DR   Proteomes; UP000006930; 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..296
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000408448"
SQ   SEQUENCE   296 AA;  33474 MW;  F4E4CB2CD4401740 CRC64;
     METVYCTFDH KLSLSDISTL CKLMNIVIPI PAHHHLIGSG NLGLYPIVSS NKDYVHIRNV
     LRTMVVTILQ KVEGNQLVLR KPMTGQQYAI KNTGPFPWEK GDTLTLIPPL STHSEEKLLK
     LGDWELTVPL VVPTAIAAEI NIRLLCIGLI AVHREYNEMQ TIIDELCSIQ YRDVLIKLPD
     IVNDKQSMYS MKTACISLSM ITAMAPDIVR TYIDRLTLED HSMLLIKCQE LLSKRTTLST
     QRCGQLHATD IKDELKKIKS VLTMIDQINS LTNEKTYFVV CDVSADNRMA TCIYKN