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P16790

- VPAP_HCMVA

UniProt

P16790 - VPAP_HCMVA

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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

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
Complete GO annotation...

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-KW
  2. virion Source: UniProtKB-KW
Complete GO annotation...

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

        10         20         30         40         50
MDRKTRLSEP PTLALRLKPY KTAIQQLRSV IRALKENTTV TFLPTPSLIL
60 70 80 90 100
QTVRSHCVSK ITFNSSCLYI TDKSFQPKTI NNSTPLLGNF MYLTSSKDLT
110 120 130 140 150
KFYVQDISDL SAKISMCAPD FNMEFSSACV HGQDIVRESE NSAVHVDLDF
160 170 180 190 200
GVVADLLKWI GPHTRVKRNV KKAPCPTGTV QILVHAGPPA IKFILTNGSE
210 220 230 240 250
LEFTANNRVS FHGVKNMRIN VQLKNFYQTL LNCAVTKLPC TLRIVTEHDT
260 270 280 290 300
LLYVASRNGL FAVENFLTEE PFQRGDPFDK NYVGNSGKSR GGGGGGGSLS
310 320 330 340 350
SLANAGGLHD DGPGLDNDLM NEPMGLGGLG GGGGGGGKKH DRGGGGGSGT
360 370 380 390 400
RKMSSGGGGG DHDHGLSSKE KYEQHKITSY LTSKGGSGGG GGGGGGGLDR
410 420 430
NSGNYFNDAK EESDSEDSVT FEFVPNTKKQ KCG
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

« Hide 'large scale' publications
  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 29, 2014
This is version 70 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