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P16790 (VPAP_HCMVA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase processivity factor
Alternative name(s):
Polymerase accessory protein
Short name=PAP
Protein ICP36
Gene names
Name:UL44
OrganismHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) [Complete proteome]
Taxonomic identifier10360 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization. Ref.11

Subunit structure

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. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Virion. Host nucleus.

Sequence similarities

Belongs to the herpesviridae polymerase accessory protein family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentHost nucleus
Virion
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

virion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA polymerase processivity factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433DNA polymerase processivity factor
PRO_0000116070

Regions

Compositional bias291 – 2977Poly-Gly
Compositional bias325 – 33713Poly-Gly
Compositional bias343 – 3497Poly-Gly
Compositional bias356 – 3605Poly-Gly
Compositional bias385 – 39713Poly-Gly

Experimental info

Mutagenesis1351I → A: Complete loss of interaction with UL54. Ref.5

Secondary structure

.................................................. 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16790 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: E3BDF4C05E4C040A

FASTA43346,233
        10         20         30         40         50         60 
MDRKTRLSEP PTLALRLKPY KTAIQQLRSV IRALKENTTV TFLPTPSLIL QTVRSHCVSK 

        70         80         90        100        110        120 
ITFNSSCLYI TDKSFQPKTI NNSTPLLGNF MYLTSSKDLT KFYVQDISDL SAKISMCAPD 

       130        140        150        160        170        180 
FNMEFSSACV HGQDIVRESE NSAVHVDLDF GVVADLLKWI GPHTRVKRNV KKAPCPTGTV 

       190        200        210        220        230        240 
QILVHAGPPA IKFILTNGSE LEFTANNRVS FHGVKNMRIN VQLKNFYQTL LNCAVTKLPC 

       250        260        270        280        290        300 
TLRIVTEHDT LLYVASRNGL FAVENFLTEE PFQRGDPFDK NYVGNSGKSR GGGGGGGSLS 

       310        320        330        340        350        360 
SLANAGGLHD DGPGLDNDLM NEPMGLGGLG GGGGGGGKKH DRGGGGGSGT RKMSSGGGGG 

       370        380        390        400        410        420 
DHDHGLSSKE KYEQHKITSY LTSKGGSGGG GGGGGGGLDR NSGNYFNDAK EESDSEDSVT 

       430 
FEFVPNTKKQ KCG 

« Hide

References

« Hide 'large scale' references
[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]Erratum
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., McGeoch D.J., Hayward G.S.
J. Gen. Virol. 84:1053-1053(2003)
[5]"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.
[6]"Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome."
Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J., Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W., Shenk T., Smith R.D., Nelson J.A.
J. Virol. 78:10960-10966(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]Erratum
Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J., Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W., Shenk T., Smith R.D., Nelson J.A.
J. Virol. 78:13395-13395(2004)
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17403 Genomic DNA. Translation: CAA35403.1.
BK000394 Genomic DNA. Translation: DAA00147.1.
PIRQQBEV2. S09807.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T6LX-ray1.85A1-290[»]
1YYPX-ray2.50A1-290[»]
ProteinModelPortalP16790.
SMRP16790. Positions 10-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46029N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004997. Herpes_PAP.
[Graphical view]
PfamPF03325. Herpes_PAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16790.

Entry information

Entry nameVPAP_HCMVA
AccessionPrimary (citable) accession number: P16790
Secondary accession number(s): Q7M6P1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references