P16790 (VPAP_HCMVA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase processivity factor

Alternative name(s):
Polymerase accessory protein
Short name=PAP
Protein ICP36

Gene names

Name:

UL44

Organism

Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) [Complete proteome]

Taxonomic identifier

10360 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Betaherpesvirinae › Cytomegalovirus › Human cytomegalovirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA replication
Cellular component	Host nucleus Virion
Ligand	DNA-binding
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 433

433

DNA polymerase processivity factor

PRO_0000116070

Regions

Compositional bias

291 – 297

7

Poly-Gly

Compositional bias

325 – 337

13

Poly-Gly

Compositional bias

343 – 349

7

Poly-Gly

Compositional bias

356 – 360

5

Poly-Gly

Compositional bias

385 – 397

13

Poly-Gly

Experimental info

Mutagenesis

135

1

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

Secondary structure

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433

Helix Strand Turn

Details...

Beta strand

12 – 15

4

Helix

17 – 26

10

Helix

28 – 32

5

Beta strand

39 – 43

5

Turn

44 – 46

3

Beta strand

47 – 54

8

Beta strand

57 – 63

7

Helix

65 – 67

3

Beta strand

68 – 71

4

Beta strand

78 – 84

7

Turn

85 – 87

3

Helix

90 – 93

4

Beta strand

101 – 105

5

Beta strand

109 – 118

10

Beta strand

121 – 129

9

Beta strand

134 – 136

3

Beta strand

144 – 148

5

Helix

150 – 160

11

Beta strand

178 – 185

8

Turn

186 – 189

4

Beta strand

190 – 195

6

Beta strand

200 – 203

4

Turn

206 – 208

3

Beta strand

209 – 213

5

Beta strand

216 – 222

7

Helix

223 – 233

11

Helix

234 – 236

3

Beta strand

240 – 257

18

Beta strand

259 – 268

10

Sequences

	Sequence		Length	Mass (Da)
	P16790 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: E3BDF4C05E4C040A	FASTA	433	46,233
	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

References

	« Hide 'large scale' referencesShow '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 3:0-0(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.

PIR

QQBEV2. S09807.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T6L	X-ray	1.85	A	1-290	[»]
1YYP	X-ray	2.50	A	1-290	[»]

ProteinModelPortal

P16790.

SMR

P16790. Positions 10-270.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46029N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR004997. Herpes_PAP.
[Graphical view]

Pfam

PF03325. Herpes_PAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P16790.

Entry information

Entry name

VPAP_HCMVA

Accession

Primary (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 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program