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Protein

Tripartite terminase subunit 1

Gene

TRM1

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.UniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri173 – 20129C3H1-typeUniRule annotationAdd
BLAST
Nucleotide bindingi619 – 6268ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Viral genome packaging, Virus exit from host cell

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite terminase subunit 1UniRule annotation
Gene namesi
Name:TRM1UniRule annotation
ORF Names:BALF3
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation1 Publication

  • Note: Found associated with the external surface of the viral capsid during assembly and DNA packaging, but seems absent in extracellular mature virions.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 685685Tripartite terminase subunit 1PRO_0000115889Add
BLAST

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Associates with TRM2 and TRM3 to form the tripartite terminase complex. Interacts with portal protein.UniRule annotation

Protein-protein interaction databases

IntActiP25939. 16 interactions.

Family & Domainsi

Sequence similaritiesi

Belongs to the herpesviridae TRM1 protein family.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri173 – 20129C3H1-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

HAMAPiMF_04014. HSV_TRM1.
InterProiIPR000501. UL28/UL56.
[Graphical view]
PfamiPF01366. PRTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLLAAAYS QVYALAVELS VCTRLDPRSL DVAAVVRNAG LLAELEAILL
60 70 80 90 100
PRLRRQNDRA CSALSLELVH LLENSREASA ALLAPGRKGT RVPPLRTPSV
110 120 130 140 150
AYSVEFYGGH KVDVSLCLIN DIEILMKRIN SVFYCMSHTM GLESLERALD
160 170 180 190 200
LLGRFRGVSP IPDPRLYITS VPCWRCVGEL MVLPNHGNPS TAEGTHVSCN
210 220 230 240 250
HLAVPVNPEP VSGLFENEVR QAGLGHLLEA EEKARPGGPE EGAVPGPGRP
260 270 280 290 300
EAEGATRALD TYNVFSTVPP EVAELSELLY WNSGGHAIGA TGQGEGGGHS
310 320 330 340 350
RLSALFARER RLALVRGACE EALAGARLTH LFDAVAPGAT ERLFCGGVYS
360 370 380 390 400
SSGDAVEALK ADCAAAFTAH PQYRAILQKR NELYTRLNRA MQRLGRGEEE
410 420 430 440 450
ASRESPEVPR PAGAREPGPS GALSDALKRK EQYLRQVATE GLAKLQSCLA
460 470 480 490 500
QQSETLTETL CLRVWGDVVY WELARMRNHF LYRRAFVSGP WEDRRAGEGA
510 520 530 540 550
AFENSKYIKT HLFTQTLSSE HLHALTHSLY TFITGPLAEE SGLFPPPSNV
560 570 580 590 600
ALARCCDAAG TLPHQKAFLT SLIWPGIEPS DWIETSFNSF YSVPGGSLAS
610 620 630 640 650
SQQILCRALR EAVLTVSLYN KTWGRSLILR RADAVSPGQA LPPDGLYLTY
660 670 680
DSDRPLILLY KGRGWVFKDL YALLYLHLQM RDDSA
Length:685
Mass (Da):74,764
Last modified:May 11, 2016 - v2
Checksum:i24F8371F54D16635
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24807.1.
AJ507799 Genomic DNA. Translation: CAD53465.1.
PIRiS33056.

Genome annotation databases

KEGGivg:3783679.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24807.1.
AJ507799 Genomic DNA. Translation: CAD53465.1.
PIRiS33056.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP25939. 16 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGivg:3783679.

Family and domain databases

HAMAPiMF_04014. HSV_TRM1.
InterProiIPR000501. UL28/UL56.
[Graphical view]
PfamiPF01366. PRTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Epstein-Barr virus BALF3 has nuclease activity and mediates mature virion production during the lytic cycle."
    Chiu S.H., Wu M.C., Wu C.C., Chen Y.C., Lin S.F., Hsu J.T., Yang C.S., Tsai C.H., Takada K., Chen M.R., Chen J.Y.
    J. Virol. 88:4962-4975(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTRM1_EBVB9
AccessioniPrimary (citable) accession number: P25939
Secondary accession number(s): Q777A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 11, 2016
Last modified: July 6, 2016
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.