TRX2_SHV21
ID TRX2_SHV21 Reviewed; 304 AA.
AC Q01008;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 02-DEC-2020, entry version 62.
DE RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=26;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(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; X64346; CAA45649.1; -; Genomic_DNA.
DR RefSeq; NP_040228.1; NC_001350.1.
DR SMR; Q01008; -.
DR PRIDE; Q01008; -.
DR GeneID; 1682465; -.
DR KEGG; vg:1682465; -.
DR Proteomes; UP000000587; 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..304
FT /note="Triplex capsid protein 2"
FT /id="PRO_0000115731"
SQ SEQUENCE 304 AA; 34357 MW; 329CAF8F1A6572A3 CRC64;
MLTDKTIIVS LTSRLFADEI TKLQKKIGSI LPLQDPHKLQ SLDTLGLNAV CSRDVFPDYV
HMFSYLSKCT LAILEEVNPD NLILTRLDPS ETYQIKNVYE PMFQWDGFSN LTVIPPVFGR
QQATVTLESN GFDLVFPSVV PSDLAQAIIG KLLLYNLYSR LVESDPEINI EEVNMYTTNV
THMGRHYVLD INHNNPNEAL KSLDDLAVYT CILSALIPRA CLRVLTILMR HDQHELLDVF
RGIVPREVYE IDANALSIGD DITRMTTFIT YLQSLSSIFN LGAKLHLSSY ASETQTATCW
ISYC