ID   TRX1_HHV2G              Reviewed;         466 AA.
AC   P22486;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Triplex capsid protein 1 {ECO:0000255|HAMAP-Rule:MF_04018};
GN   Name=TRX1 {ECO:0000255|HAMAP-Rule:MF_04018}; OrderedLocusNames=UL38;
OS   Human herpesvirus 2 (strain G) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10314;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2154597; DOI=10.1128/jvi.64.3.1124-1134.1990;
RA   Yei S., Chowdhury S.I., Bhat B.M., Conley A.J., Wold W.S., Batterson W.;
RT   "Identification and characterization of the herpes simplex virus type 2
RT   gene encoding the essential capsid protein ICP32/VP19c.";
RL   J. Virol. 64:1124-1134(1990).
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; M61774; AAA45844.1; -; Genomic_DNA.
DR   PIR; A34111; WMBEHT.
DR   PDB; 6M6G; EM; 5.39 A; S=1-466.
DR   PDB; 6M6H; EM; 4.50 A; T=1-466.
DR   PDB; 6M6I; EM; 4.05 A; K=1-466.
DR   PDBsum; 6M6G; -.
DR   PDBsum; 6M6H; -.
DR   PDBsum; 6M6I; -.
DR   SMR; P22486; -.
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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host nucleus; Virion.
FT   CHAIN           1..466
FT                   /note="Triplex capsid protein 1"
FT                   /id="PRO_0000115715"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  50469 MW;  230DF0C997666C10 CRC64;
     MKTKPLPTAP MAWAESAVET TTGPRELAGH APLRRVLRPP IARRDGPVLL GDRAPRRTAS
     TMWLLGIDPA ESSPGTRATR DDTEQAVDKI LRGARRAGGL TVPGAPRYHL TRQVTLTDLC
     QPNAERAGAL LLALRHPTDL PHLARHRAPP GRQTERLAEA WGQLLEASAL GSGRAESGCA
     RAGLVSFNFL VAACAAAYDA RDAAEAVRAH ITTNYGGTRA GARLDRFSEC LRAMVHTHVF
     PHEVMRFFGG LVSWVTQDEL ASVTAVCSGP QEATHTGHPG RPRSAVTIPA CAFVDLDAEL
     CLGGPGAAFL YLVFTYRQCR DQELCCVYVV KSQLPPRGLE AALERLFGRL RITNTIHGAE
     DMTPPPPNRN VDFPLAVLAA SSQSPRCSAS QVTNPQFVDR LYRWQPDLRG RPTARTCTYA
     AFAELGVMPD DSPRCLHRTE RFGAVGVPVV ILEGVVWRPG GWRACA