Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA polymerase processivity factor

Gene

UL44

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed-Annotation score: 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]
ProteomesiUP000008992 Componenti: Genome UP000008991 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-SubCell
  2. virion Source: UniProtKB-SubCell
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 – 154Combined sources
Helixi17 – 2610Combined sources
Helixi28 – 325Combined sources
Beta strandi39 – 435Combined sources
Turni44 – 463Combined sources
Beta strandi47 – 548Combined sources
Beta strandi57 – 637Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 714Combined sources
Beta strandi78 – 847Combined sources
Turni85 – 873Combined sources
Helixi90 – 934Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi109 – 11810Combined sources
Beta strandi121 – 1299Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi144 – 1485Combined sources
Helixi150 – 16011Combined sources
Beta strandi178 – 1858Combined sources
Turni186 – 1894Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi200 – 2034Combined sources
Turni206 – 2083Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi216 – 2227Combined sources
Helixi223 – 23311Combined sources
Helixi234 – 2363Combined sources
Beta strandi240 – 25718Combined sources
Beta strandi259 – 26810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:July 31, 1990 - v1
Checksum:iE3BDF4C05E4C040A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17403 Genomic DNA. Translation: CAA35403.1.
BK000394 Genomic DNA. Translation: DAA00147.1.
PIRiS09807. QQBEV2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17403 Genomic DNA. Translation: CAA35403.1.
BK000394 Genomic DNA. Translation: DAA00147.1.
PIRiS09807. QQBEV2.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-46029N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP16790.

Family and domain databases

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

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(1988) [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(1989) [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(2002) [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(2003) [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(2007) [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(2007) [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(2008) [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(2009) [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(2011) [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(2011) [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(2003) [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: July 31, 1990
Last sequence update: July 31, 1990
Last modified: January 6, 2015
This is version 72 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

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 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.