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: -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

GO - Biological processi

  • bidirectional double-stranded viral DNA replication Source: UniProtKB
  • DNA replication Source: UniProtKB-KW

Keywordsi

Molecular functionDNA-binding
Biological processDNA replication

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]
Proteomesi
  • UP000008992 Componenti: Genome
  • UP000008991 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi135I → A: Complete loss of interaction with UL54. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001160701 – 433DNA polymerase processivity factorAdd BLAST433

Proteomic databases

PRIDEiP16790

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
ELMiP16790
IntActiP16790, 1 interactor

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP16790
SMRiP16790
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16790

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi291 – 297Poly-Gly7
Compositional biasi325 – 337Poly-GlyAdd BLAST13
Compositional biasi343 – 349Poly-Gly7
Compositional biasi356 – 360Poly-Gly5
Compositional biasi385 – 397Poly-GlyAdd BLAST13

Sequence similaritiesi

Phylogenomic databases

OrthoDBiVOG090000FA

Family and domain databases

InterProiView protein in InterPro
IPR004997 Herpes_PAP
PfamiView protein in Pfam
PF03325 Herpes_PAP, 1 hit

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:August 1, 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

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T6LX-ray1.85A1-290[»]
1YYPX-ray2.50A1-290[»]
5IWDX-ray2.56A1-290[»]
5IXAX-ray2.68A/B1-290[»]
ProteinModelPortaliP16790
SMRiP16790
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46029N
ELMiP16790
IntActiP16790, 1 interactor

Proteomic databases

PRIDEiP16790

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090000FA

Miscellaneous databases

EvolutionaryTraceiP16790

Family and domain databases

InterProiView protein in InterPro
IPR004997 Herpes_PAP
PfamiView protein in Pfam
PF03325 Herpes_PAP, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiVPAP_HCMVA
AccessioniPrimary (citable) accession number: P16790
Secondary accession number(s): Q7M6P1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 25, 2017
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again