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Protein

Triplex capsid protein 1

Gene

TRX1

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.UniRule annotation5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Triplex capsid protein 1UniRule annotation
Gene namesi
Name:TRX1UniRule annotation
Ordered Locus Names:UL38
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009294 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation
  • Host nucleus UniRule annotation

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • viral capsid Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Triplex capsid protein 1PRO_0000436379Add
BLAST

Interactioni

Subunit structurei

Interacts with TRX2, MCP and capsid vertex component 2/CVC2.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi971404. 3 interactions.
DIPiDIP-2193N.

Family & Domainsi

Sequence similaritiesi

Belongs to the herpesviridae TRX1 protein family.UniRule annotation

Family and domain databases

HAMAPiMF_04018. HSV_TRX1.
InterProiIPR004999. Herpes_VP19C.
[Graphical view]
PfamiPF03327. Herpes_VP19C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTNPLPATP SVWGGSTVEL PPTTRDTAGQ GLLRRVLRPP ISRRDGPGLP
60 70 80 90 100
RGSGPRRAAS TLWLLGLDGT DAPPGALTPN DDTEQALDKI LRGTMRGGAA
110 120 130 140 150
LIGSPRHHLT RQVILTDLCQ PNADRAGTLL LALRHPADLP HLAHQRAPPG
160 170 180 190 200
RQTERLGEAW GQLMEATALG SGRAESGCTR AGLVSFNFLV AACAASYDAR
210 220 230 240 250
DAADAVRAHV TANYRGTRVG ARLDRFSECL RAMVHTHVFP HEVMRFFGGL
260 270 280 290 300
VSWVTQDELA SVTAVCAGPQ EAAHTGHPGR PRSAVILPAC AFVDLDAELG
310 320 330 340 350
LGGPGAAFLY LVFTYRQRRD QELCCVYVIK SQLPPRGLEP ALERLFGRLR
360 370 380 390 400
ITNTIHGTED MTPPAPNRNP DFPLAGLAAN PQTPRCSAGQ VTNPQFADRL
410 420 430 440 450
YRWQPDLRGR PTARTCTYAA FAELGMMPED SPRCLHRTER FGAVSVPVVI
460
LEGVVWRPGE WRACA
Length:465
Mass (Da):50,263
Last modified:October 1, 1993 - v1
Checksum:i5F00147AE29B3092
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32313.1.
PIRiB30088. WMBEZ8.
RefSeqiYP_009137113.1. NC_001806.2.

Genome annotation databases

GeneIDi2703359.
KEGGivg:2703359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32313.1.
PIRiB30088. WMBEZ8.
RefSeqiYP_009137113.1. NC_001806.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971404. 3 interactions.
DIPiDIP-2193N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703359.
KEGGivg:2703359.

Family and domain databases

HAMAPiMF_04018. HSV_TRX1.
InterProiIPR004999. Herpes_VP19C.
[Graphical view]
PfamiPF03327. Herpes_VP19C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
    McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
    J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of the genes encoding two capsid proteins of herpes simplex virus type 1 by direct amino acid sequencing."
    Rixon F.J., Davison M.D., Davison A.J.
    J. Gen. Virol. 71:1211-1214(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly."
    Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., Homa F.L., Thomsen D.R., Steven A.C.
    J. Mol. Biol. 263:447-462(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particles."
    Saad A., Zhou Z.H., Jakana J., Chiu W., Rixon F.J.
    J. Virol. 73:6821-6830(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: location of UL25 product in the capsid and demonstration that it binds DNA."
    Ogasawara M., Suzutani T., Yoshida I., Azuma M.
    J. Virol. 75:1427-1436(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CVC2.
  6. "Functional analysis of the triplex proteins (VP19C and VP23) of herpes simplex virus type 1."
    Okoye M.E., Sexton G.L., Huang E., McCaffery J.M., Desai P.
    J. Virol. 80:929-940(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Mutational analysis of the herpes simplex virus triplex protein VP19C."
    Adamson W.E., McNab D., Preston V.G., Rixon F.J.
    J. Virol. 80:1537-1548(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1."
    Davison M.D., Rixon F.J., Davison A.J.
    J. Gen. Virol. 73:2709-2713(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-16.

Entry informationi

Entry nameiTRX1_HHV11
AccessioniPrimary (citable) accession number: P32888
Secondary accession number(s): P10222
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.