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Protein

DNA polymerase processivity factor

Gene

UL42

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein UL9 loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB

GO - Biological processi

  • bidirectional double-stranded viral DNA replication Source: UniProtKB
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):
DNA-binding protein UL42
Polymerase accessory protein
Short name:
PAP
Gene namesi
ORF Names:UL42
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]
Proteomesi
  • UP000009294 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488DNA polymerase processivity factorPRO_0000116061Add
BLAST

Interactioni

Subunit structurei

Interacts with the DNA polymerase catalytic subunit UL30. Interacts with the origin-binding protein.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NFKB1P198384EBI-1029310,EBI-300010From a different organism.
RELAQ042066EBI-1029310,EBI-73886From a different organism.
UL30P042932EBI-1029310,EBI-8615017
UL9P101933EBI-1029310,EBI-8596799

Protein-protein interaction databases

BioGridi971437. 1 interaction.
IntActiP10226. 6 interactions.
MINTiMINT-6732523.

Structurei

Secondary structure

1
488
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 366Combined sources
Helixi37 – 4711Combined sources
Helixi48 – 503Combined sources
Turni51 – 544Combined sources
Beta strandi58 – 625Combined sources
Beta strandi65 – 728Combined sources
Beta strandi75 – 828Combined sources
Helixi83 – 853Combined sources
Beta strandi86 – 905Combined sources
Beta strandi96 – 1038Combined sources
Turni114 – 1163Combined sources
Beta strandi120 – 12910Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi175 – 1806Combined sources
Helixi182 – 19110Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi218 – 2225Combined sources
Helixi228 – 2336Combined sources
Helixi248 – 2514Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi265 – 2717Combined sources
Helixi274 – 2807Combined sources
Beta strandi285 – 2917Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi298 – 30710Combined sources
Beta strandi310 – 3156Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMLX-ray2.70A/C/E/G1-319[»]
ProteinModelPortaliP10226.
SMRiP10226. Positions 28-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10226.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi394 – 41320Bipartite nuclear localization signalAdd
BLAST

Sequence similaritiesi

Family and domain databases

InterProiIPR003202. UL42.
[Graphical view]
PfamiPF02282. Herpes_UL42. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDSPGGVAP ASPVEDASDA SLGQPEEGAP CQVVLQGAEL NGILQAFAPL
60 70 80 90 100
RTSLLDSLLV MGDRGILIHN TIFGEQVFLP LEHSQFSRYR WRGPTAAFLS
110 120 130 140 150
LVDQKRSLLS VFRANQYPDL RRVELAITGQ APFRTLVQRI WTTTSDGEAV
160 170 180 190 200
ELASETLMKR ELTSFVVLVP QGTPDVQLRL TRPQLTKVLN ATGADSATPT
210 220 230 240 250
TFELGVNGKF SVFTTSTCVT FAAREEGVSS STSTQVQILS NALTKAGQAA
260 270 280 290 300
ANAKTVYGEN THRTFSVVVD DCSMRAVLRR LQVGGGTLKF FLTTPVPSLC
310 320 330 340 350
VTATGPNAVS AVFLLKPQKI CLDWLGHSQG SPSAGSSASR ASGSEPTDSQ
360 370 380 390 400
DSASDAVSHG DPEDLDGAAR AGEAGALHAC PMPSSTTRVT PTTKRGRSGG
410 420 430 440 450
EDARADTALK KPKTGSPTAP PPADPVPLDT EDDSDAADGT AARPAAPDAR
460 470 480
SGSRYACYFR DLPTGEASPG AFSAFRGGPQ TPYGFGFP
Length:488
Mass (Da):51,159
Last modified:July 1, 1989 - v1
Checksum:i432974563DF0A81B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti349 – 3491S → N in strain: Nonneuroinvasive mutant HF10.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32305.1.
M19121 Genomic DNA. Translation: AAA45824.1.
DQ889502 Genomic DNA. Translation: ABI63504.1.
FJ593289 Genomic DNA. Translation: ACM62265.1.
PIRiD29890. WMBE42.
RefSeqiYP_009137117.1. NC_001806.2.

Genome annotation databases

GeneIDi24271471.
KEGGivg:24271471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32305.1.
M19121 Genomic DNA. Translation: AAA45824.1.
DQ889502 Genomic DNA. Translation: ABI63504.1.
FJ593289 Genomic DNA. Translation: ACM62265.1.
PIRiD29890. WMBE42.
RefSeqiYP_009137117.1. NC_001806.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMLX-ray2.70A/C/E/G1-319[»]
ProteinModelPortaliP10226.
SMRiP10226. Positions 28-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971437. 1 interaction.
IntActiP10226. 6 interactions.
MINTiMINT-6732523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24271471.
KEGGivg:24271471.

Miscellaneous databases

EvolutionaryTraceiP10226.

Family and domain databases

InterProiIPR003202. UL42.
[Graphical view]
PfamiPF02282. Herpes_UL42. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity."
    Gottlieb J., Marcy A.I., Coen D.M., Challberg M.D.
    J. Virol. 64:5976-5987(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UL30.
  6. "The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA."
    Trego K.S., Zhu Y., Parris D.S.
    Nucleic Acids Res. 33:536-545(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UL9.
  7. "Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal."
    Alvisi G., Avanzi S., Musiani D., Camozzi D., Leoni V., Ly-Huynh J.D., Ripalti A.
    Biochemistry 47:13764-13777(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR LOCALIZATION SIGNAL.
  8. "The extended left-handed helix: a simple nucleic acid-binding motif."
    Hicks J.M., Hsu V.L.
    Proteins 55:330-338(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-319.

Entry informationi

Entry nameiPAP_HHV11
AccessioniPrimary (citable) accession number: P10226
Secondary accession number(s): B9VQH0, Q09I91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 16, 2016
This is version 88 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, Reference proteome

Documents

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

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 one 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.