P10226 (PAP_HHV11) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase processivity factor

Alternative name(s):
DNA-binding protein UL42
Polymerase accessory protein
Short name=PAP

Gene names

ORF Names:

UL42

Organism

Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)

Taxonomic identifier

10299 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5
Subunit structure	Interacts with the DNA polymerase catalytic subunit UL30. Interacts with the origin-binding protein. Ref.5 Ref.6
Subcellular location	Host nucleus.
Sequence similarities	Belongs to the herpesviridae DNA polymerase processivity factor family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Host nucleus
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 488

488

DNA polymerase processivity factor

PRO_0000116061

Regions

Motif

394 – 413

20

Bipartite nuclear localization signal

Natural variations

Natural variant

349

1

S → N in strain: Nonneuroinvasive mutant HF10.

Secondary structure

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488

Helix Strand Turn

Details...

Beta strand

31 – 36

6

Helix

37 – 47

11

Helix

48 – 50

3

Turn

51 – 54

4

Beta strand

58 – 62

5

Beta strand

65 – 72

8

Beta strand

75 – 82

8

Helix

83 – 85

3

Beta strand

86 – 90

5

Beta strand

96 – 103

8

Turn

114 – 116

3

Beta strand

120 – 129

10

Beta strand

135 – 142

8

Beta strand

150 – 153

4

Beta strand

156 – 160

5

Beta strand

166 – 169

4

Beta strand

175 – 180

6

Helix

182 – 191

10

Beta strand

200 – 204

5

Beta strand

208 – 213

6

Beta strand

218 – 222

5

Beta strand

257 – 260

4

Beta strand

265 – 271

7

Helix

274 – 280

7

Beta strand

285 – 291

7

Beta strand

293 – 296

4

Beta strand

298 – 307

10

Beta strand

310 – 315

6

Sequences

	Sequence		Length	Mass (Da)
	P10226 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 432974563DF0A81B	FASTA	488	51,159
	10 20 30 40 50 60 MTDSPGGVAP ASPVEDASDA SLGQPEEGAP CQVVLQGAEL NGILQAFAPL RTSLLDSLLV 70 80 90 100 110 120 MGDRGILIHN TIFGEQVFLP LEHSQFSRYR WRGPTAAFLS LVDQKRSLLS VFRANQYPDL 130 140 150 160 170 180 RRVELAITGQ APFRTLVQRI WTTTSDGEAV ELASETLMKR ELTSFVVLVP QGTPDVQLRL 190 200 210 220 230 240 TRPQLTKVLN ATGADSATPT TFELGVNGKF SVFTTSTCVT FAAREEGVSS STSTQVQILS 250 260 270 280 290 300 NALTKAGQAA ANAKTVYGEN THRTFSVVVD DCSMRAVLRR LQVGGGTLKF FLTTPVPSLC 310 320 330 340 350 360 VTATGPNAVS AVFLLKPQKI CLDWLGHSQG SPSAGSSASR ASGSEPTDSQ DSASDAVSHG 370 380 390 400 410 420 DPEDLDGAAR AGEAGALHAC PMPSSTTRVT PTTKRGRSGG EDARADTALK KPKTGSPTAP 430 440 450 460 470 480 PPADPVPLDT EDDSDAADGT AARPAAPDAR SGSRYACYFR DLPTGEASPG AFSAFRGGPQ TPYGFGFP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2839594] [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: 2826807] [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: 17218138] [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: 2173776] [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: 15673714] [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: 19053255] [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: 15048824] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-319.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14112 Genomic DNA. Translation: CAA32305.1.
M19121 Genomic DNA. Translation: AAA45824.1.
DQ889502 Genomic DNA. Translation: ABI63504.1.
FJ593289 Genomic DNA. Translation: ACM62265.1.

PIR

WMBE42. D29890.

RefSeq

NP_044644.1. NC_001806.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DML	X-ray	2.70	A/C/E/G	1-319	[»]

ProteinModelPortal

P10226.

SMR

P10226. Positions 28-319.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10226. 1 interaction.

MINT

MINT-6732523.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2703407.

Phylogenomic databases

ProtClustDB

CLSP2509598.

Family and domain databases

InterPro

IPR003202. UL42.
[Graphical view]

Pfam

PF02282. Herpes_UL42. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PAP_HHV11

Accession

Primary (citable) accession number: P10226
Secondary accession number(s): B9VQH0, Q09I91

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	September 21, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program