TRX2_GAHVM
ID TRX2_GAHVM Reviewed; 319 AA.
AC Q9E6P9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 12-AUG-2020, entry version 60.
DE RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=MDV030;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14210.1; -; Genomic_DNA.
DR RefSeq; YP_001033946.1; NC_002229.3.
DR SMR; Q9E6P9; -.
DR GeneID; 4811491; -.
DR KEGG; vg:4811491; -.
DR Proteomes; UP000008072; 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 3: Inferred from homology;
KW Capsid protein; Host nucleus; Reference proteome; Virion.
FT CHAIN 1..319
FT /note="Triplex capsid protein 2"
FT /id="PRO_0000406533"
SQ SEQUENCE 319 AA; 34865 MW; 64F9AD7D992DB38B CRC64;
MSTSNGTIVE IELPCKLSTC DANLLQRCEG RVLFLPFVRA RVLLKDVDYK SFYIAGTEPD
TLSLLSTFKT RFAAVITRAL PGRMSAVVLG MGSIPNGLAL QNTGPFDLCN GDTVCLMPPI
FPNVCCRIRL ESIDTELLFP VTVPTRLANE ILAKTLSRAI EAIGRGQMPP PTSRESETIM
YNGRSYTISP TLHSLDAAES TVRTLLLNMI FAINEGNMIL YTMIPTLLTL GASDGYINAL
VGLETATRAV GQLIRIPNPP PLQDAWRRYP VYEALSAWIT MTLNLGNVLS LHPLLKVCTF
DGPANIKAGD LCPVIANWY