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Protein

DNA polymerase processivity factor

Gene

UL44

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed-Annotation score: Annotation score: 4 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

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):
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

Complete GO annotation...

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.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 15Combined sources4
Helixi17 – 26Combined sources10
Helixi28 – 32Combined sources5
Beta strandi39 – 43Combined sources5
Turni44 – 46Combined sources3
Beta strandi47 – 54Combined sources8
Beta strandi57 – 63Combined sources7
Helixi65 – 67Combined sources3
Beta strandi68 – 71Combined sources4
Beta strandi78 – 84Combined sources7
Turni85 – 87Combined sources3
Helixi90 – 93Combined sources4
Beta strandi101 – 105Combined sources5
Beta strandi109 – 118Combined sources10
Beta strandi121 – 129Combined sources9
Beta strandi134 – 136Combined sources3
Beta strandi144 – 148Combined sources5
Helixi150 – 160Combined sources11
Beta strandi178 – 185Combined sources8
Turni186 – 189Combined sources4
Beta strandi190 – 195Combined sources6
Beta strandi200 – 203Combined sources4
Turni206 – 208Combined sources3
Beta strandi209 – 213Combined sources5
Beta strandi216 – 222Combined sources7
Helixi223 – 233Combined sources11
Helixi234 – 236Combined sources3
Beta strandi240 – 257Combined sources18
Beta strandi259 – 268Combined sources10

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[»]
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

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: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.

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[»]
ProteinModelPortaliP16790.
SMRiP16790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46029N.

Proteomic databases

PRIDEiP16790.

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...

Entry informationi

Entry nameiVPAP_HCMVA
AccessioniPrimary (citable) accession number: P16790
Secondary accession number(s): Q7M6P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 78 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

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.