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P16790

- VPAP_HCMVA

UniProt

P16790 - VPAP_HCMVA

Protein

DNA polymerase processivity factor

Gene

UL44

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA polymerase processivity factor activity Source: InterPro

    GO - Biological processi

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

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase processivity factor
    Alternative name(s):
    Polymerase accessory protein
    Short name:
    PAP
    Protein ICP36
    Gene namesi
    Name:UL44
    OrganismiHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
    Taxonomic identifieri10360 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008991: Genome, UP000008992: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell
    2. virion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host nucleus, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351I → A: Complete loss of interaction with UL54. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433DNA polymerase processivity factorPRO_0000116070Add
    BLAST

    Interactioni

    Subunit structurei

    Forms homodimers. Interacts with host SMARCB1. Interacts with host NCL/nucleolin; this interaction is important for the organization of proteins within viral replication compartments. Interacts with UL112/UL113; this interaction is necessary for efficient viral DNA replication. Interacts with UL84. Interacts with the uracil DNA glycosylase UL114. Interacts with the DNA polymerase catalytic subunit UL54.6 Publications

    Protein-protein interaction databases

    DIPiDIP-46029N.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 154
    Helixi17 – 2610
    Helixi28 – 325
    Beta strandi39 – 435
    Turni44 – 463
    Beta strandi47 – 548
    Beta strandi57 – 637
    Helixi65 – 673
    Beta strandi68 – 714
    Beta strandi78 – 847
    Turni85 – 873
    Helixi90 – 934
    Beta strandi101 – 1055
    Beta strandi109 – 11810
    Beta strandi121 – 1299
    Beta strandi134 – 1363
    Beta strandi144 – 1485
    Helixi150 – 16011
    Beta strandi178 – 1858
    Turni186 – 1894
    Beta strandi190 – 1956
    Beta strandi200 – 2034
    Turni206 – 2083
    Beta strandi209 – 2135
    Beta strandi216 – 2227
    Helixi223 – 23311
    Helixi234 – 2363
    Beta strandi240 – 25718
    Beta strandi259 – 26810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T6LX-ray1.85A1-290[»]
    1YYPX-ray2.50A1-290[»]
    ProteinModelPortaliP16790.
    SMRiP16790. Positions 10-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16790.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi291 – 2977Poly-Gly
    Compositional biasi325 – 33713Poly-GlyAdd
    BLAST
    Compositional biasi343 – 3497Poly-Gly
    Compositional biasi356 – 3605Poly-Gly
    Compositional biasi385 – 39713Poly-GlyAdd
    BLAST

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR004997. Herpes_PAP.
    [Graphical view]
    PfamiPF03325. Herpes_PAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16790-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRKTRLSEP PTLALRLKPY KTAIQQLRSV IRALKENTTV TFLPTPSLIL    50
    QTVRSHCVSK ITFNSSCLYI TDKSFQPKTI NNSTPLLGNF MYLTSSKDLT 100
    KFYVQDISDL SAKISMCAPD FNMEFSSACV HGQDIVRESE NSAVHVDLDF 150
    GVVADLLKWI GPHTRVKRNV KKAPCPTGTV QILVHAGPPA IKFILTNGSE 200
    LEFTANNRVS FHGVKNMRIN VQLKNFYQTL LNCAVTKLPC TLRIVTEHDT 250
    LLYVASRNGL FAVENFLTEE PFQRGDPFDK NYVGNSGKSR GGGGGGGSLS 300
    SLANAGGLHD DGPGLDNDLM NEPMGLGGLG GGGGGGGKKH DRGGGGGSGT 350
    RKMSSGGGGG DHDHGLSSKE KYEQHKITSY LTSKGGSGGG GGGGGGGLDR 400
    NSGNYFNDAK EESDSEDSVT FEFVPNTKKQ KCG 433
    Length:433
    Mass (Da):46,233
    Last modified:August 1, 1990 - v1
    Checksum:iE3BDF4C05E4C040A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17403 Genomic DNA. Translation: CAA35403.1.
    BK000394 Genomic DNA. Translation: DAA00147.1.
    PIRiS09807. QQBEV2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17403 Genomic DNA. Translation: CAA35403.1 .
    BK000394 Genomic DNA. Translation: DAA00147.1 .
    PIRi S09807. QQBEV2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T6L X-ray 1.85 A 1-290 [» ]
    1YYP X-ray 2.50 A 1-290 [» ]
    ProteinModelPortali P16790.
    SMRi P16790. Positions 10-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46029N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P16790.

    Family and domain databases

    InterProi IPR004997. Herpes_PAP.
    [Graphical view ]
    Pfami PF03325. Herpes_PAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of cytomegalovirus late-gene expression: differential use of three start sites in the transcriptional activation of ICP36 gene expression."
      Leach F.S., Mocarski E.S.
      J. Virol. 63:1783-1791(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    2. "Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169."
      Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R., Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A., Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.
      Curr. Top. Microbiol. Immunol. 154:125-169(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The human cytomegalovirus genome revisited: comparison with the chimpanzee cytomegalovirus genome."
      Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., McGeoch D.J., Hayward G.S.
      J. Gen. Virol. 84:17-28(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
    4. "Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44."
      Loregian A., Appleton B.A., Hogle J.M., Coen D.M.
      J. Virol. 78:158-167(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL54, MUTAGENESIS OF ISO-135.
    5. Cited for: IDENTIFICATION.
    6. "Role of homodimerization of human cytomegalovirus DNA polymerase accessory protein UL44 in origin-dependent DNA replication in cells."
      Sinigalia E., Alvisi G., Mercorelli B., Coen D.M., Pari G.S., Jans D.A., Ripalti A., Palu G., Loregian A.
      J. Virol. 82:12574-12579(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION.
    7. "Characterization of human cytomegalovirus uracil DNA glycosylase (UL114) and its interaction with polymerase processivity factor (UL44)."
      Ranneberg-Nilsen T., Dale H.A., Luna L., Slettebakk R., Sundheim O., Rollag H., Bjoras M.
      J. Mol. Biol. 381:276-288(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL114.
    8. "Analysis of the association of the human cytomegalovirus DNA polymerase subunit UL44 with the viral DNA replication factor UL84."
      Strang B.L., Sinigalia E., Silva L.A., Coen D.M., Loregian A.
      J. Virol. 83:7581-7589(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL84.
    9. "Role of the specific interaction of UL112-113 p84 with UL44 DNA polymerase processivity factor in promoting DNA replication of human cytomegalovirus."
      Kim Y.E., Ahn J.H.
      J. Virol. 84:8409-8421(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL112/113, FUNCTION.
    10. "Host cell nucleolin is required to maintain the architecture of human cytomegalovirus replication compartments."
      Strang B.L., Boulant S., Kirchhausen T., Coen D.M.
      MBio 3:255-260(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST NCL.
    11. "The chromatin remodeling factor SMARCB1 forms a complex with human cytomegalovirus proteins UL114 and UL44."
      Ranneberg-Nilsen T., Rollag H., Slettebakk R., Backe P.H., Olsen O., Luna L., Bjoras M.
      PLoS ONE 7:E34119-E34119(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST SMARCB1.
    12. "The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer."
      Appleton B.A., Loregian A., Filman D.J., Coen D.M., Hogle J.M.
      Mol. Cell 15:233-244(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-290.

    Entry informationi

    Entry nameiVPAP_HCMVA
    AccessioniPrimary (citable) accession number: P16790
    Secondary accession number(s): Q7M6P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 69 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

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3