Q1PD04 · Q1PD04_HBV

Function

function

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.

Miscellaneous

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

Catalytic activity

Activity regulation

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.

Features

Showing features for site, binding site.

Type
IDPosition(s)Description
Site63Priming of reverse-transcription by covalently linking the first nucleotide of the -DNA
Binding site429Mg2+ (UniProtKB | ChEBI); catalytic
Binding site551Mg2+ (UniProtKB | ChEBI); catalytic
Binding site552Mg2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Molecular FunctionDNA binding
Molecular FunctionDNA-directed DNA polymerase activity
Molecular Functionmetal ion binding
Molecular FunctionRNA-directed DNA polymerase activity
Molecular FunctionRNA-DNA hybrid ribonuclease activity
Biological ProcessDNA replication
Biological Processsymbiont-mediated suppression of host innate immune response
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein P

Including 3 domains:

  • Recommended name
    DNA-directed DNA polymerase
  • EC number
  • Recommended name
    RNA-directed DNA polymerase
  • EC number
  • Recommended name
    Ribonuclease H
  • EC number

Gene names

    • Name
      P
    • ORF names
      HBVgp1

Organism names

Accessions

  • Primary accession
    Q1PD04

Proteomes

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-177Terminal protein domain (TP)
Region178-346Spacer
Compositional bias219-238Polar residues
Region219-269Disordered
Region297-316Disordered
Region347-690Polymerase/reverse transcriptase domain (RT)
Domain357-600Reverse transcriptase

Domain

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.
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.

Sequence similarities

Belongs to the hepadnaviridae P protein family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    843
  • Mass (Da)
    94,397
  • Last updated
    2006-05-16 v1
  • MD5 Checksum
    066C3A6A2A72C4E8CD2297F3FB51A1E2
MPLSYQHFRKLLLLDEEAGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPCFNPKWQTPSFPDIHLQEDIVDRCKQFVGPLTVNENRRLKLIMPARFYPNVTKYLPLDKGIKPYYPEYVVNHYFQTRHYLHTLWKAGILYKRESTRSASFCGSPYSWEQDLQHGRLVFQTSKRHGDKSFCPQSPGILPRSSVGPCIQSQLRKSRLGPQPAQGQLAGRQQGGSGSIRARVHPSPWGTVGVEPSGSGPTHNCASSSSSCLHQSAVRKAAYSLISTSKGHSSSGHAVELHHFPPNSSRSQSQGPVLSCWWLQFRNSEPCSEYCLCHIVNLIEDWGPCTEHGEHRIRTPRTPARVTGGVFLVDKNPHNTTESRLVVDFSQFSRGNTRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHLPLHPAAMPHLLVGSSGLSRYVARLSSNSRIINNQHRTMQNLHNSCSRNLYVSLMLLYKTYGRKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHLESLYAAVTNFLLSLGIHLNPHKTKRWGYSLNFMGYVIGSWGTLPQEHIVQKIKMCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACIQAKQAFTFSPTYKAFLSKQYLNLYPVARQRPGLCQVFADATPTGWGLAIGHQRMRGTFVSPLPIHTAELLAACFARSRSGAKLIGTDNSVVLSRKYTSFPWLLGCAANWILRGTSFVYVPSALNPADDPSRGRLGLYRPLLRLLYRPTTGRTSLYADSPSVPSHLPDRVHFASPLHVAWRPP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias219-238Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ448621
EMBL· GenBank· DDBJ
ABE03781.1
EMBL· GenBank· DDBJ
Genomic DNA
GQ205440
EMBL· GenBank· DDBJ
ACS74742.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815620
EMBL· GenBank· DDBJ
ADF06088.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815621
EMBL· GenBank· DDBJ
ADF06095.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815626
EMBL· GenBank· DDBJ
ADF06129.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815632
EMBL· GenBank· DDBJ
ADF06169.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815633
EMBL· GenBank· DDBJ
ADF06176.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815646
EMBL· GenBank· DDBJ
ADF06263.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815647
EMBL· GenBank· DDBJ
ADF06269.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815649
EMBL· GenBank· DDBJ
ADF06283.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815652
EMBL· GenBank· DDBJ
ADF06304.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815653
EMBL· GenBank· DDBJ
ADF06311.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815659
EMBL· GenBank· DDBJ
ADF06351.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815660
EMBL· GenBank· DDBJ
ADF06358.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815664
EMBL· GenBank· DDBJ
ADF06386.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815665
EMBL· GenBank· DDBJ
ADF06393.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815666
EMBL· GenBank· DDBJ
ADF06400.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815668
EMBL· GenBank· DDBJ
ADF06414.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815669
EMBL· GenBank· DDBJ
ADF06421.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815674
EMBL· GenBank· DDBJ
ADF06452.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815675
EMBL· GenBank· DDBJ
ADF06459.1
EMBL· GenBank· DDBJ
Genomic DNA
GU815676
EMBL· GenBank· DDBJ
ADF06466.1
EMBL· GenBank· DDBJ
Genomic DNA
JQ688405
EMBL· GenBank· DDBJ
AFY98983.1
EMBL· GenBank· DDBJ
Genomic DNA
KC510647
EMBL· GenBank· DDBJ
AGL51171.1
EMBL· GenBank· DDBJ
Genomic DNA
KJ173365
EMBL· GenBank· DDBJ
AHV89969.1
EMBL· GenBank· DDBJ
Genomic DNA
KP341008
EMBL· GenBank· DDBJ
AJP07110.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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