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P10192

- HEPA_HHV11

UniProt

P10192 - HEPA_HHV11

Protein

DNA helicase/primase complex-associated protein

Gene

UL8

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW
    2. viral genome replication Source: InterPro

    Keywords - Biological processi

    DNA replication

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA helicase/primase complex-associated protein
    Short name:
    HEPA
    Alternative name(s):
    Primase-associated factor
    Gene namesi
    ORF Names:UL8
    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]
    ProteomesiUP000009294: Genome

    Subcellular locationi

    Host nucleus By similarity

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 750750DNA helicase/primase complex-associated proteinPRO_0000115856Add
    BLAST

    Interactioni

    Subunit structurei

    Associates with the helicase-primase complex composed of the primase, the helicase and the primase-associated factor. Interacts with origin-binding protein. Interacts with the polymerase catalytic subunit.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UL30P042934EBI-7185538,EBI-8615017

    Protein-protein interaction databases

    BioGridi971456. 1 interaction.
    DIPiDIP-1097N.
    IntActiP10192. 2 interactions.
    MINTiMINT-6732582.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi337 – 3437Poly-Ala

    Sequence similaritiesi

    Belongs to the herpesviridae HEPA family.Curated

    Family and domain databases

    InterProiIPR004996. DNA_helic/primase-assoc_herpes.
    [Graphical view]
    PfamiPF03324. Herpes_HEPA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10192-1 [UniParc]FASTAAdd to Basket

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    MDTADIVWVE ESVSAITLYA VWLPPRAREY FHALVYFVCR NAAGEGRARF    50
    AEVSVTATEL RDFYGSADVS VQAVVAAARA ATTPAASPLE PLENPTLWRA 100
    LYACVLAALE RQTGPVALFA PLRIGSDPRT GLVVKVERAS WGPPAAPRAA 150
    LLVAEANIDI DPMALAARVA EHPDARLAWA RLAAIRDTPQ CASAASLTVN 200
    ITTGTALFAR EYQTLAFPPI KKEGAFGDLV EVCEVGLRPR GHPQRVTARV 250
    LLPRDYDYFV SAGEKFSAPA LVALFRQWHT TVHAAPGALA PVFAFLGPEF 300
    EVRGGPVPYF AVLGFPGWPT FTVPATAESA RDLVRGAAAA YAALLGAWPA 350
    VGARVVLPPR AWPGVASAAA GCLLPAVREA VARWHPATKI IQLLDPPAAV 400
    GPVWTARFCF PGLRAQLLAA LADLGGSGLA DPHGRTGLAR LDALVVAAPS 450
    EPWAGAVLER LVPDTCNACP ALRQLLGGVM AAVCLQIEET ASSVKFAVCG 500
    GDGGAFWGVF NVDPQDADAA SGVIEDARRA IETAVGAVLR ANAVRLRHPL 550
    CLALEGVYTH AVAWSQAGVW FWNSRDNTDH LGGFPLRGPA YTTAAGVVRD 600
    TLRRVLGLTT ACVPEEDALT ARGLMEDACD RLILDAFNKR LDAEYWSVRV 650
    SPFEASDPLP PTAFRGGALL DAEHYWRRVV RVCPGGGESV GVPVDLYPRP 700
    LVLPPVDCAH HLREILREIE LVFTGVLAGV WGEGGKFVYP FDDKMSFLFA 750
    Length:750
    Mass (Da):79,926
    Last modified:July 1, 1989 - v1
    Checksum:iECA9ABD0E85CB392
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti247 – 2471T → M in strain: Nonneuroinvasive mutant HF10.
    Natural varianti330 – 3301A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti353 – 3531A → V in strain: Nonneuroinvasive mutant HF10.
    Natural varianti467 – 4671N → D in strain: Nonneuroinvasive mutant HF10.
    Natural varianti471 – 4711A → V in strain: Nonneuroinvasive mutant HF10.
    Natural varianti543 – 5442AV → GL in strain: Nonneuroinvasive mutant HF10 and 17 syn+.
    Natural varianti612 – 6121C → G in strain: Nonneuroinvasive mutant HF10.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32344.1.
    M19120 Genomic DNA. Translation: AAA45823.1.
    DQ889502 Genomic DNA. Translation: ABI63470.1.
    FJ593289 Genomic DNA. Translation: ACM62230.1.
    PIRiC29890. WMBEX8.
    RefSeqiNP_044609.1. NC_001806.1.

    Genome annotation databases

    GeneIDi2703432.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32344.1 .
    M19120 Genomic DNA. Translation: AAA45823.1 .
    DQ889502 Genomic DNA. Translation: ABI63470.1 .
    FJ593289 Genomic DNA. Translation: ACM62230.1 .
    PIRi C29890. WMBEX8.
    RefSeqi NP_044609.1. NC_001806.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 971456. 1 interaction.
    DIPi DIP-1097N.
    IntActi P10192. 2 interactions.
    MINTi MINT-6732582.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703432.

    Family and domain databases

    InterProi IPR004996. DNA_helic/primase-assoc_herpes.
    [Graphical view ]
    Pfami PF03324. Herpes_HEPA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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 [LARGE SCALE GENOMIC DNA].
    2. "Structures of herpes simplex virus type 1 genes required for replication of virus DNA."
      McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P., Challberg M.D.
      J. Virol. 62:444-453(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
      Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
      Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Nonneuroinvasive mutant HF10.
    4. "Herpes simplex virus type 1 bacterial artificial chromosome."
      Cunningham C., Davison A.J.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 17 syn+.
    5. "The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein."
      McLean G.W., Abbotts A.P., Parry M.E., Marsden H.S., Stow N.D.
      J. Gen. Virol. 75:2699-2706(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL9, FUNCTION.
    6. "The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex."
      Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K., Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D.
      J. Virol. 71:6390-6397(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL30, FUNCTION.

    Entry informationi

    Entry nameiHEPA_HHV11
    AccessioniPrimary (citable) accession number: P10192
    Secondary accession number(s): B9VQD5, Q09IC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 62 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

    External Data

    Dasty 3