TRX2_EHV1B
ID TRX2_EHV1B Reviewed; 314 AA.
AC P28921;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 23-FEB-2022, entry version 76.
DE RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=43;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
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; AY665713; AAT67301.1; -; Genomic_DNA.
DR PIR; I36799; WZBED7.
DR RefSeq; YP_053089.1; NC_001491.2.
DR SMR; P28921; -.
DR PRIDE; P28921; -.
DR GeneID; 1487527; -.
DR KEGG; vg:1487527; -.
DR Proteomes; UP000001189; 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..314
FT /note="Triplex capsid protein 2"
FT /id="PRO_0000115726"
SQ SEQUENCE 314 AA; 33842 MW; BE2A56D4871ED3E6 CRC64;
MASAAFEIDI LLPSDLSPAD LSALQKCEGK LVFLTALRRR VMLSSVTLSS YYVNGAPPDT
LSLMAAFRRR FPAIIQRVLP NKMIAAALGV APLPPGAFIQ NTGPFDLCNG DSVCALPPIL
DVEDKLRLGS VGEEILFPLT VPLAQARELI ARLVARAVQA LTPNAQAQRG AEVMFYNGRK
YNVTPDLRHR DAVNGVARSL VLNMIFAMNE GSLVLLSLIP NLLTLGTQDG FVNAIIQMGS
ATREVGQLVH QQPVPQPQDG ARRFCVYDAL MSWISVASRL GDVVGGKPLV RICTFEGQAT
ISRGEKAPVI QTLL