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Protein

Protein P

Gene

P

Organism
Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979) (HBV-A)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery.UniRule annotation

Miscellaneous

Hepadnaviral virions contain probably just one P protein molecule per particle.UniRule annotation

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).UniRule annotation
Endonucleolytic cleavage to 5'-phosphomonoester.UniRule annotation

Enzyme regulationi

Activated by host HSP70 and HSP40 in vitro to be able to bind the epsilon loop of the pgRNA. Because deletion of the RNase H region renders the protein partly chaperone-independent, the chaperones may be needed indirectly to relieve occlusion of the RNA-binding site by this domain. Inhibited by several reverse-transcriptase inhibitors: Lamivudine, Adefovir and Entecavir.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei65Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNAUniRule annotation1
Metal bindingi431Magnesium; catalyticUniRule annotation1
Metal bindingi553Magnesium; catalyticUniRule annotation1
Metal bindingi554Magnesium; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, RNA-directed DNA polymerase, Transferase
Biological processDNA replication, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host RLR pathway by virus, Viral immunoevasion
LigandMagnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PUniRule annotation
Including the following 3 domains:
DNA-directed DNA polymeraseUniRule annotation (EC:2.7.7.7UniRule annotation)
RNA-directed DNA polymeraseUniRule annotation (EC:2.7.7.49UniRule annotation)
Ribonuclease HUniRule annotation (EC:3.1.26.4UniRule annotation)
Gene namesi
Name:PUniRule annotation
OrganismiHepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979) (HBV-A)
Taxonomic identifieri480116 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeOrthohepadnavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Proteomesi
  • UP000008766 Componenti: Genome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3833482

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002223331 – 845Protein PAdd BLAST845

Proteomic databases

PRIDEiP03159

Structurei

3D structure databases

ProteinModelPortaliP03159
SMRiP03159
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini359 – 602Reverse transcriptaseUniRule annotationAdd BLAST244

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 179Terminal protein domain (TP)UniRule annotationAdd BLAST179
Regioni180 – 348SpacerUniRule annotationAdd BLAST169
Regioni349 – 692Polymerase/reverse transcriptase domain (RT)UniRule annotationAdd BLAST344
Regioni693 – 845RnaseH domain (RH)Add BLAST153

Domaini

Terminal protein domain (TP) is hepadnavirus-specific. Spacer domain is highly variable and separates the TP and RT domains. Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain (RH) are similar to retrovirus reverse transcriptase/RNase H.UniRule annotation
The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template.UniRule annotation

Sequence similaritiesi

Belongs to the hepadnaviridae P protein family.UniRule annotation

Phylogenomic databases

OrthoDBiVOG0900002B

Family and domain databases

HAMAPiMF_04073 HBV_DPOL, 1 hit
InterProiView protein in InterPro
IPR001462 DNApol_viral_C
IPR000201 DNApol_viral_N
IPR037531 HBV_DPOL
IPR000477 RT_dom
PfamiView protein in Pfam
PF00336 DNA_pol_viral_C, 1 hit
PF00242 DNA_pol_viral_N, 1 hit
PF00078 RVT_1, 1 hit
PROSITEiView protein in PROSITE
PS50878 RT_POL, 1 hit

Sequencei

Sequence statusi: Complete.

P03159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLSYQHFRK LLLLDDGTEA GPLEEELPRL ADADLHRRVA EDLNLGNLNV
60 70 80 90 100
SIPWTHKVGN FTGLYSSTVP IFNPEWQTPS FPKIHLQEDI INRCQQFVGP
110 120 130 140 150
LTVNEKRRLK LIMPARFYPT HTKYLPLDKG IKPYYPDQVV NHYFQTRHYL
160 170 180 190 200
HTLWKAGILY KRETTRSASF CGSPYSWEQE LQHGRLVIKT SQRHGDESFC
210 220 230 240 250
SQSSGILSRS SVGPCIRSQL KQSRLGLQPR QGRLASSQPS RSGSIRAKAH
260 270 280 290 300
PSTRRYFGVE PSGSGHIDHS VNNSSSCLHQ SAVRKAAYSH LSTSKRQSSS
310 320 330 340 350
GHAVEFHCLP PNSAGSQSQG SVSSCWWLQF RNSKPCSEYC LSHLVNLRED
360 370 380 390 400
WGPCDEHGEH HIRIPRTPAR VTGGVFLVDK NPHNTAESRL VVDFSQFSRG
410 420 430 440 450
ISRVSWPKFA VPNLQSLTNL LSSNLSWLSL DVSAAFYHIP LHPAAMPHLL
460 470 480 490 500
IGSSGLSRYV ARLSSNSRIN NNQYGTMQNL HDSCSRQLYV SLMLLYKTYG
510 520 530 540 550
WKLHLYSHPI VLGFRKIPMG VGLSPFLLAQ FTSAICSVVR RAFPHCLAFS
560 570 580 590 600
YMDDVVLGAK SVQHRESLYT AVTNFLLSLG IHLNPNKTKR WGYSLNFMGY
610 620 630 640 650
IIGSWGTLPQ DHIVQKIKHC FRKLPVNRPI DWKVCQRIVG LLGFAAPFTQ
660 670 680 690 700
CGYPALMPLY ACIQAKQAFT FSPTYKAFLS KQYMNLYPVA RQRPGLCQVF
710 720 730 740 750
ADATPTGWGL AIGHQRMRGT FVAPLPIHTA ELLAACFARS RSGAKLIGTD
760 770 780 790 800
NSVVLSRKYT SFPWLLGCTA NWILRGTSFV YVPSALNPAD DPSRGRLGLS
810 820 830 840
RPLLRLPFQP TTGRTSLYAV SPSVPSHLPV RVHFASPLHV AWRPP
Length:845
Mass (Da):94,800
Last modified:July 21, 1986 - v1
Checksum:i68A09F4783463D98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02205 Genomic RNA No translation available.
X02763 Genomic DNA Translation: CAA26538.1
PIRiA94409 JDVLVD

Similar proteinsi

Entry informationi

Entry nameiDPOL_HBVA3
AccessioniPrimary (citable) accession number: P03159
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 18, 2018
This is version 86 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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