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Protein

Tripartite terminase subunit 1

Gene

TRM1

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri197 – 22529C3H1-typeUniRule annotationAdd
BLAST
Nucleotide bindingi696 – 7038ATPUniRule 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
Ordered Locus Names:UL28
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

  • 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 – 785785Tripartite terminase subunit 1PRO_0000115874Add
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 annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRM2P102176EBI-7032948,EBI-7033000
TRM3P042958EBI-7032948,EBI-7032965

Protein-protein interaction databases

BioGridi971470. 1 interaction.
IntActiP10212. 3 interactions.
MINTiMINT-6732646.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi465 – 4684Poly-Gly

Sequence similaritiesi

Belongs to the herpesviridae TRM1 protein family.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri197 – 22529C3H1-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P10212-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPVSEPTV ARQKLLALLG QVQTYVFQIE LLRRCDPHIG RGKLPQLKLN
60 70 80 90 100
ALQVRALRRR LRPGLEAQAG AFLTPLSVTL ELLLEYAWRE GERLLGSLET
110 120 130 140 150
FATAGDVAAF FTETMGLARP CPYHQRVRLD TYGGTVHMEL CFLHDVENFL
160 170 180 190 200
KQLNYCHLIT PSRGATAALE RVREFMVGAV GSGLIVPPEL SDPSHPCAVC
210 220 230 240 250
FEELCVTANQ GATIARRLAD RICNHVTQQA QVRLDANELR RYLPHAAGLS
260 270 280 290 300
DADRARALSV LDHALARTAG GDGQPHPSPE NDSVRKEADA LLEAHDVFQA
310 320 330 340 350
TTPGLYAISE LRFWLASGDR AGQTTMDAFA SNLTALARRE LQQETAAVAV
360 370 380 390 400
ELALFGRRAE HFDRAFGSHL AALDMVDALI IGGQATSPDD QIEALIRACY
410 420 430 440 450
DHHLTTPLLR RLVSPEQCDE EALRRVLARM GAGGAADAPK GGAGPDDDGD
460 470 480 490 500
RVAVEEGARG LGAPGGGGED EDRRRGPGGQ GPETWGDIAT QAAADVRERR
510 520 530 540 550
RLYADRLTKR SLASLGRCVR EQRGELEKML RVSVHGEVLP ATFAAVANGF
560 570 580 590 600
AARARFCALT AGAGTVIDNR SAPGVFDAHR FMRASLLRHQ VDPALLPSIT
610 620 630 640 650
HRFFELVNGP LFDHSTHSFA QPPNTALYYS VENVGLLPHL KEELARFIMG
660 670 680 690 700
AGGSGADWAV SEFQRFYCFD GISGITPTQR AAWRYIRELI IATTLFASVY
710 720 730 740 750
RCGELELRRP DCSRPTSEGR YRYPPGVYLT YDSDCPLVAI VESAPDGCIG
760 770 780
PRSVVVYDRD VFSILYSVLQ HLAPRLPDGG HDGPP
Length:785
Mass (Da):85,578
Last modified:July 1, 1989 - v1
Checksum:iCFE8868BAA86F616
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32321.1.
PIRiA30085. WMBEW8.
RefSeqiYP_009137103.1. NC_001806.2.

Genome annotation databases

GeneIDi2703457.
KEGGivg:2703457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32321.1.
PIRiA30085. WMBEW8.
RefSeqiYP_009137103.1. NC_001806.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971470. 1 interaction.
IntActiP10212. 3 interactions.
MINTiMINT-6732646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703457.
KEGGivg:2703457.

Family and domain databases

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

Entry informationi

Entry nameiTRM1_HHV11
AccessioniPrimary (citable) accession number: P10212
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 7, 2016
This is version 77 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, 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.